ID   SUMT_PRIMG              Reviewed;         238 AA.
AC   P29928;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000305|PubMed:1906874};
DE            Short=Urogen III methylase;
DE            EC=2.1.1.107 {ECO:0000269|PubMed:1906874};
DE   AltName: Full=S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase {ECO:0000303|PubMed:1906874};
DE            Short=SUMT {ECO:0000303|PubMed:1906874};
DE   AltName: Full=Uroporphyrinogen III methylase;
DE            Short=UROM;
GN   Name=cobA {ECO:0000303|PubMed:1906874};
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, PATHWAY, AND SUBUNIT.
RC   STRAIN=ATCC 10778 / DSM 2894 / NCIMB 8508 / NRRL B-938;
RX   PubMed=1906874; DOI=10.1128/jb.173.15.4893-4896.1991;
RA   Robin C., Blanche F., Cauchois L., Cameron B., Couder M., Crouzet J.;
RT   "Primary structure, expression in Escherichia coli, and properties of S-
RT   adenosyl-L-methionine:uroporphyrinogen III methyltransferase from Bacillus
RT   megaterium.";
RL   J. Bacteriol. 173:4893-4896(1991).
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:0000269|PubMed:1906874}.
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:0000269|PubMed:1906874};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32460;
CC         Evidence={ECO:0000305|PubMed:1906874};
CC   -!- ACTIVITY REGULATION: SUMT exhibits a substrate inhibition phenomenon at
CC       uroporphyrinogen III concentrations above 0.5 uM; this property might
CC       play a regulatory role in cobalamin biosynthesis.
CC       {ECO:0000269|PubMed:1906874}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000305|PubMed:1906874}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000305|PubMed:1906874}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1906874}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M62881; AAA22317.1; -; Genomic_DNA.
DR   PIR; A42479; A42479.
DR   AlphaFoldDB; P29928; -.
DR   SMR; P29928; -.
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   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Methyltransferase; Porphyrin biosynthesis;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..238
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /id="PRO_0000150369"
FT   BINDING         11
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         170
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
SQ   SEQUENCE   238 AA;  25822 MW;  97993B56C894F307 CRC64;
     MGKVYLVGAG PGDPDLITLK GLKAIQQADV ILYDRLVNKD LLEYAKSDAD IIYCGKLPNY
     HTLKQETINN FLVKFAKKGK IVTRLKGGDP FVFGRGGEEA EALVQQGISF EIVPGITSGI
     AAAAYAGIPV THREYSASFA FVAGHRKDSK HDAIKWDSLA KGVDTLAIYM GVRNLPYICQ
     QLMKHGKTSA TPIALIHWGT CADQRTVTGT LGTIVDIVKE EQIENPSMII VGEVVNFS