ID   SUMT_METIV              Reviewed;         231 AA.
AC   P29564;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-SEP-2023, entry version 95.
DE   RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000305|PubMed:1856165};
DE            Short=Urogen III methylase;
DE            EC=2.1.1.107 {ECO:0000269|PubMed:1856165};
DE   AltName: Full=S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase {ECO:0000303|PubMed:1856165};
DE            Short=SUMT {ECO:0000303|PubMed:1856165};
DE   AltName: Full=Uroporphyrinogen III methylase;
DE            Short=UROM;
GN   Name=cobA; Synonyms=corA {ECO:0000303|PubMed:1856165};
OS   Methanobacterium ivanovii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=2163;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31 AND 201-212,
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, SUBUNIT, AND PATHWAY.
RC   STRAIN=DSM 2611;
RX   PubMed=1856165; DOI=10.1128/jb.173.15.4637-4645.1991;
RA   Blanche F., Robin C., Couder M., Faucher D., Cauchois L., Cameron B.,
RA   Crouzet J.;
RT   "Purification, characterization, and molecular cloning of S-adenosyl-L-
RT   methionine: uroporphyrinogen III methyltransferase from Methanobacterium
RT   ivanovii.";
RL   J. Bacteriol. 173:4637-4645(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 coenzyme F430.
CC       {ECO:0000269|PubMed:1856165}.
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:1856165};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32460;
CC         Evidence={ECO:0000305|PubMed:1856165};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uroporphyrinogen III = H(+) +
CC         precorrin-1 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19089,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58893, ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000269|PubMed:1856165};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19090;
CC         Evidence={ECO:0000305|PubMed:1856165};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=precorrin-1 + S-adenosyl-L-methionine = precorrin-2 + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:21972, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58827, ChEBI:CHEBI:58893, ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000269|PubMed:1856165};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21973;
CC         Evidence={ECO:0000305|PubMed:1856165};
CC   -!- ACTIVITY REGULATION: Does not show substrate inhibition at
CC       uroporphyrinogen III concentrations of up to 20 uM, in contrast to SUMT
CC       from Sinorhizobium (previously believed to be P.denitrificans).
CC       {ECO:0000269|PubMed:1856165}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=52 nM for uroporphyrinogen III {ECO:0000269|PubMed:1856165};
CC         Vmax=1537 umol/min/mg enzyme {ECO:0000269|PubMed:1856165};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000305|PubMed:1856165}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1856165}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M62874; AAA72997.1; -; Genomic_DNA.
DR   PIR; A42471; A42471.
DR   AlphaFoldDB; P29564; -.
DR   SMR; P29564; -.
DR   BioCyc; MetaCyc:MONOMER-12172; -.
DR   BRENDA; 2.1.1.107; 13650.
DR   SABIO-RK; P29564; -.
DR   UniPathway; UPA00148; 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:InterPro.
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.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Direct protein sequencing; Methyltransferase;
KW   Porphyrin biosynthesis; S-adenosyl-L-methionine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1856165"
FT   CHAIN           2..231
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /id="PRO_0000150370"
FT   BINDING         10
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         85..87
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         115..116
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         218
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
SQ   SEQUENCE   231 AA;  24916 MW;  6EB100DAA96EB37A CRC64;
     MVVYLVGAGP GDPELITLKA VNVLKKADVV LYDKPANEEI LKYAEGAKLI YVGKQAGHHY
     KSQNEINTLL VEEAKENDLV VRLKGGDPFV FGRGGEEILA LVEEGIDFEL VPGVTSAIGV
     PTTIGLPVTH RGVATSFTVV TGHEDPTKCK KQVGWDFKAD TIVILMGIGN LAENTAEIMK
     HKDPETPVCV IENGTMEGQR IITGTLENIA GKDIKPPALV VLEMLSMFLK K
//