ID   COBI_SINSX              Reviewed;         245 AA.
AC   P21639;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Precorrin-2 C(20)-methyltransferase;
DE            EC=2.1.1.130;
DE   AltName: Full=S-adenosyl-L-methionine--precorrin-2 methyltransferase;
DE            Short=SP2MT;
GN   Name=cobI;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-18.
RC   STRAIN=SC510;
RX   PubMed=2211521; DOI=10.1128/jb.172.10.5980-5990.1990;
RA   Crouzet J., Cameron B., Cauchois L., Rigault S., Rouyez M.-C., Blanche F.,
RA   Thibaut D., Debussche L.;
RT   "Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans
RT   fragment carrying eight genes involved in transformation of precorrin-2 to
RT   cobyrinic acid.";
RL   J. Bacteriol. 172:5980-5990(1990).
CC   -!- FUNCTION: Methylates precorrin-2 at the C-20 position to produce
CC       precorrin-3A.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=precorrin-2 + S-adenosyl-L-methionine = H(+) + precorrin-3A +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16841, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58561, ChEBI:CHEBI:58827,
CC         ChEBI:CHEBI:59789; EC=2.1.1.130;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 1/10.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
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DR   EMBL; M59301; AAA25797.1; -; Genomic_DNA.
DR   AlphaFoldDB; P21639; -.
DR   SMR; P21639; -.
DR   PRIDE; P21639; -.
DR   BioCyc; MetaCyc:MON-83; -.
DR   UniPathway; UPA00148; UER00212.
DR   GO; GO:0030788; F:precorrin-2 C20-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   CDD; cd11645; Precorrin_2_C20_MT; 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; IPR012382; CobI/CbiL.
DR   InterPro; IPR006364; CobI/CbiL/CobIJ_dom.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036427; Precrrn-2_mtase; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR01467; cobI_cbiL; 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   S-adenosyl-L-methionine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2211521"
FT   CHAIN           2..245
FT                   /note="Precorrin-2 C(20)-methyltransferase"
FT                   /id="PRO_0000150389"
SQ   SEQUENCE   245 AA;  25895 MW;  1F4A0C847C90E324 CRC64;
     MSGVGVGRLI GVGTGPGDPE LLTVKAVKAL GQADVLAYFA KAGRSGNGRA VVEGLLKPDL
     VELPLYYPVT TEIDKDDGAY KTQITDFYNA SAEAVAAHLA AGRTVAVLSE GDPLFYGSYM
     HLHVRLANRF PVEVIPGITA MSGCWSLAGL PLVQGDDVLS VLPGTMAEAE LGRRLADTEA
     AVIMKVGRNL PKIRRALAAS GRLDQAVYVE RGTMKNAAMT ALAEKADDEA PYFSLVLVPG
     WKDRP