ID   SUMT_PSEAE              Reviewed;         245 AA.
AC   Q9I2W4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 118.
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=PA1778;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG05167.1; -; Genomic_DNA.
DR   PIR; H83423; H83423.
DR   RefSeq; NP_250469.1; NC_002516.2.
DR   RefSeq; WP_003087845.1; NZ_QZGE01000003.1.
DR   AlphaFoldDB; Q9I2W4; -.
DR   SMR; Q9I2W4; -.
DR   STRING; 208964.PA1778; -.
DR   PaxDb; 208964-PA1778; -.
DR   GeneID; 877770; -.
DR   KEGG; pae:PA1778; -.
DR   PATRIC; fig|208964.12.peg.1843; -.
DR   PseudoCAP; PA1778; -.
DR   HOGENOM; CLU_011276_7_0_6; -.
DR   InParanoid; Q9I2W4; -.
DR   OrthoDB; 9815856at2; -.
DR   PhylomeDB; Q9I2W4; -.
DR   BioCyc; PAER208964:G1FZ6-1809-MONOMER; -.
DR   UniPathway; UPA00148; UER00211.
DR   UniPathway; UPA00262; UER00211.
DR   Proteomes; UP000002438; 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   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.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; Porphyrin biosynthesis;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..245
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /id="PRO_0000287818"
FT   BINDING         12
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         87..89
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         168
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         197
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         225
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
SQ   SEQUENCE   245 AA;  25925 MW;  7BB11C9942E56F7F CRC64;
     MSGKVWLVGA GPGDPELLTL KAVRALQDAD VVMVDDLVNP SILEHCPSAR LVRVGKRGGC
     RSTPQDFIQR LMLRHARQGR SVVRLKGGDP CIFGRAGEEA EWLARHGIDS EIVNGITAGL
     AGATACGIPL TYRGISRGVT LVTAHTQDDS PLAWEALARS GTTLVVYMGV ARLAEIQAGL
     LAGGMAEDTP LAMIENATLG NQRECRSNLG ELLRDAGRFA LKSPAILVIG EVTRDIVSQP
     ISLSA
//