eF-site ID 1umd-ABCD PDB Code 1umd Chain A, B, C, D click to enlarge Title branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 with 4-methyl-2-oxopentanoate as an intermediate Classification OXIDOREDUCTASE Compound 2-oxo acid dehydrogenase alpha subunit Source null (ODBB_THET8) Sequence A:  HRFETFTEEPIRLIGEEGEWLGDFPLDLEGEKLRRLYRDM LAARMLDERYTILIRTGKTSFIAPAAGHEAAQVAIAHAIR PGFDWVFPYYRDHGLALALGIPLKELLGQMLATKADPNKG RQMPEHPGSKALNFFTVASPIASHVPPAAGAAISMKLLRT GQVAVCTFGDGATSEGDWYAGINFAAVQGAPAVFIAENNF YAISVDYRHQTHSPTIADKAHAFGIPGYLVDGMDVLASYY VVKEAVERARRGEGPSLVELRVYRYGPHSSADDDSRYRPK EEVAFWRKKDPIPRFRRFLEARGLWNEEWEEDVREEIRAE LERGLKEAEEAGPVPPEWMFEDVFAEKPWHLLRQEALLKE EL B:  ALMTMVQALNRALDEEMAKDPRVVVLGEDVGKRGGVFLVT EGLLQKYGPDRVMDTPLSEAAIVGAALGMAAHGLRPVAEI QFADYIFPGFDQLVSQVAKLRYRSGGQFTAPLVVRMPSGG GVRGGHHHSQSPEAHFVHTAGLKVVAVSTPYDAKGLLKAA IRDEDPVVFLEPKRLYRSVKEEVPEEDYTLPIGKAALRRE GKDLTLICYGTVMPEVLQAAAELAKAGVSAEVLDLRTLMP WDYEAVMNSVAKTGRVVLVSDAPRHASFVSEVAATIAEDL LDMLLAPPIRVTGFDTPYPYAQDKLYLPTVTRILNAAKRA LDY C:  HRFETFTEEPIRLIGEEGEWLGDFPLDLEGEKLRRLYRDM LAARMLDERYTILIRTGKTSFIAPAAGHEAAQVAIAHAIR PGFDWVFPYYRDHGLALALGIPLKELLGQMLATKADPNKG RQMPEHPGSKALNFFTVASPIASHVPPAAGAAISMKLLRT GQVAVCTFGDGATSEGDWYAGINFAAVQGAPAVFIAENNF YAISVDYRHQTHSPTIADKAHAFGIPGYLVDGMDVLASYY VVKEAVERARRGEGPSLVELRVYRYGPHSSADDDSRYRPK EEVAFWRKKDPIPRFRRFLEARGLWNEEWEEDVREEIRAE LERGLKEAEEAGPVPPEWMFEDVFAEKPWHLLRQEALLKE E D:  ALMTMVQALNRALDEEMAKDPRVVVLGEDVGKRGGVFLVT EGLLQKYGPDRVMDTPLSEAAIVGAALGMAAHGLRPVAEI QFADYIFPGFDQLVSQVAKLRYRSGGQFTAPLVVRMPSGG GVRGGHHHSQSPEAHFVHTAGLKVVAVSTPYDAKGLLKAA IRDEDPVVFLEPKRLYRSVKEEVPEEDYTLPIGKAALRRE GKDLTLICYGTVMPEVLQAAAELAKAGVSAEVLDLRTLMP WDYEAVMNSVAKTGRVVLVSDAPRHASFVSEVAATIAEDL LDMLLAPPIRVTGFDTPYPYAQDKLYLPTVTRILNAAKRA LDY Description Functional site 1) chain A residue 175 type sequence D description BINDING SITE FOR RESIDUE MG A 1401 source : AC1 2) chain A residue 204 type sequence N description BINDING SITE FOR RESIDUE MG A 1401 source : AC1 3) chain A residue 206 type sequence Y description BINDING SITE FOR RESIDUE MG A 1401 source : AC1 4) chain C residue 175 type sequence D description BINDING SITE FOR RESIDUE MG C 2401 source : AC2 5) chain C residue 204 type sequence N description BINDING SITE FOR RESIDUE MG C 2401 source : AC2 6) chain C residue 206 type sequence Y description BINDING SITE FOR RESIDUE MG C 2401 source : AC2 7) chain A residue 94 type sequence Y description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 8) chain A residue 95 type sequence Y description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 9) chain A residue 96 type sequence R description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 10) chain A residue 144 type sequence S description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 11) chain A residue 145 type sequence P description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 12) chain A residue 146 type sequence I description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 13) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 14) chain A residue 175 type sequence D description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 15) chain A residue 176 type sequence G description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 16) chain A residue 177 type sequence A description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 17) chain A residue 180 type sequence E description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 18) chain A residue 204 type sequence N description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 19) chain A residue 206 type sequence Y description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 20) chain A residue 207 type sequence A description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 21) chain A residue 208 type sequence I description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 22) chain A residue 273 type sequence H description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 23) chain D residue 29 type sequence E description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 24) chain D residue 58 type sequence L description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 25) chain D residue 60 type sequence E description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 26) chain D residue 82 type sequence Q description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 27) chain D residue 86 type sequence Y description BINDING SITE FOR RESIDUE TPP A 1402 source : AC3 28) chain A residue 66 type sequence F description BINDING SITE FOR RESIDUE COI A 1403 source : AC4 29) chain A residue 144 type sequence S description BINDING SITE FOR RESIDUE COI A 1403 source : AC4 30) chain D residue 86 type sequence Y description BINDING SITE FOR RESIDUE COI A 1403 source : AC4 31) chain D residue 129 type sequence H description BINDING SITE FOR RESIDUE COI A 1403 source : AC4 32) chain B residue 29 type sequence E description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 33) chain B residue 58 type sequence L description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 34) chain B residue 60 type sequence E description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 35) chain B residue 82 type sequence Q description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 36) chain B residue 86 type sequence Y description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 