ID   COBIJ_MYCTU             Reviewed;         508 AA.
AC   P9WGB3; L0TB91; P66877; Q10677;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Cobalamin biosynthesis protein CobIJ;
DE   Includes:
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;
DE   Includes:
DE     RecName: Full=Precorrin-3B C17-methyltransferase;
DE              EC=2.1.1.131;
DE     AltName: Full=S-adenosyl-L-methionine--precorrin-3B methyltransferase;
GN   Name=cobIJ; Synonyms=cobI; OrderedLocusNames=Rv2066; ORFNames=MTCY49.05;
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: Methylates precorrin-2 at the C-20 position to produce
CC       precorrin-3A. {ECO:0000250}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=precorrin-3B + S-adenosyl-L-methionine = 3 H(+) + precorrin-4
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12761, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57769, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:77870; EC=2.1.1.131;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 1/10.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 3/10.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP44840.1; -; Genomic_DNA.
DR   PIR; E70764; E70764.
DR   RefSeq; NP_216582.1; NC_000962.3.
DR   RefSeq; WP_003410659.1; NZ_NVQJ01000047.1.
DR   AlphaFoldDB; P9WGB3; -.
DR   SMR; P9WGB3; -.
DR   STRING; 83332.Rv2066; -.
DR   PaxDb; P9WGB3; -.
DR   GeneID; 888483; -.
DR   KEGG; mtu:Rv2066; -.
DR   TubercuList; Rv2066; -.
DR   eggNOG; COG1010; Bacteria.
DR   eggNOG; COG2243; Bacteria.
DR   OMA; YMHMHKR; -.
DR   PhylomeDB; P9WGB3; -.
DR   UniPathway; UPA00148; UER00212.
DR   UniPathway; UPA00148; UER00214.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030789; F:precorrin-3B C17-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   CDD; cd11646; Precorrin_3B_C17_MT; 1.
DR   Gene3D; 3.30.950.10; -; 2.
DR   Gene3D; 3.40.1010.10; -; 2.
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; IPR006363; Cbl_synth_CobJ/CibH_dom.
DR   InterPro; IPR012382; CobI/CbiL.
DR   InterPro; IPR006364; CobI/CbiL/CobIJ_dom.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   Pfam; PF00590; TP_methylase; 2.
DR   SUPFAM; SSF53790; SSF53790; 2.
DR   TIGRFAMs; TIGR01467; cobI_cbiL; 1.
DR   TIGRFAMs; TIGR01466; cobJ_cbiH; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Methyltransferase; Multifunctional enzyme;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..508
FT                   /note="Cobalamin biosynthesis protein CobIJ"
FT                   /id="PRO_0000150390"
FT   REGION          1..243
FT                   /note="Precorrin-2 C20-methyltransferase"
FT   REGION          244..508
FT                   /note="Precorrin-3 methylase"
FT   REGION          489..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  53911 MW;  95AC066F022C4DC1 CRC64;
     MSARGTLWGV GLGPGDPELV TVKAARVIGE ADVVAYHSAP HGHSIARGIA EPYLRPGQLE
     EHLVYPVTTE ATNHPGGYAG ALEDFYADAT ERIATHLDAG RNVALLAEGD PLFYSSYMHL
     HTRLTRRFNA VIVPGVTSVS AASAAVATPL VAGDQVLSVL PGTLPVGELT RRLADADAAV
     VVKLGRSYHN VREALSASGL LGDAFYVERA STAGQRVLPA ADVDETSVPY FSLAMLPGGR
     RRALLTGTVA VVGLGPGDSD WMTPQSRREL AAATDLIGYR GYLDRVEVRD GQRRHPSDNT
     DEPARARLAC SLADQGRAVA VVSSGDPGVF AMATAVLEEA EQWPGVRVRV IPAMTAAQAV
     ASRVGAPLGH DYAVISLSDR LKPWDVIAAR LTAAAAADLV LAIYNPASVT RTWQVGAMRE
     LLLAHRDPGI PVVIGRNVSG PVSGPNEDVR VVKLADLNPA EIDMRCLLIV GSSQTRWYSV
     DSQDRVFTPR RYPEAGRATA TKSSRHSD