eF-site ID 3hmj-ABCGHI PDB Code 3hmj Chain A, B, C, G, H, I Title Saccharomyces cerevisiae FAS type I Classification TRANSFERASE Compound Fatty acid synthase subunit alpha Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (FAS1_YEAST) Sequence A:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPIADEPVKASLLLHVLVAHKLKKSLDS IPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETP LEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKA FLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLARYL KMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGV ATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDR EVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNIT YSEEPREKVRKLSQYVQEMALGGPITKESQMDVEDALDKD STKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGD WKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSI GAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAK GSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAI IPFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKK QKSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSLET LFNRWHSESWANQLTVCGAIIGWTRGTNNIIAEGIEKMGV RTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFV PELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSA DAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLL DLERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEGCVEM AWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDVKAKY ETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEP FEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATL YIPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITL FVLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGSGMGG VSALRGMFKDRFKDEPVQNDILQESFINTMSAWVNMLLIS SSGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYD DFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTR NGFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDK IGRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRKRQLV TREAQIKDWVENELEALKLEAEEIPSEDQNEFLLERTREI HNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTI DDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVI GVFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADN VDKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQKGGQA IVVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFHNGMI YNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTF NSKNIQSKDSYINTIETAKMIENMTKEKVSNGVGVDVELI TSINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWSAK EAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAVELHGNAK KAAEEAGVTDVKVSISHDDLQAVAVAVSTK B:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPIADEPVKASLLLHVLVAHKLKKSLDS IPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETP LEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKA FLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLARYL KMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGV ATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDR EVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNIT YSEEPREKVRKLSQYVQEMALGGPITKESQMDVEDALDKD STKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGD WKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSI GAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAK GSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAI IPFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKK QKSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSLET LFNRWHSESWANQLTVCGAIIGWTRGTNNIIAEGIEKMGV RTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFV PELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSA DAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLL DLERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEGCVEM AWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDVKAKY ETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEP FEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATL YIPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITL FVLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGSGMGG VSALRGMFKDRFKDEPVQNDILQESFINTMSAWVNMLLIS SSGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYD DFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTR NGFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDK IGRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRKRQLV TREAQIKDWVENELEALKLEAEEIPSEDQNEFLLERTREI HNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTI DDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVI GVFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADN VDKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQKGGQA IVVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFHNGMI YNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTF NSKNIQSKDSYINTIETAKMIENMTKEKVSNGVGVDVELI TSINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWSAK EAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAVELHGNAK KAAEEAGVTDVKVSISHDDLQAVAVAVSTK C:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPIADEPVKASLLLHVLVAHKLKKSLDS IPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETP LEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKA FLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLARYL KMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGV ATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDR EVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNIT YSEEPREKVRKLSQYVQEMALGGPITKESQMDVEDALDKD STKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGD WKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSI GAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAK GSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAI IPFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKK QKSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSLET LFNRWHSESWANQLTVCGAIIGWTRGTNNIIAEGIEKMGV RTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFV PELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSA DAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLL DLERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEGCVEM AWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDVKAKY ETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEP FEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATL YIPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITL FVLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGSGMGG VSALRGMFKDRFKDEPVQNDILQESFINTMSAWVNMLLIS SSGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYD DFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTR NGFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDK IGRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRKRQLV TREAQIKDWVENELEALKLEAEEIPSEDQNEFLLERTREI HNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTI DDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVI GVFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADN VDKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQKGGQA IVVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFHNGMI YNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTF NSKNIQSKDSYINTIETAKMIENMTKEKVSNGVGVDVELI TSINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWSAK EAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAVELHGNAK KAAEEAGVTDVKVSISHDDLQAVAVAVSTK G:  STRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEP TEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVL NLCLTEFENCYLEGNDIHALAAKLLQENDTTLVKTKELIK NYITARIMAKRPFDKKSNSALFRAVGEGNAQLVAIFGGQG NTDDYFEELRDLYQTYHVLVGDLIKFSAETLSELIRTTLD AEKVFTQGLNILEWLENPSNTPDKDYLLSIPISCPLIGVI QLAHYVVTAKLLGFTPGELRSYLKGATGHSQGLVTAVAIA ETDSWESFFVSVRKAITVLFFIGVRCYEAYPNTSLPPSIL EDSLENNEGVPSPMLSISNLTQEQVQDYVNKTNSHLPAGK QVEISLVNGAKNLVVSGPPQSLYGLNLTLRKAKAPSGLDQ SRIPFSERKLKFSNRFLPVASPFHSHLLVPASDLINKDLV KNNVSFNAKDIQIPVYDTFDGSDLRVLSGSISERIVDCII RLPVKWETTTQFKATHILDFGPGGASGLGVLTHRNKDGTG VRVIVAGTLDINPDDDYGFKQEIFDVTSNGLKKNPNWLEE YHPKLIKNKSGKIFVETKFSKLIGRPPLLVPGMTPCTVSP DFVAATTNAGYTIELAGGGYFSAAGMTAAIDSVVSQIEKG STFGINLIYVNPFMLQWGIPLIKELRSKGYPIQFLTIGAG VPSLEVASEYIETLGLKYLGLKPGSIDAISQVINIAKAHP NFPIALQWTGGRGGGHHSFEDAHTPMLQMYSKIRRHPNIM LIFGSGFGSADDTYPYLTGEWSTKFDYPPMPFDGFLFGSR VMIAKEVKTSPDAKKCIAACTGVPDDKWEQTYKKPTGGIV TVRSEMGEPIHKIATRGVMLWKEFDETIFNLPKNKLVPTL EAKRDYIISRLNADFQKPWFATVNGQARDLATMTYEEVAK RLVELMFIRSTNSWFDVTWRTFTGDFLRRVEERFTKSKTL SLIQSYSLLDKPDEAIEKVFNAYPAAREQFLNAQDIDHFL SMCQNPMQKPVPFVPVLDRRFEIFFKKDSLWQSEHLEAVV DQDVQRTCILHGPVAAQFTKVIDEPIKSIMDGIHDGHIKK LLHQYYGDDESKIPAVEYFGGESPVDSAVFKATSSTDEES WFKALAGSEINWRHASFLCSFITQDKMFVSNPIRKVFKPS QGMVVEISNGNTSSKTVVTLSEPVQGELKPTVILKLLKEN IIQMEMIENRTMDGKPVSLPLLYNFNPDNGFAPISEVMED RNQRIKEMYWKLWIDEPFNLDFDPRDVIKGKDFEITAKEV YDFTHAVGNNCEDFVSRPDRTMLAPMDFAIVVGWRAIIKA IFPNTVDGDLLKLVHLSNGYKMIPGAKPLQVGDVVSTTAV IESVVNQPTGKIVDVVGTLSRNGKPVMEVTSSFFYRGNYT DFENTFQKTVEPVYQMHIKTSKDIAVLRSKEWFQLDDEDF DLLNKTLTFETETEVTFKNANIFSSVKCFGPIKVELPTKE TVEIGIVDYEAGASHGNPVVDFLKRNGSTLEQKVNLENPI PIAVLDSYTPSTNEPYARVSGDLNPIHVSRHFASYANLPG TITHGMFSSASVRALIENWAADSVSSRVRGYTCQFVDMVL PNTALKTSIQHVGMINGRKLIKFETRNEDDVVVLTGEAEI EQPVTTFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNH