ID A0A3A3KD82_SALMO Unreviewed; 457 AA. AC A0A3A3KD82; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 26-FEB-2020, entry version 12. 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}, DOA62_18105 GN {ECO:0000313|EMBL:EAA3557976.1}, E4933_11310 GN {ECO:0000313|EMBL:KAA7153371.1}, 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=473905 {ECO:0000313|EMBL:EAA3557976.1}, 64947 RC {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:KAA7153371.1, ECO:0000313|Proteomes:UP000322618} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ME2L-19-263 {ECO:0000313|EMBL:KAA7153371.1, RC ECO:0000313|Proteomes:UP000322618}; RX PubMed=31527278; DOI=.1073/pnas.1907787116; RA Rudman S.M., Greenblum S., Hughes R.C., Rajpurohit S., Kiratli O., RA Lowder D.B., Lemmon S.G., Petrov D.A., Chaston J.M., Schmidt P.; RT "Microbiome composition shapes rapid genomic adaptation of Drosophila RT melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 116:20025-20032(2019). RN [4] {ECO:0000313|EMBL:KAA7153371.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ME2L-19-263 {ECO:0000313|EMBL:KAA7153371.1}; RA Levent G., Schlochtermeier A., Ives S.E., Norman K.N., Lawhon S.D., RA Loneragan G.H., Anderson R.C., Scott H.M.; RL Submitted (MAR-2019) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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; AAABFP010000062; EAA3557976.1; -; Genomic_DNA. 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; SRBT01000004; KAA7153371.1; -; Genomic_DNA. DR RefSeq; WP_000349904.1; NZ_VCUN02000005.1. DR UniPathway; UPA00148; UER00222. DR UniPathway; UPA00262; UER00211. DR Proteomes; UP000322618; 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: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 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; 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 //