SUMT_SYNY3
ID SUMT_SYNY3 Reviewed; 263 AA.
AC Q55749;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
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;
DE Short=UROM;
GN Name=cobA; OrderedLocusNames=sll0378;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA10394.1; -; Genomic_DNA.
DR PIR; S76548; S76548.
DR AlphaFoldDB; Q55749; -.
DR SMR; Q55749; -.
DR STRING; 1148.1001660; -.
DR PaxDb; Q55749; -.
DR EnsemblBacteria; BAA10394; BAA10394; BAA10394.
DR KEGG; syn:sll0378; -.
DR eggNOG; COG0007; Bacteria.
DR InParanoid; Q55749; -.
DR OMA; TRPEQEE; -.
DR PhylomeDB; Q55749; -.
DR UniPathway; UPA00148; UER00211.
DR UniPathway; UPA00262; UER00211.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..263
FT /note="Uroporphyrinogen-III C-methyltransferase"
FT /id="PRO_0000150375"
FT BINDING 20
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 96..98
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 126..127
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 180
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 237
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
SQ SEQUENCE 263 AA; 27833 MW; 581847CFF32C7BDE CRC64;
MVVRLQNGLM GKVYLVGAGP GDPGLITVKG KTLLENAEAV VYDALVSTAI LAMVNPQAEL
IDAGKRRGRH TKLQSETTQL LAQLAEKHAV VVRLKGGDPF IFGRGGEEME DLVKAGIEVE
VVPGITAGIA APAYAQIPLT HRAYSSSVTF VTGHESAGKY RPEVNWAAIA KGSETIVIYM
GVYSLATILP QLMLAGLGED TPIALIRWGT CPEQQKLVGT FATILAQIEV ENFQAPAIVV
IGAVVNYPAN LRQQLAPILG GVN