FKDTYGFSILDIVINNPVNLTIHFGGEKGKRIRENYSAMI FETIVDGKLKTEKIFKEINEHSTSYTFRSEKGLLSATQFT QPALTLMEKAAFEDLKSKGLIPADATFAGHSLGEYAALAS LADVMSIESLVEVVFYRGMTMQVAVPRDELGRSNYGMIAI NPGRVAASFSQEALQYVVERVGKRTGWLVEIVNYNVENQQ YVAAGDLRALDTVTNVLNFIKLQKIDIIELQKSLSLEEVE GHLFEIIDEASKKSAVKPRPLKLERGFACIPLVGISVPFH STYLMNGVKPFKSFLKKNIIKENVKVARLAGKYIPNLTAK PFQVTKEYFQDVYDLTGSEPIKEIIDNWEKYEQ H:  STRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEP TEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVL NLCLTEFENCYLEGNDIHALAAKLLQENDTTLVKTKELIK NYITARIMAKRPFDKKSNSALFRAVGEGNAQLVAIFGGQG NTDDYFEELRDLYQTYHVLVGDLIKFSAETLSELIRTTLD AEKVFTQGLNILEWLENPSNTPDKDYLLSIPISCPLIGVI QLAHYVVTAKLLGFTPGELRSYLKGATGHSQGLVTAVAIA ETDSWESFFVSVRKAITVLFFIGVRCYEAYPNTSLPPSIL EDSLENNEGVPSPMLSISNLTQEQVQDYVNKTNSHLPAGK QVEISLVNGAKNLVVSGPPQSLYGLNLTLRKAKAPSGLDQ SRIPFSERKLKFSNRFLPVASPFHSHLLVPASDLINKDLV KNNVSFNAKDIQIPVYDTFDGSDLRVLSGSISERIVDCII RLPVKWETTTQFKATHILDFGPGGASGLGVLTHRNKDGTG VRVIVAGTLDINPDDDYGFKQEIFDVTSNGLKKNPNWLEE YHPKLIKNKSGKIFVETKFSKLIGRPPLLVPGMTPCTVSP DFVAATTNAGYTIELAGGGYFSAAGMTAAIDSVVSQIEKG STFGINLIYVNPFMLQWGIPLIKELRSKGYPIQFLTIGAG VPSLEVASEYIETLGLKYLGLKPGSIDAISQVINIAKAHP NFPIALQWTGGRGGGHHSFEDAHTPMLQMYSKIRRHPNIM LIFGSGFGSADDTYPYLTGEWSTKFDYPPMPFDGFLFGSR VMIAKEVKTSPDAKKCIAACTGVPDDKWEQTYKKPTGGIV TVRSEMGEPIHKIATRGVMLWKEFDETIFNLPKNKLVPTL EAKRDYIISRLNADFQKPWFATVNGQARDLATMTYEEVAK RLVELMFIRSTNSWFDVTWRTFTGDFLRRVEERFTKSKTL SLIQSYSLLDKPDEAIEKVFNAYPAAREQFLNAQDIDHFL SMCQNPMQKPVPFVPVLDRRFEIFFKKDSLWQSEHLEAVV DQDVQRTCILHGPVAAQFTKVIDEPIKSIMDGIHDGHIKK LLHQYYGDDESKIPAVEYFGGESPVDSAVFKATSSTDEES WFKALAGSEINWRHASFLCSFITQDKMFVSNPIRKVFKPS QGMVVEISNGNTSSKTVVTLSEPVQGELKPTVILKLLKEN IIQMEMIENRTMDGKPVSLPLLYNFNPDNGFAPISEVMED RNQRIKEMYWKLWIDEPFNLDFDPRDVIKGKDFEITAKEV YDFTHAVGNNCEDFVSRPDRTMLAPMDFAIVVGWRAIIKA IFPNTVDGDLLKLVHLSNGYKMIPGAKPLQVGDVVSTTAV IESVVNQPTGKIVDVVGTLSRNGKPVMEVTSSFFYRGNYT DFENTFQKTVEPVYQMHIKTSKDIAVLRSKEWFQLDDEDF DLLNKTLTFETETEVTFKNANIFSSVKCFGPIKVELPTKE TVEIGIVDYEAGASHGNPVVDFLKRNGSTLEQKVNLENPI PIAVLDSYTPSTNEPYARVSGDLNPIHVSRHFASYANLPG TITHGMFSSASVRALIENWAADSVSSRVRGYTCQFVDMVL PNTALKTSIQHVGMINGRKLIKFETRNEDDVVVLTGEAEI EQPVTTFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNH FKDTYGFSILDIVINNPVNLTIHFGGEKGKRIRENYSAMI FETIVDGKLKTEKIFKEINEHSTSYTFRSEKGLLSATQFT QPALTLMEKAAFEDLKSKGLIPADATFAGHSLGEYAALAS LADVMSIESLVEVVFYRGMTMQVAVPRDELGRSNYGMIAI NPGRVAASFSQEALQYVVERVGKRTGWLVEIVNYNVENQQ YVAAGDLRALDTVTNVLNFIKLQKIDIIELQKSLSLEEVE GHLFEIIDEASKKSAVKPRPLKLERGFACIPLVGISVPFH STYLMNGVKPFKSFLKKNIIKENVKVARLAGKYIPNLTAK PFQVTKEYFQDVYDLTGSEPIKEIIDNWEKYEQ I:  STRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEP TEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVL NLCLTEFENCYLEGNDIHALAAKLLQENDTTLVKTKELIK NYITARIMAKRPFDKKSNSALFRAVGEGNAQLVAIFGGQG NTDDYFEELRDLYQTYHVLVGDLIKFSAETLSELIRTTLD AEKVFTQGLNILEWLENPSNTPDKDYLLSIPISCPLIGVI QLAHYVVTAKLLGFTPGELRSYLKGATGHSQGLVTAVAIA ETDSWESFFVSVRKAITVLFFIGVRCYEAYPNTSLPPSIL EDSLENNEGVPSPMLSISNLTQEQVQDYVNKTNSHLPAGK QVEISLVNGAKNLVVSGPPQSLYGLNLTLRKAKAPSGLDQ SRIPFSERKLKFSNRFLPVASPFHSHLLVPASDLINKDLV KNNVSFNAKDIQIPVYDTFDGSDLRVLSGSISERIVDCII RLPVKWETTTQFKATHILDFGPGGASGLGVLTHRNKDGTG VRVIVAGTLDINPDDDYGFKQEIFDVTSNGLKKNPNWLEE YHPKLIKNKSGKIFVETKFSKLIGRPPLLVPGMTPCTVSP DFVAATTNAGYTIELAGGGYFSAAGMTAAIDSVVSQIEKG STFGINLIYVNPFMLQWGIPLIKELRSKGYPIQFLTIGAG VPSLEVASEYIETLGLKYLGLKPGSIDAISQVINIAKAHP NFPIALQWTGGRGGGHHSFEDAHTPMLQMYSKIRRHPNIM LIFGSGFGSADDTYPYLTGEWSTKFDYPPMPFDGFLFGSR VMIAKEVKTSPDAKKCIAACTGVPDDKWEQTYKKPTGGIV TVRSEMGEPIHKIATRGVMLWKEFDETIFNLPKNKLVPTL EAKRDYIISRLNADFQKPWFATVNGQARDLATMTYEEVAK RLVELMFIRSTNSWFDVTWRTFTGDFLRRVEERFTKSKTL SLIQSYSLLDKPDEAIEKVFNAYPAAREQFLNAQDIDHFL SMCQNPMQKPVPFVPVLDRRFEIFFKKDSLWQSEHLEAVV DQDVQRTCILHGPVAAQFTKVIDEPIKSIMDGIHDGHIKK LLHQYYGDDESKIPAVEYFGGESPVDSAVFKATSSTDEES WFKALAGSEINWRHASFLCSFITQDKMFVSNPIRKVFKPS QGMVVEISNGNTSSKTVVTLSEPVQGELKPTVILKLLKEN IIQMEMIENRTMDGKPVSLPLLYNFNPDNGFAPISEVMED RNQRIKEMYWKLWIDEPFNLDFDPRDVIKGKDFEITAKEV YDFTHAVGNNCEDFVSRPDRTMLAPMDFAIVVGWRAIIKA IFPNTVDGDLLKLVHLSNGYKMIPGAKPLQVGDVVSTTAV IESVVNQPTGKIVDVVGTLSRNGKPVMEVTSSFFYRGNYT DFENTFQKTVEPVYQMHIKTSKDIAVLRSKEWFQLDDEDF DLLNKTLTFETETEVTFKNANIFSSVKCFGPIKVELPTKE TVEIGIVDYEAGASHGNPVVDFLKRNGSTLEQKVNLENPI PIAVLDSYTPSTNEPYARVSGDLNPIHVSRHFASYANLPG TITHGMFSSASVRALIENWAADSVSSRVRGYTCQFVDMVL PNTALKTSIQHVGMINGRKLIKFETRNEDDVVVLTGEAEI EQPVTTFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNH FKDTYGFSILDIVINNPVNLTIHFGGEKGKRIRENYSAMI FETIVDGKLKTEKIFKEINEHSTSYTFRSEKGLLSATQFT QPALTLMEKAAFEDLKSKGLIPADATFAGHSLGEYAALAS LADVMSIESLVEVVFYRGMTMQVAVPRDELGRSNYGMIAI