ID   COBIJ_MYCBO             Reviewed;         508 AA.
AC   P66878; A0A1R3Y075; Q10677; X2BJX9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=BQ2027_MB2092;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00699.1; -; Genomic_DNA.
DR   RefSeq; NP_855742.1; NC_002945.3.
DR   RefSeq; WP_003410659.1; NC_002945.4.
DR   AlphaFoldDB; P66878; -.
DR   SMR; P66878; -.
DR   EnsemblBacteria; SIU00699; SIU00699; BQ2027_MB2092.
DR   PATRIC; fig|233413.5.peg.2300; -.
DR   OMA; YMHMHKR; -.
DR   UniPathway; UPA00148; UER00212.
DR   UniPathway; UPA00148; UER00214.
DR   Proteomes; UP000001419; Chromosome.
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   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; Multifunctional enzyme;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..508
FT                   /note="Cobalamin biosynthesis protein CobIJ"
FT                   /id="PRO_0000150391"
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