ID A0A3Z6P493_SALTU Unreviewed; 457 AA. AC A0A3Z6P493; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 29-SEP-2021, entry version 14. 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:AEF09312.1}; GN OrderedLocusNames=STMUK_3463 {ECO:0000313|EMBL:AEF09312.1}; OS Salmonella typhimurium (strain ATCC 68169 / UK-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=990282 {ECO:0000313|EMBL:AEF09312.1, ECO:0000313|Proteomes:UP000008278}; RN [1] {ECO:0000313|EMBL:AEF09312.1, ECO:0000313|Proteomes:UP000008278} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 68169 / UK-1 {ECO:0000313|Proteomes:UP000008278}; RX PubMed=21622747; DOI=10.1128/JB.05224-11; RA Luo Y., Kong Q., Yang J., Golden G., Wanda S.Y., Jensen R.V., Ernst P.B., RA Curtiss R.III.; RT "Complete genome sequence of the universal killer Salmonella enterica RT serovar typhimurium UK-1 (ATCC 68169)."; RL J. Bacteriol. 193:4035-4036(2011). 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; 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; CP002614; AEF09312.1; -; Genomic_DNA. DR RefSeq; WP_000349895.1; NC_016863.1. DR SMR; A0A3Z6P493; -. DR KEGG; sej:STMUK_3463; -. DR UniPathway; UPA00148; UER00211. DR UniPathway; UPA00262; UER00222. DR Proteomes; UP000008278; Chromosome. 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|ARBA:ARBA00022573, ECO:0000256|HAMAP- KW Rule:MF_01646}; Coiled coil {ECO:0000256|SAM:Coils}; 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="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; 50147 MW; 359C8CAF4B78092D 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 VGRVVALRDK LNWFSNH //