NPGRVAASFSQEALQYVVERVGKRTGWLVEIVNYNVENQQ YVAAGDLRALDTVTNVLNFIKLQKIDIIELQKSLSLEEVE GHLFEIIDEASKKSAVKPRPLKLERGFACIPLVGISVPFH STYLMNGVKPFKSFLKKNIIKENVKVARLAGKYIPNLTAK PFQVTKEYFQDVYDLTGSEPIKEIIDNWEKYEQ Description Functional site 1) chain A residue 1279 type sequence F description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 2) chain A residue 1304 type sequence A description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 3) chain A residue 1305 type sequence C description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 4) chain A residue 1343 type sequence F description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 5) chain A residue 1542 type sequence H description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 6) chain A residue 1583 type sequence H description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 7) chain A residue 1585 type sequence K description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 8) chain A residue 1644 type sequence F description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 9) chain A residue 1646 type sequence F description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 10) chain B residue 1305 type sequence C description BINDING SITE FOR RESIDUE CER B 2748 source : AC2 11) chain B residue 1343 type sequence F description BINDING SITE FOR RESIDUE CER B 2748 source : AC2 12) chain B residue 1542 type sequence H description BINDING SITE FOR RESIDUE CER B 2748 source : AC2 13) chain B residue 1583 type sequence H description BINDING SITE FOR RESIDUE CER B 2748 source : AC2 14) chain B residue 1585 type sequence K description BINDING SITE FOR RESIDUE CER B 2748 source : AC2 15) chain B residue 1644 type sequence F description BINDING SITE FOR RESIDUE CER B 2748 source : AC2 16) chain B residue 1646 type sequence F description BINDING SITE FOR RESIDUE CER B 2748 source : AC2 17) chain C residue 1279 type sequence F description BINDING SITE FOR RESIDUE CER B 2748 source : AC2 18) chain B residue 1279 type sequence F description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 19) chain C residue 1304 type sequence A description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 20) chain C residue 1305 type sequence C description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 21) chain C residue 1343 type sequence F description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 22) chain C residue 1542 type sequence H description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 23) chain C residue 1583 type sequence H description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 24) chain C residue 1585 type sequence K description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 25) chain C residue 1644 type sequence F description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 26) chain C residue 1646 type sequence F description BINDING SITE FOR RESIDUE CER C 2748 source : AC3 27) chain G residue 595 type sequence P description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 28) chain G residue 596 type sequence G description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 29) chain G residue 597 type sequence M description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 30) chain G residue 598 type sequence T description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 31) chain G residue 599 type sequence P description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 32) chain G residue 650 type sequence N description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 33) chain G residue 682 type sequence G description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 34) chain G residue 706 type sequence K description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 35) chain G residue 733 type sequence T description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 36) chain G residue 737 type sequence G description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 37) chain G residue 738 type sequence G description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 38) chain G residue 769 type sequence S description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 39) chain G residue 770 type sequence G description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 40) chain G residue 802 type sequence G description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 41) chain G residue 803 type sequence S