ID   CYSG1_YERE8             Reviewed;         472 AA.
AC   A1JJS8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Siroheme synthase 1 {ECO:0000255|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Uroporphyrinogen-III C-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01646};
DE              Short=Urogen III methylase 1 {ECO:0000255|HAMAP-Rule:MF_01646};
DE              EC=2.1.1.107 {ECO:0000255|HAMAP-Rule:MF_01646};
DE     AltName: Full=SUMT 1 {ECO:0000255|HAMAP-Rule:MF_01646};
DE     AltName: Full=Uroporphyrinogen III methylase 1 {ECO:0000255|HAMAP-Rule:MF_01646};
DE              Short=UROM 1 {ECO:0000255|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Precorrin-2 dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01646};
DE              EC=1.3.1.76 {ECO:0000255|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Sirohydrochlorin ferrochelatase 1 {ECO:0000255|HAMAP-Rule:MF_01646};
DE              EC=4.99.1.4 {ECO:0000255|HAMAP-Rule:MF_01646};
GN   Name=cysG1 {ECO:0000255|HAMAP-Rule:MF_01646};
GN   OrderedLocusNames=YE0761;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent
CC       methylations of uroporphyrinogen III at position C-2 and C-7 to form
CC       precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring
CC       dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it
CC       catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
CC       {ECO:0000255|HAMAP-Rule:MF_01646}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) +
CC         precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01646};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin;
CC         Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827; EC=1.3.1.76;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01646};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin;
CC         Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01646};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01646}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01646}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01646}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; siroheme from sirohydrochlorin: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01646}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01646}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2
CC       dehydrogenase / sirohydrochlorin ferrochelatase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01646}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the precorrin
CC       methyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01646}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM286415; CAL10865.1; -; Genomic_DNA.
DR   RefSeq; WP_011815607.1; NC_008800.1.
DR   RefSeq; YP_001005104.1; NC_008800.1.
DR   AlphaFoldDB; A1JJS8; -.
DR   SMR; A1JJS8; -.
DR   KEGG; yen:YE0761; -.
DR   PATRIC; fig|393305.7.peg.855; -.
DR   eggNOG; COG0007; Bacteria.
DR   eggNOG; COG1648; Bacteria.
DR   HOGENOM; CLU_011276_2_0_6; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00148; UER00211.
DR   UniPathway; UPA00148; UER00222.
DR   UniPathway; UPA00262; UER00211.
DR   UniPathway; UPA00262; UER00222.
DR   UniPathway; UPA00262; UER00376.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11642; SUMT; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.8.210; Sirohaem synthase, dimerisation domain; 1.
DR   HAMAP; MF_01646; Siroheme_synth; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006366; CobA/CysG_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR037115; Sirohaem_synt_dimer_dom_sf.
DR   InterPro; IPR012409; Sirohaem_synth.
DR   InterPro; IPR028281; Sirohaem_synthase_central.
DR   InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
DR   InterPro; IPR006367; Sirohaem_synthase_N.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR   NCBIfam; TIGR01470; cysG_Nterm; 1.
DR   PANTHER; PTHR45790:SF1; SIROHEME SYNTHASE; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF10414; CysG_dimeriser; 1.
DR   Pfam; PF13241; NAD_binding_7; 1.
DR   Pfam; PF14824; Sirohm_synth_M; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036426; Sirohaem_synth; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Lyase; Methyltransferase; Multifunctional enzyme;
KW   NAD; Oxidoreductase; Phosphoprotein; Porphyrin biosynthesis;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..472
FT                   /note="Siroheme synthase 1"
FT                   /id="PRO_0000330570"
FT   REGION          1..203
FT                   /note="Precorrin-2 dehydrogenase /sirohydrochlorin
FT                   ferrochelatase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   REGION          215..472
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   ACT_SITE        269
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   BINDING         22..23
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   BINDING         43..44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   BINDING         224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   BINDING         300..302
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   BINDING         305
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   BINDING         330..331
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   BINDING         382
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   BINDING         411
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
SQ   SEQUENCE   472 AA;  50883 MW;  83AFFDE728DFB39B CRC64;
     MDYLPLFADL KRRPVLVVGG GEVAARKIDL LHRAGAQVRV VAQTLSSELE QLHQDGRIHW
     LALDFLPEQL DEVFLVIAAT NDTALNAAVF AAADQRHLLA NVVDDQPRCS FIFPSIVDRS
     PLVVAISSAG QAPVLARILR EKLEALLPSS LGDMAAVAGR WRGRVKQHIA SMGERRRFWE
     NAFSGRFASL ISRGQLAQAE EELQLSLEGQ NRNQGEVALV GAGPGDPGLL TLRGLQVIQQ
     ADVVLYDHLV SPEVLDLVRR DAQRICVGKR AGAHSVAQEE TNQLLVTLAQ RGKRVVRLKG
     GDPFIFGRGG EELQVVARAG IPFHIVPGVT AASGATAYAG IPLTHRDYAQ SVTFITGHCR
     ADGDDVDWQA LARGRQTLAI YMGTVKAAEI SQQLIAHGRA STTPVAVIGR GTRADQQVLT
     GTLAELELLA HQAPTPALLV IGEVVDLHHQ IAWFGQQPQT EQAISPSVVN LA
//