ID A0A3A3KD82_SALMO Unreviewed; 457 AA. AC A0A3A3KD82; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 18-SEP-2019, entry version 8. 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=cobA {ECO:0000313|EMBL:EAA5755080.1}; GN Synonyms=cysG {ECO:0000256|HAMAP-Rule:MF_01646}; GN ORFNames=AAN00_09060 {ECO:0000313|EMBL:EAB5747702.1}, AXU21_23170 GN {ECO:0000313|EMBL:EAA9237225.1}, AXU38_13655 GN {ECO:0000313|EMBL:EAA5755080.1}, CM22_11685 GN {ECO:0000313|EMBL:EAA7519904.1}, CVB19_01830 GN {ECO:0000313|EMBL:EAA8532710.1}, FG488_05840 GN {ECO:0000313|EMBL:TOS71526.1}, FG720_14190 GN {ECO:0000313|EMBL:TOT75366.1}, FG734_04960 GN {ECO:0000313|EMBL:TOT40521.1}, QB52_09305 GN {ECO:0000313|EMBL:EAA7131451.1}, UK00_22635 GN {ECO:0000313|EMBL:EAA8125631.1}, XU87_13655 GN {ECO:0000313|EMBL:EAA9554405.1}; OS Salmonella montevideo. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=115981 {ECO:0000313|EMBL:EAA5755080.1}; RN [1] {ECO:0000313|EMBL:EAA5755080.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ADRDL-1578 {ECO:0000313|EMBL:EAA8532710.1}, CFSAN004243 RC {ECO:0000313|EMBL:EAA8125631.1}, CFSAN032150 RC {ECO:0000313|EMBL:EAA9237225.1}, CFSAN032167 RC {ECO:0000313|EMBL:EAA5755080.1}, MDH-2014-00193 RC {ECO:0000313|EMBL:EAA7519904.1}, and NY-N13154 RC {ECO:0000313|EMBL:EAA9554405.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAA7131451.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=64947 {ECO:0000313|EMBL:EAB5747702.1}, and H120360356 RC {ECO:0000313|EMBL:EAA7131451.1}; 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. RN [3] {ECO:0000313|EMBL:TOS71526.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIY0203 {ECO:0000313|EMBL:TOT75366.1}, HIY0226 RC {ECO:0000313|EMBL:TOT40521.1}, and HIY0283 RC {ECO:0000313|EMBL:TOS71526.1}; RX PubMed=30902850; RA Diemert S., Yan T.; RT "Clinically Unreported Salmonellosis Outbreak Detected via Comparative RT Genomic Analysis of Municipal Wastewater Salmonella Isolates."; RL Appl. Environ. Microbiol. 85:e00139-19(2019). 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: 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; CC EC=1.3.1.76; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAA5755080.1}. 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; AAABXU010000007; EAA5755080.1; -; Genomic_DNA. DR EMBL; AAACJZ010000006; EAA7131451.1; -; Genomic_DNA. DR EMBL; AAACMB010000004; EAA7519904.1; -; Genomic_DNA. DR EMBL; AAACQX010000028; EAA8125631.1; -; Genomic_DNA. DR EMBL; AAACTW010000002; EAA8532710.1; -; Genomic_DNA. DR EMBL; AAACZB010000023; EAA9237225.1; -; Genomic_DNA. DR EMBL; AAADCM010000006; EAA9554405.1; -; Genomic_DNA. DR EMBL; AAAFDE010000006; EAB5747702.1; -; Genomic_DNA. DR EMBL; VCTO01000003; TOS71526.1; -; Genomic_DNA. DR EMBL; VCUH01000002; TOT40521.1; -; Genomic_DNA. DR EMBL; VCUN01000005; TOT75366.1; -; Genomic_DNA. DR RefSeq; WP_000349904.1; NZ_UGVP01000002.1. DR UniPathway; UPA00148; UER00222. DR UniPathway; UPA00262; UER00211. 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 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:SAAS00467449, KW ECO:0000313|EMBL:EAA5755080.1}; 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}; 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:EAA5755080.1}. 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; 50128 MW; 5B2A57B48D62A3AF CRC64; MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLEAGARLTV NALTFIPQFT VWANEGMLTL VEGPFDETLL DSCWLAIAAT DDDTVNQRVS EAAESRRIFC NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPQH LGQVARYAGQ LRARVKKQFA TMGERRRFWE KFFVNDRLAQ SLANADEKAV NATTEHLFSE 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 //