SUMT_METIV
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 03-AUG-2022, entry version 92.
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:MON-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 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; 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
