ID A0A0T9XSH3_SALET Unreviewed; 457 AA. AC A0A0T9XSH3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-NOV-2018, entry version 31. DE RecName: Full=Siroheme synthase {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}; 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}; GN Name=cysG {ECO:0000256|HAMAP-Rule:MF_01646, GN ECO:0000313|EMBL:CNU86473.1}; GN ORFNames=ERS008202_03718 {ECO:0000313|EMBL:CNU86473.1}, GN ERS008207_04139 {ECO:0000313|EMBL:CNV04810.1}, 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:CNU86473.1, ECO:0000313|Proteomes:UP000039541}; 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}; RA Murphy D.; 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. CC -!- FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent CC methylations of uroporphyrinogen III at position C-2 and C-7 to CC form precorrin-2 via precorrin-1. Then it catalyzes the NAD- CC dependent ring dehydrogenation of precorrin-2 to yield CC sirohydrochlorin. Finally, it catalyzes the ferrochelation of CC sirohydrochlorin to yield siroheme. {ECO:0000256|HAMAP- CC Rule:MF_01646, ECO:0000256|SAAS:SAAS00971394}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + uroporphyrinogen CC III = 2 S-adenosyl-L-homocysteine + precorrin-2. CC {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00970331}. CC -!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin + CC NADH. {ECO:0000256|HAMAP-Rule:MF_01646, CC ECO:0000256|SAAS:SAAS01024975}. CC -!- CATALYTIC ACTIVITY: Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+). CC {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS01024976}. 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; UGVQ01000002; SUE45696.1; -; Genomic_DNA. DR RefSeq; WP_000349896.1; NZ_UGVQ01000002.1. 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 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: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 Complete proteome {ECO:0000313|Proteomes:UP000039541, KW ECO:0000313|Proteomes:UP000042394, ECO:0000313|Proteomes:UP000254190}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|SAAS:SAAS01024979}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00099290}; 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:CNU86473.1}; 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:SAAS00099242}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01646, KW ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00099286}. FT DOMAIN 119 145 Sirohm_synth_M. {ECO:0000259|Pfam: FT PF14824}. FT DOMAIN 150 207 CysG_dimeriser. {ECO:0000259|Pfam: FT PF10414}. FT DOMAIN 218 426 TP_methylase. {ECO:0000259|Pfam:PF00590}. FT NP_BIND 22 23 NAD. {ECO:0000256|HAMAP-Rule:MF_01646}. FT NP_BIND 43 44 NAD. {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 1 204 precorrin-2 dehydrogenase / FT sirohydrochlorin ferrochelatase. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 216 457 Uroporphyrinogen-III C-methyltransferase. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 301 303 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT REGION 331 332 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT COILED 185 205 {ECO:0000256|SAM:Coils}. FT ACT_SITE 248 248 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01646, ECO:0000256|PIRSR:PIRSR036426- FT 1}. FT ACT_SITE 270 270 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_01646, ECO:0000256|PIRSR:PIRSR036426- FT 1}. FT BINDING 225 225 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 306 306 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 382 382 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_01646}. FT BINDING 411 411 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01646}. FT MOD_RES 128 128 Phosphoserine. {ECO:0000256|HAMAP-Rule: FT 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 //