ID   COBM_RHOER              Reviewed;         249 AA.
AC   Q53138;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Precorrin-4 C(11)-methyltransferase;
DE            EC=2.1.1.133;
DE   AltName: Full=Precorrin-3 methylase;
GN   Name=cobM;
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NI86/21;
RX   PubMed=8200543; DOI=10.1016/0378-1119(94)90610-6;
RA   de Mot R., Nagy I., Schoofs G., Vanderleyden J.;
RT   "Sequences of the cobalamin biosynthetic genes cobK, cobL and cobM from
RT   Rhodococcus sp. NI86/21.";
RL   Gene 143:91-93(1994).
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}.
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DR   EMBL; L21196; AAC37130.1; -; Genomic_DNA.
DR   PIR; T46836; T46836.
DR   AlphaFoldDB; Q53138; -.
DR   SMR; Q53138; -.
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   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..249
FT                   /note="Precorrin-4 C(11)-methyltransferase"
FT                   /id="PRO_0000150398"
SQ   SEQUENCE   249 AA;  25963 MW;  62C069692E178148 CRC64;
     MTVYFIGAGP GAADLITVRA QRIIAASPVC LYAGSLVPQE LLAECPEGAR VIDTARLSLD
     EIVALLIEAD AAGQDVARLH SGDPSIFSAV AEQVRRLESA GVAYQVVPGV PAFTAAAASL
     GRELTVPGVS QSIVLTRVST LSTAMPEGED LRSLGRSGAT MVVHLGAHRI DQIAEELIED
     YGRDCPAAVV AFASRPDEIV LRGTLATIAD QVKAAGVTKT AVVIVGRVLA AEGFPDSYLY
     SATRERTTH