ID A0A0T9XSH3_SALET Unreviewed; 457 AA. AC A0A0T9XSH3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 22-APR-2020, entry version 42. 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:EBR9036564.1}; GN ORFNames=A3789_22195 {ECO:0000313|EMBL:ECU6653166.1}, AL561_21920 GN {ECO:0000313|EMBL:ECW9499245.1}, AVB48_23795 GN {ECO:0000313|EMBL:EBV8404472.1}, B7N00_17765 GN {ECO:0000313|EMBL:EDG5018796.1}, B7N01_22860 GN {ECO:0000313|EMBL:EDG4997244.1}, B7N34_07200 GN {ECO:0000313|EMBL:EDG5152717.1}, B7N35_03805 GN {ECO:0000313|EMBL:EDG5125156.1}, B7N60_09345 GN {ECO:0000313|EMBL:EBW1389355.1}, B7N72_07840 GN {ECO:0000313|EMBL:EDG5370017.1}, B7N78_06830 GN {ECO:0000313|EMBL:EDG5279492.1}, B7N79_22455 GN {ECO:0000313|EMBL:EDG5295682.1}, B7N80_01670 GN {ECO:0000313|EMBL:EDG5287099.1}, B7N84_22475 GN {ECO:0000313|EMBL:EDG5269097.1}, B7N95_10635 GN {ECO:0000313|EMBL:EBW9311316.1}, CAD68_22700 GN {ECO:0000313|EMBL:ECS6729423.1}, CBK57_12055 GN {ECO:0000313|EMBL:ECS6796805.1}, DK062_22460 GN {ECO:0000313|EMBL:EBU7446472.1}, DP779_23750 GN {ECO:0000313|EMBL:EBS4177298.1}, DPA33_23350 GN {ECO:0000313|EMBL:EBR9036564.1}, DPK57_18130 GN {ECO:0000313|EMBL:EBW4419427.1}, DPS13_08175 GN {ECO:0000313|EMBL:EBS4100180.1}, DPZ52_08960 GN {ECO:0000313|EMBL:EBS4193368.1}, 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}, EWF75_22415 GN {ECO:0000313|EMBL:ECB3324869.1}, EXP31_04405 GN {ECO:0000313|EMBL:ECB4582461.1}, NCTC5754_00479 GN {ECO:0000313|EMBL:SUE45696.1}; OS Salmonella enterica subsp. enterica serovar Bovismorbificans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE45696.1, ECO:0000313|Proteomes:UP000254190}; RN [1] {ECO:0000313|EMBL:CNU86473.1, 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: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 [3] {ECO:0000313|EMBL:EBR9036564.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=135059 {ECO:0000313|EMBL:ECW9499245.1}, 136768 RC {ECO:0000313|EMBL:EDG4997244.1}, 138330 RC {ECO:0000313|EMBL:EDG5287099.1}, 143652 RC {ECO:0000313|EMBL:EDG5370017.1}, 232714 RC {ECO:0000313|EMBL:EDG5295682.1}, 273631 RC {ECO:0000313|EMBL:EDG5018796.1}, 299804 RC {ECO:0000313|EMBL:EDG5152717.1}, 329869 RC {ECO:0000313|EMBL:EBW1389355.1}, 330535 RC {ECO:0000313|EMBL:EDG5269097.1}, 333944 RC {ECO:0000313|EMBL:EDG5279492.1}, 337042 RC {ECO:0000313|EMBL:EDG5125156.1}, 337073 RC {ECO:0000313|EMBL:EBW9311316.1}, 364560 RC {ECO:0000313|EMBL:EBR9036564.1}, 372681 RC {ECO:0000313|EMBL:ECB4582461.1}, 387147 RC {ECO:0000313|EMBL:EBS2452198.1}, 449715 RC {ECO:0000313|EMBL:ECB3324869.1}, 470200 RC {ECO:0000313|EMBL:ECE8535249.1}, 478619 RC {ECO:0000313|EMBL:EBS4177298.1}, 511816 RC {ECO:0000313|EMBL:EBS4100180.1}, 513486 RC {ECO:0000313|EMBL:EBS4193368.1}, 513487 RC {ECO:0000313|EMBL:EBW4419427.1}, 520500 RC {ECO:0000313|EMBL:EBU7446472.1}, 598023 RC {ECO:0000313|EMBL:ECA2724100.1, ECO:0000313|Proteomes:UP000424060}, RC 692616 {ECO:0000313|EMBL:ECF1448880.1}, and 77325 RC {ECO:0000313|EMBL:EBV8404472.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ECS6729423.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PNUSAS011130 {ECO:0000313|EMBL:ECS6729423.1}, and PNUSAS013377 RC {ECO:0000313|EMBL:ECS6796805.1}; RG PulseNet: The National Subtyping Network for Foodborne Disease Surveillance; RA Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S., RA Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:ECU6653166.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSIS1606031 {ECO:0000313|EMBL:ECU6653166.1}; RG NARMS: The National Antimicrobial Resistance Monitoring System; 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, ECO:0000256|SAAS:SAAS00971394}. 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 ECO:0000256|SAAS:SAAS01123671}; 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 ECO:0000256|SAAS:SAAS01116480}; 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|HAMAP-Rule:MF_01646, CC ECO:0000256|SAAS:SAAS01123666}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01646, ECO:0000256|SAAS:SAAS01024981}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00971402}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; siroheme from sirohydrochlorin: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS01024978}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS01024982}. CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family. CC {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 ECO:0000256|SAAS:SAAS00971398}. CC -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2 CC dehydrogenase / sirohydrochlorin ferrochelatase family. CC {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00971404}. 