SUMT_METJA
ID SUMT_METJA Reviewed; 242 AA.
AC Q58375;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Uroporphyrinogen-III C-methyltransferase;
DE Short=Urogen III methylase;
DE EC=2.1.1.107 {ECO:0000250|UniProtKB:P29564};
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; Synonyms=corA; OrderedLocusNames=MJ0965;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(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 coenzyme F430.
CC {ECO:0000250|UniProtKB:P29564}.
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:P29564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32460;
CC Evidence={ECO:0000250|UniProtKB:P29564};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC precorrin-2 from uroporphyrinogen III: step 1/1.
CC {ECO:0000250|UniProtKB:P29564}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29564}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98967.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98967.1; ALT_INIT; Genomic_DNA.
DR PIR; E64420; E64420.
DR RefSeq; WP_064496681.1; NC_000909.1.
DR AlphaFoldDB; Q58375; -.
DR SMR; Q58375; -.
DR STRING; 243232.MJ_0965; -.
DR EnsemblBacteria; AAB98967; AAB98967; MJ_0965.
DR GeneID; 1451863; -.
DR KEGG; mja:MJ_0965; -.
DR eggNOG; arCOG00644; Archaea.
DR HOGENOM; CLU_011276_7_0_2; -.
DR InParanoid; Q58375; -.
DR OMA; TRPEQEE; -.
DR OrthoDB; 67633at2157; -.
DR PhylomeDB; Q58375; -.
DR UniPathway; UPA00148; UER00211.
DR Proteomes; UP000000805; 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..242
FT /note="Uroporphyrinogen-III C-methyltransferase"
FT /id="PRO_0000150371"
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 170
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
SQ SEQUENCE 242 AA; 26340 MW; BBE8388F036B6851 CRC64;
MTGKVILVGA GPGDPELITI KGLKAIKEAD VVVYDDLISK ELLNYAKKDA ELIYVGKRKG
KHSFKQEEIN KILVEKAKEG KLVVRLKGGD PFVFGRGGEE ILELKKHNIP YEVIPGITSA
IAVPEVAGIP VTHRKVATSF TVVTGHEAED KKEKQVDLSK LNADTIVILM GITNLENLVK
ELLQNPKRSK ETPVAIIMEG TTKNQRVIKG TLGDIVEKAK KENARPPGVI VVGEVVNVLD
SQ