description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 42) chain G residue 806 type sequence M description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 43) chain G residue 1054 type sequence L description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 44) chain G residue 1059 type sequence A description BINDING SITE FOR RESIDUE FMN G 3051 source : AC4 45) chain H residue 595 type sequence P description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 46) chain H residue 596 type sequence G description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 47) chain H residue 597 type sequence M description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 48) chain H residue 598 type sequence T description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 49) chain H residue 599 type sequence P description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 50) chain H residue 650 type sequence N description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 51) chain H residue 652 type sequence I description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 52) chain H residue 682 type sequence G description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 53) chain H residue 706 type sequence K description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 54) chain H residue 733 type sequence T description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 55) chain H residue 737 type sequence G description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 56) chain H residue 738 type sequence G description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 57) chain H residue 769 type sequence S description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 58) chain H residue 770 type sequence G description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 59) chain H residue 802 type sequence G description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 60) chain H residue 803 type sequence S description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 61) chain H residue 1054 type sequence L description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 62) chain H residue 1059 type sequence A description BINDING SITE FOR RESIDUE FMN H 3051 source : AC5 63) chain I residue 595 type sequence P description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 64) chain I residue 596 type sequence G description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 65) chain I residue 597 type sequence M description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 66) chain I residue 598 type sequence T description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 67) chain I residue 650 type sequence N description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 68) chain I residue 652 type sequence I description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 69) chain I residue 682 type sequence G description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 70) chain I residue 706 type sequence K description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 71) chain I residue 733 type sequence T description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 72) chain I residue 737 type sequence G description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 73) chain I residue 738 type sequence G description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 74) chain I residue 739 type sequence G description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 75) chain I residue 769 type sequence S description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 76) chain I residue 770 type sequence G description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 77) chain I residue 802 type sequence G description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 78) chain I residue 803 type sequence S description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 79) chain I residue 1054 type sequence L description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 80) chain I residue 1059 type sequence A description BINDING SITE FOR RESIDUE FMN I 3051 source : AC6 81) chain A residue 175-190 type prosite sequence LVGGKSTVQNEILGDL description PHOSPHOPANTETHEINE Phosphopantetheine attachment site. LVGGKSTVQNEILGDL source prosite : PS00012 82) chain A residue 1296-1312 type prosite sequence GPIKTPVGACATSVESV description KS3_1 Ketosynthase family 3 (KS3) active site signature. GPIktPVgACATSveSV