ID SUMT_SYNE7 Reviewed; 243 AA. AC P42451; Q31RL6; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=Uroporphyrinogen-III C-methyltransferase; DE Short=Urogen III methylase; DE EC=2.1.1.107 {ECO:0000250|UniProtKB:P21631}; DE AltName: Full=S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase; DE Short=SUMT; DE AltName: Full=Uroporphyrinogen III methylase {ECO:0000303|PubMed:8123787}; DE Short=UROM {ECO:0000303|PubMed:8123787}; GN Name=cobA {ECO:0000303|PubMed:8123787}; GN OrderedLocusNames=Synpcc7942_0271; OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8123787; DOI=10.1007/bf00024112; RA Jones M.C., Jenkins J.M., Smith A.G., Howe C.J.; RT "Cloning and characterisation of genes for tetrapyrrole biosynthesis from RT the cyanobacterium Anacystis nidulans R2."; RL Plant Mol. Biol. 24:435-448(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Golden S., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the two successive C-2 and C-7 methylation CC reactions involved in the conversion of uroporphyrinogen III to CC precorrin-2 via the intermediate formation of precorrin-1. It is a step CC in the biosynthesis of both cobalamin (vitamin B12) and siroheme. CC {ECO:0000250|UniProtKB:P21631}. 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:0000250|UniProtKB:P21631}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32460; CC Evidence={ECO:0000250|UniProtKB:P21631}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC precorrin-2 from uroporphyrinogen III: step 1/1. CC {ECO:0000250|UniProtKB:P21631}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. CC {ECO:0000250|UniProtKB:P21631}. CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family. CC {ECO:0000305}. 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; X70966; CAA50302.1; -; Genomic_DNA. DR EMBL; CP000100; ABB56303.1; -; Genomic_DNA. DR RefSeq; WP_011243554.1; NZ_JACJTX010000002.1. DR AlphaFoldDB; P42451; -. DR SMR; P42451; -. DR STRING; 1140.Synpcc7942_0271; -. DR PaxDb; 1140-Synpcc7942_0271; -. DR GeneID; 76399018; -. DR KEGG; syf:Synpcc7942_0271; -. DR eggNOG; COG0007; Bacteria. DR HOGENOM; CLU_011276_7_0_3; -. DR OrthoDB; 9815856at2; -. DR BioCyc; SYNEL:SYNPCC7942_0271-MONOMER; -. DR UniPathway; UPA00148; UER00211. DR UniPathway; UPA00262; UER00211. DR Proteomes; UP000889800; Chromosome. DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd11642; SUMT; 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; IPR003043; Uropor_MeTrfase_CS. DR NCBIfam; TIGR01469; cobA_cysG_Cterm; 1. DR PANTHER; PTHR45790:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1. DR Pfam; PF00590; TP_methylase; 1. DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1. DR PROSITE; PS00839; SUMT_1; 1. DR PROSITE; PS00840; SUMT_2; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Methyltransferase; Porphyrin biosynthesis; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..243 FT /note="Uroporphyrinogen-III C-methyltransferase" FT /id="PRO_0000150374" FT BINDING 12 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000250|UniProtKB:P21631" FT BINDING 88..90 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000250|UniProtKB:P21631" FT BINDING 118..119 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000250|UniProtKB:P21631" FT BINDING 166 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000250|UniProtKB:P21631" FT BINDING 195 FT /ligand="S-adenosyl-L-homocysteine" FT /ligand_id="ChEBI:CHEBI:57856" FT /evidence="ECO:0000250|UniProtKB:P21631" SQ SEQUENCE 243 AA; 26463 MW; 9E11AA90724A9870 CRC64; MTGKVYLVGA GPGDPEYLTL QAQQCLQSAE VLIYDALIDP RILDLVPANC DRIAVGKRGG AESTPQATIN QLLVEHCQQG RKVIRLKSGD PFVFGRAASE LDALERSGCD YAVLPGLSTA LAAPLLAGIP ITDPVLSRGF AVYTVHEPDA LNWEALAQLE TLILLMGSRH LLTIGHELIR HGRSPDSPVA LIQWAGHPQQ TVLESSLSRM AQQWGDQPLS PCVIVIGEVV RLRKYWAHYR YDG //