eF-site ID 2vkz-ABCGHI PDB Code 2vkz Chain A, B, C, G, H, I Title Structure of the cerulenin-inhibited fungal fatty acid synthase type I multienzyme complex Classification TRANSFERASE Compound FATTY ACID SYNTHASE SUBUNIT ALPHA Source ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; 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 NSKNIQSKDSYINA 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 NSKNIQSKDSYINA 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 NSKNIQSKDSYINA 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 (1)  FATTY ACID SYNTHASE SUBUNIT ALPHA (E.C.2.3.1.86, 2.3.1.41), FATTY ACID SYNTHASE SUBUNIT BETA (E.C.2.3.1.86, 3.1.2.14) Functional site 1) chain G residue 595 type sequence P description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 2) chain G residue 596 type sequence G description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 3) chain G residue 597 type sequence M description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 4) chain G residue 598 type sequence T description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 5) chain G residue 599 type sequence P description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 6) chain G residue 650 type sequence N description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 7) chain G residue 682 type sequence G description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 8) chain G residue 706 type sequence K description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 9) chain G residue 733 type sequence T description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 10) chain G residue 737 type sequence G description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 11) chain G residue 738 type sequence G description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 12) chain G residue 769 type sequence S description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 13) chain G residue 770 type sequence G description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 14) chain G residue 802 type sequence G description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 15) chain G residue 803 type sequence S description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 16) chain G residue 806 type sequence M description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 17) chain G residue 1054 type sequence L description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 18) chain G residue 1059 type sequence A description BINDING SITE FOR RESIDUE FMN G3051 source : AC1 19) chain H residue 595 type sequence P description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 20) chain H residue 596 type sequence G description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 21) chain H residue 597 type sequence M description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 22) chain H residue 598 type sequence T description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 23) chain H residue 599 type sequence P description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 24) chain H residue 650 type sequence N description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 25) chain H residue 652 type sequence I description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 26) chain H residue 682 type sequence G description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 27) chain H residue 706 type sequence K description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 28) chain H residue 733 type sequence T description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 29) chain H residue 737 type sequence G description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 30) chain H residue 738 type sequence G description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 31) chain H residue 769 type sequence S description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 32) chain H residue 770 type sequence G description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 33) chain H residue 802 type sequence G description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 34) chain H residue 803 type sequence S description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 35) chain H residue 1054 type sequence L description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 36) chain H residue 1059 type sequence A description BINDING SITE FOR RESIDUE FMN H3051 source : AC2 37) chain I residue 595 type sequence P description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 38) chain I residue 596 type sequence G description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 39) chain I residue 597 type sequence M description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 40) chain I residue 598 type sequence T description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 41) chain I residue 650 type sequence N description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 42) chain I residue 652 type sequence I description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 43) chain I residue 682 type sequence G description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 44) chain I residue 706 type sequence K description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 45) chain I residue 733 type sequence T description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 46) chain I residue 737 type sequence G description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 47) chain I residue 738 type sequence G description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 48) chain I residue 739 type sequence G description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 49) chain I residue 769 type sequence S description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 50) chain I residue 770 type sequence G description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 51) chain I residue 802 type sequence G description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 52) chain I residue 803 type sequence S description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 53) chain I residue 1054 type sequence L description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 54) chain I residue 1059 type sequence A description BINDING SITE FOR RESIDUE FMN I3051 source : AC3 55) chain A residue 1279 type sequence F description BINDING SITE FOR RESIDUE CER A2748 source : AC4 56) chain A residue 1304 type sequence A description BINDING SITE FOR RESIDUE CER A2748 source : AC4 57) chain A residue 1305 type sequence C description BINDING SITE FOR RESIDUE CER A2748 source : AC4 58) chain A residue 1343 type sequence F description BINDING SITE FOR RESIDUE CER A2748 source : AC4 59) chain A residue 1542 type sequence H description BINDING SITE FOR RESIDUE CER A2748 source : AC4 60) chain A residue 1583 type sequence H description BINDING SITE FOR RESIDUE CER A2748 source : AC4 61) chain A residue 1585 type sequence K description BINDING SITE FOR RESIDUE CER A2748 source : AC4 62) chain A residue 1644 type sequence F description BINDING SITE FOR RESIDUE CER A2748 source : AC4 63) chain A residue 1646 type sequence F description BINDING SITE FOR RESIDUE CER A2748 source : AC4 64) chain B residue 1305 type sequence C description BINDING SITE FOR RESIDUE CER B2748 source : AC5 65) chain B residue 1343 type sequence F description BINDING SITE FOR RESIDUE CER B2748 source : AC5 66) chain B residue 1542 type sequence H description BINDING SITE FOR RESIDUE CER B2748 source : AC5 67) chain B residue 1583 type sequence H description BINDING SITE FOR RESIDUE CER B2748 source : AC5 68) chain B residue 1585 type sequence K description BINDING SITE FOR RESIDUE CER B2748 source : AC5 69) chain B residue 1644 type sequence F description BINDING SITE FOR RESIDUE CER B2748 source : AC5 70) chain B residue 1646 type sequence F description BINDING SITE FOR RESIDUE CER B2748 source : AC5 71) chain C residue 1279 type sequence F description BINDING SITE FOR RESIDUE CER B2748 source : AC5 72) chain B residue 1279 type sequence F description BINDING SITE FOR RESIDUE CER C2748 source : AC6 73) chain C residue 1304 type sequence A description BINDING SITE FOR RESIDUE CER C2748 source : AC6 74) chain C residue 1305 type sequence C description BINDING SITE FOR RESIDUE CER C2748 source : AC6 75) chain C residue 1343 type sequence F description BINDING SITE FOR RESIDUE CER C2748 source : AC6 76) chain C residue 1542 type sequence H description BINDING SITE FOR RESIDUE CER C2748 source : AC6 77) chain C residue 1583 type sequence H description BINDING SITE FOR RESIDUE CER C2748 source : AC6 78) chain C residue 1585 type sequence K description BINDING SITE FOR RESIDUE CER C2748 source : AC6 79) chain C residue 1644 type sequence F description BINDING SITE FOR RESIDUE CER C2748 source : AC6 80) chain C residue 1646 type sequence F description BINDING SITE FOR RESIDUE CER C2748 source : AC6 81) 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 82) 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 83) 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 84) chain A residue 1296-1312 type prosite sequence GPIKTPVGACATSVESV description KS3_1 Ketosynthase family 3 (KS3) active site signature. GPIktPVgACATSveSV source prosite : PS00606 85) chain G residue 274 type ACT_SITE sequence S description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 86) chain H residue 274 type ACT_SITE sequence S description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 87) chain I residue 274 type ACT_SITE sequence S description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 88) chain B residue 1305 type ACT_SITE sequence C description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 89) chain B residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 90) chain B residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 91) chain C residue 1305 type ACT_SITE sequence C description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 92) chain C residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 93) chain C residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 94) chain G residue 1808 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 95) chain H residue 1808 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 96) chain I residue 1808 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 97) chain I residue 733 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 98) chain G residue 733 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 99) chain H residue 733 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 100) 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 101) 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 102) 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 103) 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 104) chain A residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 105) chain A residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 106) chain B residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 107) chain B residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 108) chain C residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 109) chain C residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 110) chain A residue 175-190 type prosite sequence LVGGKSTVQNEILGDL description PHOSPHOPANTETHEINE Phosphopantetheine attachment site. LVGGKSTVQNEILGDL source prosite : PS00012

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