37) chain C residue 94 type sequence Y description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 38) chain C residue 95 type sequence Y description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 39) chain C residue 96 type sequence R description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 40) chain C residue 144 type sequence S description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 41) chain C residue 145 type sequence P description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 42) chain C residue 146 type sequence I description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 43) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 44) chain C residue 175 type sequence D description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 45) chain C residue 176 type sequence G description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 46) chain C residue 177 type sequence A description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 47) chain C residue 180 type sequence E description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 48) chain C residue 204 type sequence N description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 49) chain C residue 206 type sequence Y description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 50) chain C residue 207 type sequence A description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 51) chain C residue 208 type sequence I description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 52) chain C residue 273 type sequence H description BINDING SITE FOR RESIDUE TPP C 2402 source : AC5 53) chain B residue 86 type sequence Y description BINDING SITE FOR RESIDUE COI C 2403 source : AC6 54) chain B residue 129 type sequence H description BINDING SITE FOR RESIDUE COI C 2403 source : AC6 55) chain C residue 66 type sequence F description BINDING SITE FOR RESIDUE COI C 2403 source : AC6 56) chain C residue 144 type sequence S description BINDING SITE FOR RESIDUE COI C 2403 source : AC6 57) chain A residue 95 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 273 type ACT_SITE sequence H description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 59) chain C residue 66 type ACT_SITE sequence F description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 60) chain C residue 94 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 61) chain C residue 95 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 62) chain C residue 128 type ACT_SITE sequence M description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 63) chain C residue 144 type ACT_SITE sequence S description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 64) chain C residue 174 type ACT_SITE sequence G description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 65) chain C residue 175 type ACT_SITE sequence D description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 66) chain C residue 204 type ACT_SITE sequence N description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 67) chain C residue 206 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 68) chain C residue 273 type ACT_SITE sequence H description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 144 type ACT_SITE sequence S description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 70) chain A residue 174 type ACT_SITE sequence G description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 71) chain A residue 175 type ACT_SITE sequence D description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 72) chain A residue 204 type ACT_SITE sequence N description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 206 type ACT_SITE sequence Y description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 74) chain A residue 128 type ACT_SITE sequence M description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 75) chain B residue 129 type ACT_SITE sequence H description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 76) chain D residue 129 type ACT_SITE sequence H description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 77) chain A residue 364-367 type prosite sequence KEEL description ER_TARGET Endoplasmic reticulum targeting sequence. KEEL source prosite : PS00014 78) chain B residue 82 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15033367 source Swiss-Prot : SWS_FT_FI2 79) chain D residue 29 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15033367 source Swiss-Prot : SWS_FT_FI2 80) chain D residue 82 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15033367 source Swiss-Prot : SWS_FT_FI2 81) chain B residue 29 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15033367 source Swiss-Prot : SWS_FT_FI2 82) chain D residue 58 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 83) chain D residue 83 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 84) chain D residue 86 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 85) chain B residue 58 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 86) chain B residue 83 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 87) chain B residue 86 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 88) chain D residue 129 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI4 89) chain B residue 129 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI4

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