ID A0A0T9XSH3_SALET Unreviewed; 457 AA. AC A0A0T9XSH3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 27-MAR-2024, entry version 60. DE RecName: Full=Siroheme synthase {ECO:0000256|HAMAP-Rule:MF_01646}; DE Includes: DE RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01646}; DE Short=Urogen III methylase {ECO:0000256|HAMAP-Rule:MF_01646}; DE EC=2.1.1.107 {ECO:0000256|HAMAP-Rule:MF_01646}; DE AltName: Full=SUMT {ECO:0000256|HAMAP-Rule:MF_01646}; DE AltName: Full=Uroporphyrinogen III methylase {ECO:0000256|HAMAP-Rule:MF_01646}; DE Short=UROM {ECO:0000256|HAMAP-Rule:MF_01646}; DE Includes: DE RecName: Full=Precorrin-2 dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01646}; DE EC=1.3.1.76 {ECO:0000256|HAMAP-Rule:MF_01646}; DE Includes: DE RecName: Full=Sirohydrochlorin ferrochelatase {ECO:0000256|HAMAP-Rule:MF_01646}; DE EC=4.99.1.4 {ECO:0000256|HAMAP-Rule:MF_01646}; GN Name=cysG {ECO:0000256|HAMAP-Rule:MF_01646, GN ECO:0000313|EMBL:SUE45696.1}; GN Synonyms=cobA {ECO:0000313|EMBL:EBS2452198.1}; GN ORFNames=B7N00_17765 {ECO:0000313|EMBL:EDG5018796.1}, B7N01_22860 GN {ECO:0000313|EMBL:EDG4997244.1}, B7N35_03805 GN {ECO:0000313|EMBL:EDG5125156.1}, B7N72_07840 GN {ECO:0000313|EMBL:EDG5370017.1}, B7N78_06830 GN {ECO:0000313|EMBL:EDG5279492.1}, B7N80_01670 GN {ECO:0000313|EMBL:EDG5287099.1}, B7N84_22475 GN {ECO:0000313|EMBL:EDG5269097.1}, DRU31_07635 GN {ECO:0000313|EMBL:EBS2452198.1}, E0916_23440 GN {ECO:0000313|EMBL:ECF1448880.1}, EJV93_23300 GN {ECO:0000313|EMBL:ECA2724100.1}, ERS008202_03718 GN {ECO:0000313|EMBL:CNU86473.1}, ERS008207_04139 GN {ECO:0000313|EMBL:CNV04810.1}, EWC73_03270 GN {ECO:0000313|EMBL:ECE8535249.1}, G0B02_04370 GN {ECO:0000313|EMBL:HAC6378371.1}, G0D18_07700 GN {ECO:0000313|EMBL:HAC6680548.1}, G2206_22895 GN {ECO:0000313|EMBL:HAE0437581.1}, NCTC5754_00479 GN {ECO:0000313|EMBL:SUE45696.1}; OS Salmonella enterica subsp. enterica serovar Bovismorbificans. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE45696.1, ECO:0000313|Proteomes:UP000254190}; RN [1] {ECO:0000313|Proteomes:UP000039541, ECO:0000313|Proteomes:UP000042394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3476 {ECO:0000313|EMBL:CNU86473.1, RC ECO:0000313|Proteomes:UP000039541}, and D4891 RC {ECO:0000313|EMBL:CNV04810.1, ECO:0000313|Proteomes:UP000042394}; RG Pathogen Informatics; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:HAC6378371.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378371.1}, M123 RC {ECO:0000313|EMBL:HAC6680548.1}, and MS140073 RC {ECO:0000313|EMBL:HAE0437581.1}; RX PubMed=30286803; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-153(2018). RN [3] {ECO:0000313|EMBL:SUE45696.1, ECO:0000313|Proteomes:UP000254190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE45696.1, RC ECO:0000313|Proteomes:UP000254190}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:HAC6680548.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378371.1}, M123 RC {ECO:0000313|EMBL:HAC6680548.1}, and MS140073 RC {ECO:0000313|EMBL:HAE0437581.1}; RG NCBI Pathogen Detection Project; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:EBS2452198.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=136768 {ECO:0000313|EMBL:EDG4997244.1}, 138330 RC {ECO:0000313|EMBL:EDG5287099.1}, 143652 RC {ECO:0000313|EMBL:EDG5370017.1}, 273631 RC {ECO:0000313|EMBL:EDG5018796.1}, 330535 RC {ECO:0000313|EMBL:EDG5269097.1}, 333944 RC {ECO:0000313|EMBL:EDG5279492.1}, 337042 RC {ECO:0000313|EMBL:EDG5125156.1}, 387147 RC {ECO:0000313|EMBL:EBS2452198.1}, 470200 RC {ECO:0000313|EMBL:ECE8535249.1}, 598023 RC {ECO:0000313|EMBL:ECA2724100.1}, and 692616 RC {ECO:0000313|EMBL:ECF1448880.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|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:0000256|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:0000256|ARBA:ARBA00001156, ECO:0000256|HAMAP- CC Rule:MF_01646}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01646}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01646}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. CC {ECO:0000256|ARBA:ARBA00025705, ECO:0000256|HAMAP-Rule:MF_01646}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; siroheme from sirohydrochlorin: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01646}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. CC {ECO:0000256|ARBA:ARBA00005010, ECO:0000256|HAMAP-Rule:MF_01646}. CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family. CC {ECO:0000256|ARBA:ARBA00005879, ECO:0000256|RuleBase:RU003960}. CC -!