SUMT_SYNE7
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 03-AUG-2022, entry version 122.
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}; OrderedLocusNames=Synpcc7942_0271;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; 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=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., 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}.
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DR EMBL; X70966; CAA50302.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB56303.1; -; Genomic_DNA.
DR RefSeq; WP_011243554.1; NC_007604.1.
DR AlphaFoldDB; P42451; -.
DR SMR; P42451; -.
DR STRING; 1140.Synpcc7942_0271; -.
DR PRIDE; P42451; -.
DR EnsemblBacteria; ABB56303; ABB56303; Synpcc7942_0271.
DR KEGG; syf:Synpcc7942_0271; -.
DR eggNOG; COG0007; Bacteria.
DR HOGENOM; CLU_011276_7_0_3; -.
DR OMA; QGVSFIT; -.
DR OrthoDB; 1185397at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0271-MON; -.
DR UniPathway; UPA00148; UER00211.
DR UniPathway; UPA00262; UER00211.
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 Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 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 Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 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 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
