COBM_MYCTU
ID COBM_MYCTU Reviewed; 251 AA.
AC P9WGB1; L0TB96; Q10672;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Precorrin-4 C(11)-methyltransferase;
DE EC=2.1.1.133;
DE AltName: Full=Precorrin-3 methylase;
GN Name=cobM; OrderedLocusNames=Rv2071c; ORFNames=MTCY49.10c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
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DR EMBL; AL123456; CCP44845.1; -; Genomic_DNA.
DR PIR; B70765; B70765.
DR RefSeq; NP_216587.1; NC_000962.3.
DR RefSeq; WP_003906733.1; NZ_NVQJ01000047.1.
DR AlphaFoldDB; P9WGB1; -.
DR SMR; P9WGB1; -.
DR STRING; 83332.Rv2071c; -.
DR PaxDb; P9WGB1; -.
DR DNASU; 888521; -.
DR GeneID; 888521; -.
DR KEGG; mtu:Rv2071c; -.
DR TubercuList; Rv2071c; -.
DR eggNOG; COG2875; Bacteria.
DR OMA; WSAMGEQ; -.
DR PhylomeDB; P9WGB1; -.
DR UniPathway; UPA00148; UER00215.
DR Proteomes; UP000001584; 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 1: Evidence at protein level;
KW Cobalamin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..251
FT /note="Precorrin-4 C(11)-methyltransferase"
FT /id="PRO_0000150396"
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