- SIMILARITY: In the C-terminal section; belongs to the precorrin CC methyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01646}. CC -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2 CC dehydrogenase / sirohydrochlorin ferrochelatase family. CC {ECO:0000256|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; CQPC01000062; CNU86473.1; -; Genomic_DNA. DR EMBL; CQPD01000056; CNV04810.1; -; Genomic_DNA. DR EMBL; AAGUWJ010000004; EBS2452198.1; -; Genomic_DNA. DR EMBL; AAHTVM010000024; ECA2724100.1; -; Genomic_DNA. DR EMBL; AAIJHK010000002; ECE8535249.1; -; Genomic_DNA. DR EMBL; AAIKGE010000028; ECF1448880.1; -; Genomic_DNA. DR EMBL; AAMEJW010000038; EDG4997244.1; -; Genomic_DNA. DR EMBL; AAMEJY010000013; EDG5018796.1; -; Genomic_DNA. DR EMBL; AAMEKY010000002; EDG5125156.1; -; Genomic_DNA. DR EMBL; AAMEMC010000023; EDG5269097.1; -; Genomic_DNA. DR EMBL; AAMEMH010000003; EDG5279492.1; -; Genomic_DNA. DR EMBL; AAMEML010000001; EDG5287099.1; -; Genomic_DNA. DR EMBL; AAMEMP010000005; EDG5370017.1; -; Genomic_DNA. DR EMBL; DAAMEZ010000002; HAC6378371.1; -; Genomic_DNA. DR EMBL; DAAMHM010000004; HAC6680548.1; -; Genomic_DNA. DR EMBL; DAAQQK010000040; HAE0437581.1; -; Genomic_DNA. DR EMBL; UGVQ01000002; SUE45696.1; -; Genomic_DNA. DR RefSeq; WP_000349896.1; NZ_WFIN01000005.1. DR AlphaFoldDB; A0A0T9XSH3; -. DR SMR; A0A0T9XSH3; -. DR UniPathway; UPA00148; UER00211. DR UniPathway; UPA00262; UER00211. DR Proteomes; UP000039541; Unassembled WGS sequence. DR Proteomes; UP000042394; Unassembled WGS sequence. DR Proteomes; UP000254190; Unassembled WGS sequence. DR Proteomes; UP000839929; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP- KW Rule:MF_01646}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01646}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_01646}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01646}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01646}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01646}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01646}; KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP- KW Rule:MF_01646}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_01646}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01646}. FT DOMAIN 119..145 FT /note="Siroheme synthase central" FT /evidence="ECO:0000259|Pfam:PF14824" FT DOMAIN 150..207 FT /note="Sirohaem synthase dimerisation" FT /evidence="ECO:0000259|Pfam:PF10414" FT DOMAIN 218..426 FT /note="Tetrapyrrole methylase" FT /evidence="ECO:0000259|Pfam:PF00590" FT REGION 1..204 FT /note="Precorrin-2 dehydrogenase / sirohydrochlorin FT ferrochelatase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT REGION 216..457 FT /note="Uroporphyrinogen-III C-methyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT ACT_SITE 248 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646, FT ECO:0000256|PIRSR:PIRSR036426-1" FT ACT_SITE 270 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646, FT ECO:0000256|PIRSR:PIRSR036426-1" FT BINDING 22..23 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 43..44 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 225 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 301..303 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 306 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 331..332 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 382 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 411 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT MOD_RES 128 FT /note="Phosphoserine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" SQ SEQUENCE 457 AA; 50133 MW; 359C8CA8D578092D CRC64; MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLEAGARLTV NALTFIPQFT VWANEGMLTL VEGPFDETLL DSCWLAIAAT DDDTVNQRVS DAAESRRIFC NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPQH LGQVARYAGQ LRARVKKQFA TMGERRRFWE KFFVNDRLAQ SLANADEKAV NATTERLFSE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADIVVYDRL VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK GGDPFIFGRG GEELETLCHA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA QSVRLVTGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QEKLIAFGMQ ADMPVALVEN GTSVKQRVVH GVLTQLGELA QQVESPALII VGRVVGLRDK LNWFSNH //