ID   COBQ_MYCTO              Reviewed;         494 AA.
AC   P9WP94; L0T2Z2; O53677; P0A532;
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=Cobyric acid synthase;
GN   Name=cobQ; Synonyms=cbiP; OrderedLocusNames=MT0268;
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 amidations at positions B, D, E, and G on
CC       adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC       and one molecule of ATP is hydrogenolyzed for each amidation (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44486.1; -; Genomic_DNA.
DR   PIR; C70940; C70940.
DR   RefSeq; WP_003899877.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP94; -.
DR   EnsemblBacteria; AAK44486; AAK44486; MT0268.
DR   KEGG; mtc:MT0268; -.
DR   PATRIC; fig|83331.31.peg.287; -.
DR   HOGENOM; CLU_019250_2_2_11; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00028; CobQ; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR033949; CobQ_GATase1.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00313; cobQ; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase.
FT   CHAIN           1..494
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000426991"
FT   DOMAIN          253..432
FT                   /note="GATase cobBQ-type"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        424
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  52135 MW;  D97858AA7BB56CA2 CRC64;
     MSGLLVAGTT SDAGKSAVTA GLCRALARRG VRVAPFKAQN MSNNSMVCRG PDGTGVEIGR
     AQWVQALAAR TTPEAAMNPV LLKPASDHRS HVVLMGKPWG EVASSSWCAG RRALAEAACR
     AFDALAARYD VVVAEGAGSP AEINLRAGDY VNMGLARHAG LPTIVVGDID RGGVFAAFLG
     TVALLAAEDQ ALVAGFVVNK FRGDSDLLAP GLRDLERVTG RRVYGTLPWH PDLWLDSEDA
     LDLQGRRAAG TGARRVAVVR LPRISNFTDV DALGLEPDLD VVFASDPRAL DDADLIVLPG
     TRATIADLAW LRARDLDRAL LVHVAAGKPL LGICGGFQML GRVIRDPYGI EGPGGQVTEV
     EGLGLLDVET AFSPHKVLRL PRGEGLGVPA SGYEIHHGRI TRGDTAEEFL GGARDGPVFG
     TMWHGSLEGD ALREAFLRET LGLAPSGSCF LAARERRLDL LGDLVERHLD VDALLNLARH
     GCPPTLPFLA PGAP