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6P7D

D104N S. typhimurium siroheme synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004325molecular_functionferrochelatase activity
A0004851molecular_functionuroporphyrin-III C-methyltransferase activity
A0006779biological_processporphyrin-containing compound biosynthetic process
A0008168molecular_functionmethyltransferase activity
A0009236biological_processcobalamin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0016829molecular_functionlyase activity
A0019354biological_processsiroheme biosynthetic process
A0032259biological_processmethylation
A0043115molecular_functionprecorrin-2 dehydrogenase activity
A0051266molecular_functionsirohydrochlorin ferrochelatase activity
A0051287molecular_functionNAD binding
B0003824molecular_functioncatalytic activity
B0004325molecular_functionferrochelatase activity
B0004851molecular_functionuroporphyrin-III C-methyltransferase activity
B0006779biological_processporphyrin-containing compound biosynthetic process
B0008168molecular_functionmethyltransferase activity
B0009236biological_processcobalamin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0016829molecular_functionlyase activity
B0019354biological_processsiroheme biosynthetic process
B0032259biological_processmethylation
B0043115molecular_functionprecorrin-2 dehydrogenase activity
B0051266molecular_functionsirohydrochlorin ferrochelatase activity
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue SAH A 501
ChainResidue
APRO225
ACYS336
ATYR381
AMET382
AVAL408
AASN410
AGLY411
AALA437
ALEU438
ALEU250
AGLY301
AGLY302
AASP303
AILE306
APHE307
ATHR331
AALA332

site_idAC2
Number of Residues17
Detailsbinding site for residue SAH B 501
ChainResidue
BPRO225
BGLY301
BGLY302
BASP303
BILE306
BPHE307
BTHR331
BALA332
BTYR381
BMET382
BVAL408
BASN410
BGLY411
BPRO436
BALA437
BLEU438
BHOH621

site_idAC3
Number of Residues4
Detailsbinding site for residue CL B 502
ChainResidue
BALA128
BGLY130
BSER132
BPRO133

Functional Information from PROSITE/UniProt
site_idPS00839
Number of Residues15
DetailsSUMT_1 Uroporphyrin-III C-methyltransferase signature 1. VGAGPGdagLLTLKG
ChainResidueDetails
AVAL221-GLY235

site_idPS00840
Number of Residues34
DetailsSUMT_2 Uroporphyrin-III C-methyltransferase signature 2. VvrLkgGDpfiFGrggeeletLchagipFsVvPG
ChainResidueDetails
AVAL296-GLY329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues396
DetailsRegion: {"description":"Precorrin-2 dehydrogenase /sirohydrochlorin ferrochelatase"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 702
ChainResidueDetails
AASP248electrostatic stabiliser, proton acceptor, proton donor
ALYS270electrostatic stabiliser
AMET382electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 702
ChainResidueDetails
BASP248electrostatic stabiliser, proton acceptor, proton donor
BLYS270electrostatic stabiliser
BMET382electrostatic stabiliser

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PDB entries from 2025-07-09

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