ID   COBM_MYCTO              Reviewed;         251 AA.
AC   P9WGB0; L0TB96; Q10672;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Precorrin-4 C(11)-methyltransferase;
DE            EC=2.1.1.133;
DE   AltName: Full=Precorrin-3 methylase;
GN   Name=cobM; OrderedLocusNames=MT2131;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the methylation of C-11 in precorrin-4 to form
CC       precorrin-5. {ECO:0000250}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46411.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70765; B70765.
DR   RefSeq; WP_003906733.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGB0; -.
DR   SMR; P9WGB0; -.
DR   EnsemblBacteria; AAK46411; AAK46411; MT2131.
DR   KEGG; mtc:MT2131; -.
DR   PATRIC; fig|83331.31.peg.2299; -.
DR   HOGENOM; CLU_011276_7_1_11; -.
DR   UniPathway; UPA00148; UER00215.
DR   Proteomes; UP000001020; Chromosome.
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..251
FT                   /note="Precorrin-4 C(11)-methyltransferase"
FT                   /id="PRO_0000428393"
SQ   SEQUENCE   251 AA;  26420 MW;  8D8F213ABFC91CD3 CRC64;
     MTVYFIGAGP GAADLITVRG QRLLQRCPVC LYAGSIMPDD LLAQCPPGAT IVDTGPLTLE
     QIVRKLADAD ADGRDVARLH SGDPSLYSAL AEQCRELDAL GIGYEIVPGV PAFAAAAAAL
     KRELTVPGVA QTVTLTRVAT LSTPIPPGED LAALARSRAT LVLHLAAAQI DAIVPRLLDG
     GYRPETPVAV VAFASWPQQR TLRGTLADIA ARMHDAKITR TAVIVVGDVL TAEGFTDSYL
     YSVARHGRYA Q