ID   SUMT_PSEFL              Reviewed;         247 AA.
AC   P37725;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 88.
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 {ECO:0000303|PubMed:7959054};
DE            Short=SUMT {ECO:0000303|PubMed:7959054};
DE   AltName: Full=Uroporphyrinogen III methylase;
DE            Short=UROM;
GN   Name=cobA {ECO:0000303|PubMed:7959054};
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OE 28.3;
RX   PubMed=7959054; DOI=10.1016/0378-1119(94)90886-9;
RA   de Mot R., Schoofs G., Nagy I., Vanderleyden J.;
RT   "Sequence of the cobA gene encoding S-adenosyl-L-methionine:
RT   uroporhyrinogen III methyltransferase of Pseudomonas fluorescens.";
RL   Gene 150:199-200(1994).
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; AF115334; AAD45977.1; -; Genomic_DNA.
DR   AlphaFoldDB; P37725; -.
DR   SMR; P37725; -.
DR   STRING; 690597.JH730914_gene3693; -.
DR   eggNOG; COG0007; Bacteria.
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..247
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /id="PRO_0000150373"
FT   BINDING         12
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   247 AA;  26062 MW;  E4BE93D60A629D79 CRC64;
     MSAKVWLVGA GPGDPELLTL KAVRALHAAD VVLIDDLVNP RVLEHCPDAR VITVGKRGGC
     RSTPQDFIHR LMLAMRAKAN AWCDLRAATP CIFGRGGEEA LWLRERGVEV ELVNGITAGL
     AGATNCDIPL TLRGVSRGVT LVTAHTQDDS SLNWRALAEG GTTLVVYMGV AKLEEIRQQL
     LEGAMAADTP VAMIENASLP QQRECRSTLA HMHTDAQVFA LKSPAILVIG SVAGAGQAAS
     ITVSASA