ID   COBM_SINSX              Reviewed;         253 AA.
AC   P21922;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Precorrin-4 C(11)-methyltransferase;
DE            EC=2.1.1.133;
DE   AltName: Full=Precorrin-3 methylase;
GN   Name=cobM;
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].
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).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=8226690; DOI=10.1128/jb.175.22.7430-7440.1993;
RA   Debussche L., Thibaut D., Cameron B., Crouzet J., Blanche F.J.;
RT   "Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas
RT   denitrificans.";
RL   J. Bacteriol. 175:7430-7440(1993).
CC   -!- FUNCTION: Catalyzes the methylation of C-11 in precorrin-4 to form
CC       precorrin-5.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=precorrin-4 + S-adenosyl-L-methionine = precorrin-5 + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:22012, ChEBI:CHEBI:57769,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77871;
CC         EC=2.1.1.133;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 4/10.
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; AAA25801.1; -; Genomic_DNA.
DR   AlphaFoldDB; P21922; -.
DR   SMR; P21922; -.
DR   KEGG; ag:AAA25801; -.
DR   BioCyc; MetaCyc:MON-86; -.
DR   UniPathway; UPA00148; UER00215.
DR   GO; GO:0046026; F:precorrin-4 C11-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; cd11641; Precorrin-4_C11-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; IPR006362; Cbl_synth_CobM/CibF.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR01465; cobM_cbiF; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..253
FT                   /note="Precorrin-4 C(11)-methyltransferase"
FT                   /id="PRO_0000150395"
SQ   SEQUENCE   253 AA;  26863 MW;  50F5E6F5F67FF733 CRC64;
     MTVHFIGAGP GAADLITVRG RDLIGRCPVC LYAGSIVSPE LLRYCPPGAR IVDTAPMSLD
     EIEAEYVKAE AEGLDVARLH SGDLSVWSAV AEQIRRLEKH GIAYTMTPGV PSFAAAASAL
     GRELTIPAVA QSLVLTRVSG RASPMPNSET LSAFGATGST LAIHLAIHAL QQVVEELTPL
     YGADCPVAIV VKASWPDERV VRGTLGDIAA KVAEEPIERT ALIFVGPGLE ASDFRESSLY
     DPAYQRRFRG RGE