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; AAGTUA010000034; EBR9036564.1; -; Genomic_DNA. DR EMBL; AAGUWJ010000004; EBS2452198.1; -; Genomic_DNA. DR EMBL; AAGVJX010000006; EBS4100180.1; -; Genomic_DNA. DR EMBL; AAGVKZ010000134; EBS4177298.1; -; Genomic_DNA. DR EMBL; AAGVKX010000040; EBS4193368.1; -; Genomic_DNA. DR EMBL; AAHDAE010000035; EBU7446472.1; -; Genomic_DNA. DR EMBL; AAHGNB010000039; EBV8404472.1; -; Genomic_DNA. DR EMBL; AAHHLN010000004; EBW1389355.1; -; Genomic_DNA. DR EMBL; AAHIIT010000059; EBW4419427.1; -; Genomic_DNA. DR EMBL; AAHJRS010000005; EBW9311316.1; -; Genomic_DNA. DR EMBL; AAHTVM010000024; ECA2724100.1; -; Genomic_DNA. DR EMBL; AAHXFT010000035; ECB3324869.1; -; Genomic_DNA. DR EMBL; AAHXQG010000002; ECB4582461.1; -; Genomic_DNA. DR EMBL; AAIJHK010000002; ECE8535249.1; -; Genomic_DNA. DR EMBL; AAIKGE010000028; ECF1448880.1; -; Genomic_DNA. DR EMBL; AAKKIF010000024; ECS6729423.1; -; Genomic_DNA. DR EMBL; AAKKIU010000004; ECS6796805.1; -; Genomic_DNA. DR EMBL; AAKQQO010000019; ECU6653166.1; -; Genomic_DNA. DR EMBL; AAKYDU010000047; ECW9499245.1; -; 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; AAMELF010000003; EDG5152717.1; -; 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; AAMEMM010000028; EDG5295682.1; -; Genomic_DNA. DR EMBL; AAMEMP010000005; EDG5370017.1; -; Genomic_DNA. DR EMBL; UGVQ01000002; SUE45696.1; -; Genomic_DNA. DR RefSeq; WP_000349896.1; NZ_WFIN01000005.1. DR SMR; A0A0T9XSH3; -. DR EnsemblBacteria; CFW73352; CFW73352; ERS008215_02382. DR EnsemblBacteria; CNU86473; CNU86473; ERS008202_03718. DR EnsemblBacteria; CNV04810; CNV04810; ERS008207_04139. DR EnsemblBacteria; CPR44771; CPR44771; ERS008210_01062. DR UniPathway; UPA00148; UER00222. DR UniPathway; UPA00262; UER00211. DR Proteomes; UP000039541; Unassembled WGS sequence. DR Proteomes; UP000042394; Unassembled WGS sequence. DR Proteomes; UP000254190; Unassembled WGS sequence. DR Proteomes; UP000424060; 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; 1.10.8.210; -; 1. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 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 Pfam; PF10414; CysG_dimeriser; 1. DR Pfam; PF14824; Sirohm_synth_M; 1. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF036426; Sirohaem_synth; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1. DR TIGRFAMs; TIGR01470; cysG_Nterm; 1. DR PROSITE; PS00839; SUMT_1; 1. DR PROSITE; PS00840; SUMT_2; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS01024974}; Coiled coil {ECO:0000256|SAM:Coils}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS01024979}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00467449, KW ECO:0000313|EMBL:EBR9036564.1}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS01024984}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS01024985}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS01024988, ECO:0000313|EMBL:SUE45696.1}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01646}; KW Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS01024977}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS00467481}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00467429, KW ECO:0000313|EMBL:EBR9036564.1}. FT DOMAIN 119..145 FT /note="Sirohm_synth_M" FT /evidence="ECO:0000259|Pfam:PF14824" FT DOMAIN 150..207 FT /note="CysG_dimeriser" FT /evidence="ECO:0000259|Pfam:PF10414" FT DOMAIN 218..426 FT /note="TP_methylase" FT /evidence="ECO:0000259|Pfam:PF00590" FT NP_BIND 22..23 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT NP_BIND 43..44 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" 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 REGION 301..303 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT REGION 331..332 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT COILED 185..205 FT /evidence="ECO:0000256|SAM:Coils" 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 225 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 306 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 382 FT /note="S-adenosyl-L-methionine; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01646" FT BINDING 411 FT /note="S-adenosyl-L-methionine; via amide nitrogen and FT carbonyl oxygen" 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 //