source prosite : PS00606 83) chain G residue 274 type ACT_SITE sequence S description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 84) chain H residue 274 type ACT_SITE sequence S description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 85) chain I residue 274 type ACT_SITE sequence S description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 86) chain B residue 1305 type ACT_SITE sequence C description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 87) chain B residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 88) chain B residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 89) chain C residue 1305 type ACT_SITE sequence C description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 90) chain C residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 91) chain C residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 92) chain G residue 1808 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 93) chain B residue 1773 type ACT_SITE sequence V description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 94) chain B residue 1774 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 95) chain B residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 96) chain B residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 97) chain B residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 98) chain B residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 99) chain B residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 100) chain C residue 1772 type ACT_SITE sequence D description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 101) chain C residue 1773 type ACT_SITE sequence V description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 102) chain C residue 1774 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 103) chain H residue 1808 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 104) chain C residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 105) chain C residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 106) chain C residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 107) chain C residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 108) chain C residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 109) chain I residue 1808 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 110) chain A residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 111) chain A residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 112) chain A residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 113) chain A residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 114) chain A residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 115) chain B residue 1772 type ACT_SITE sequence D description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 116) chain B residue 1808 type MOD_RES sequence S description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 117) chain C residue 1798 type MOD_RES sequence Y description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 118) chain C residue 1808 type MOD_RES sequence S description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 119) chain G residue 733 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 120) chain H residue 733 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 121) chain I residue 733 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 122) chain G residue 1364 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 123) chain B residue 523 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 124) chain H residue 1364 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 125) chain I residue 1364 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 126) chain A residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 127) chain A residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 128) chain B residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 129) chain B residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 130) chain C residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 131) chain C residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 132) chain A residue 37 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI8 133) chain B residue 37 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI8 134) chain C residue 37 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI8

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