eF-site ID 1umy-ABCD PDB Code 1umy Chain A, B, C, D click to enlarge Title BHMT from rat liver Classification TRANSFERASE Compound Betaine--homocysteine S-methyltransferase 1 Source (BHMT1_RAT) Sequence A:  KRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAA VEHPEAVRQLHREFLRAGSNVMQTFTFYASSGQKVNEAAC DIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQQ LEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAAT MCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPSTS LQTIKLMKEGLEAARLKAYLMSQPLAYHTPDCGKQGFIDL PEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEP YHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIR ARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELMQ QKEATTEQQLRALFE B:  KRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAA VEHPEAVRQLHREFLRAGSNVMQTFTFYASEDAEKISGQK VNEAACDIARQVADEGDALVAGGVSQTPSYLSCKSETEVK KIFHQQLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSG KPIAATMCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCH FDPSTSLQTIKLMKEGLEAARLKAYLMSQPLAYHTPDCGK QGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGG CCGFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMH TKPWIRARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKG AAELMQQKEATTEQQLRALFE C:  KRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAA VEHPEAVRQLHREFLRAGSNVMQTFTFYASGQKVNEAACD IARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQQL EVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAATM CIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPSTSL QTIKLMKEGLEAARLKAYLMSQPLAYHTPDCGKQGFIDLP EFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEPY HIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRA RARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELMQQ KEATTEQQLRALFEKQKFKSA D:  KRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAA VEHPEAVRQLHREFLRAGSNVMQTFTFYAKISGQKVNEAA CDIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQ QLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAA TMCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPST SLQTIKLMKEGLEAARLKAYLMSQPLAYHTPDCGKQGFID LPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFE PYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWI RARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELM QQKEATTEQQLRALFEKQKFKS Description Functional site 1) chain A residue 160 type sequence Y description BINDING SITE FOR RESIDUE ZN A1399 source : AC1 2) chain A residue 217 type sequence C description BINDING SITE FOR RESIDUE ZN A1399 source : AC1 3) chain A residue 299 type sequence C description BINDING SITE FOR RESIDUE ZN A1399 source : AC1 4) chain A residue 300 type sequence C description BINDING SITE FOR RESIDUE ZN A1399 source : AC1 5) chain B residue 160 type sequence Y description BINDING SITE FOR RESIDUE ZN B1399 source : AC2 6) chain B residue 217 type sequence C description BINDING SITE FOR RESIDUE ZN B1399 source : AC2 7) chain B residue 299 type sequence C description BINDING SITE FOR RESIDUE ZN B1399 source : AC2 8) chain B residue 300 type sequence C description BINDING SITE FOR RESIDUE ZN B1399 source : AC2 9) chain C residue 160 type sequence Y description BINDING SITE FOR RESIDUE ZN C1406 source : AC3 10) chain C residue 217 type sequence C description BINDING SITE FOR RESIDUE ZN C1406 source : AC3 11) chain C residue 299 type sequence C description BINDING SITE FOR RESIDUE ZN C1406 source : AC3 12) chain C residue 300 type sequence C description BINDING SITE FOR RESIDUE ZN C1406 source : AC3 13) chain D residue 160 type sequence Y description BINDING SITE FOR RESIDUE ZN D1405 source : AC4 14) chain D residue 217 type sequence C description BINDING SITE FOR RESIDUE ZN D1405 source : AC4 15) chain D residue 299 type sequence C description BINDING SITE FOR RESIDUE ZN D1405 source : AC4 16) chain D residue 300 type sequence C description BINDING SITE FOR RESIDUE ZN D1405 source : AC4 17) chain A residue 217 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 18) chain D residue 217 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 19) chain D residue 299 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 20) chain D residue 300 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 299 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 300 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 217 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 299 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 300 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 217 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 27) chain C residue 299 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 28) chain C residue 300 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 40 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 98 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 232 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 241 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 340 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 377 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 35) chain C residue 40 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 36) chain C residue 98 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 37) chain C residue 232 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 38) chain C residue 241 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 39) chain C residue 340 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 40) chain C residue 377 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 41) chain D residue 40 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 42) chain D residue 93 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 43) chain D residue 98 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 44) chain D residue 232 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 45) chain D residue 241 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 46) chain D residue 340 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 47) chain D residue 377 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 98 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 232 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 241 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 340 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 377 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 53) chain B residue 40 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 54) chain B residue 93 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O35490 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 330 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 56) chain B residue 330 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 57) chain C residue 330 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 58) chain D residue 330 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3

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