eF-site ID 6qak-ABCDEFGH PDB Code 6qak Chain A, B, C, D, E, F, G, H click to enlarge Title Structure of human ALDH9 in P21212 space group Classification OXIDOREDUCTASE Compound 4-trimethylaminobutyraldehyde dehydrogenase Source (AL9A1_HUMAN) Sequence A:  PMSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRV IATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLE AARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEY YAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYP FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA GVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGGKSPLII FSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFV KVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRD DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGV FTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS GFGRENGRVTIEYYSQLKTVCVEMGDVESAF B:  PMSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRV IATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLE AARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEY YAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYP FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA GVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGGKSPLII FSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFV KVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRD DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGV FTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS GFGRENGRVTIEYYSQLKTVCVEMGDVESAF C:  PMSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRV IATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLE AARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEY YAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYP FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA GVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGGKSPLII FSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFV KVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRD DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGV FTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS GFGRENGRVTIEYYSQLKTVCVEMGDVESAF D:  PMSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRV IATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLE AARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEY YAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYP FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA GVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGGKSPLII FSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFV KVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRD DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGV FTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS GFGRENGRVTIEYYSQLKTVCVEMGDVESAF E:  PMSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRV IATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLE AARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEY YAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYP FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA GVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGGKSPLII FSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFV KVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRD DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGV FTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS GFGRENGRVTIEYYSQLKTVCVEMGDVESAF F:  PMSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRV IATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLE AARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEY YAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYP FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA GVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGGKSPLII FSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFV KVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRD DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGV FTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS GFGRENGRVTIEYYSQLKTVCVEMGDVESAF G:  PMSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRV IATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLE AARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEY YAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYP FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA GVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGGKSPLII FSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFV KVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRD DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGV FTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS GFGRENGRVTIEYYSQLKTVCVEMGDVESAF H:  PMSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRV IATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLE AARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEY YAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYP FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA GVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGGKSPLII FSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFV KVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRD DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGV FTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS GFGRENGRVTIEYYSQLKTVCVEMGDVESAF Description Functional site 1) chain B residue 217 type sequence Q description binding site for residue EDO B 501 source : AC1 2) chain E residue 303 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 3) chain F residue 30 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 4) chain F residue 303 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 5) chain G residue 30 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 6) chain G residue 303 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 7) chain H residue 30 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 8) chain H residue 303 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 9) chain E residue 30 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 10) chain A residue 303 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 11) chain B residue 30 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 12) chain B residue 303 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 13) chain C residue 30 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 14) chain D residue 30 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 15) chain D residue 303 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 16) chain A residue 30 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 17) chain C residue 303 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI6 18) chain B residue 59 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI7 19) chain C residue 59 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI7 20) chain D residue 59 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI7 21) chain E residue 59 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI7 22) chain F residue 59 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI7 23) chain G residue 59 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI7 24) chain H residue 59 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI7 25) chain A residue 59 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI7 26) chain B residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 27) chain C residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 28) chain D residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 29) chain E residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 30) chain F residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 31) chain G residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 32) chain H residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 33) chain A residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 344 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI9 35) chain B residue 344 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI9 36) chain C residue 344 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI9 37) chain D residue 344 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI9 38) chain E residue 344 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI9 39) chain F residue 344 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI9 40) chain G residue 344 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI9 41) chain H residue 344 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9JLJ2 source Swiss-Prot : SWS_FT_FI9 42) chain A residue 281-292 type prosite sequence FLTQGQVCCNGT description ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FlTQGQVCCNGT source prosite : PS00070 43) chain B residue 288 type ACT_SITE sequence C description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI2 44) chain C residue 288 type ACT_SITE sequence C description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI2 45) chain D residue 288 type ACT_SITE sequence C description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI2 46) chain E residue 288 type ACT_SITE sequence C description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI2 47) chain G residue 288 type ACT_SITE sequence C description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI2 48) chain H residue 288 type ACT_SITE sequence C description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 288 type ACT_SITE sequence C description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI2 50) chain F residue 288 type ACT_SITE sequence C description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI2 51) chain D residue 180 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 52) chain D residue 391 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 53) chain E residue 180 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 54) chain E residue 391 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 55) chain F residue 180 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 56) chain F residue 391 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 57) chain G residue 180 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 58) chain G residue 391 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 59) chain H residue 180 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 60) chain H residue 391 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 61) chain C residue 391 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 62) chain A residue 391 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 63) chain B residue 180 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 64) chain C residue 180 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 65) chain A residue 180 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 66) chain B residue 391 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P56533 source Swiss-Prot : SWS_FT_FI3 67) chain B residue 157 type SITE sequence N description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 68) chain C residue 157 type SITE sequence N description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 69) chain D residue 157 type SITE sequence N description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 70) chain E residue 157 type SITE sequence N description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 71) chain F residue 157 type SITE sequence N description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 72) chain G residue 157 type SITE sequence N description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 73) chain H residue 157 type SITE sequence N description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 74) chain A residue 157 type SITE sequence N description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 75) chain B residue 2 type MOD_RES sequence S description N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 76) chain C residue 2 type MOD_RES sequence S description N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 77) chain D residue 2 type MOD_RES sequence S description N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 78) chain E residue 2 type MOD_RES sequence S description N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 79) chain G residue 2 type MOD_RES sequence S description N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 80) chain H residue 2 type MOD_RES sequence S description N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 81) chain A residue 2 type MOD_RES sequence S description N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 82) chain F residue 2 type MOD_RES sequence S description N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links