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1FUG

S-ADENOSYLMETHIONINE SYNTHETASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004478molecular_functionmethionine adenosyltransferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006556biological_processS-adenosylmethionine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0016740molecular_functiontransferase activity
A0030955molecular_functionpotassium ion binding
A0033353biological_processS-adenosylmethionine cycle
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004478molecular_functionmethionine adenosyltransferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006556biological_processS-adenosylmethionine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0016740molecular_functiontransferase activity
B0030955molecular_functionpotassium ion binding
B0033353biological_processS-adenosylmethionine cycle
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00376
Number of Residues11
DetailsADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY
ChainResidueDetails
AGLY115-TYR125

site_idPS00377
Number of Residues9
DetailsADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD
ChainResidueDetails
AGLY258-ASP266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9
ChainResidueDetails
AHIS14
BGLN98
BASP163
BARG229
BARG244
BLYS269
AGLU55
AGLN98
AASP163
AARG229
AARG244
ALYS269
BHIS14
BGLU55

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9
ChainResidueDetails
AASP16
AALA261
ALYS265
BASP16
BALA261
BLYS265

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0000305|PubMed:7629147, ECO:0007744|PDB:1MXC, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9
ChainResidueDetails
AGLU42
BGLU42

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L
ChainResidueDetails
AASP238
BASP238

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS2
BLYS2

Catalytic Information from CSA
site_idCSA1
Number of Residues7
Detailsa catalytic site defined by CSA, PubMed 10551856, 8550549, 8611562, 8723769
ChainResidueDetails
ALYS269
ALYS265
AASP271
BLYS245
BHIS14
BLYS165
BARG244

site_idCSA2
Number of Residues7
Detailsa catalytic site defined by CSA, PubMed 10551856, 8550549, 8611562, 8723769
ChainResidueDetails
ALYS245
AHIS14
ALYS165
AARG244
BLYS269
BLYS265
BASP271

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PDB entries from 2025-06-18

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