ID   COBQ_MYCTU              Reviewed;         494 AA.
AC   P9WP95; L0T2Z2; O53677; P0A532;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   18-SEP-2019, entry version 30.
DE   RecName: Full=Cobyric acid synthase;
GN   Name=cobQ; Synonyms=cbiP; OrderedLocusNames=Rv0255c;
GN   ORFNames=MTV034.21c;
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.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete 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.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC       adenosylcobyrinic A,C-diamide. NH(2) groups are provided by
CC       glutamine, and one molecule of ATP is hydrogenolyzed for each
CC       amidation (By 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; AL123456; CCP42984.1; -; Genomic_DNA.
DR   PIR; C70940; C70940.
DR   RefSeq; WP_003899877.1; NZ_NVQJ01000001.1.
DR   RefSeq; YP_177703.1; NC_000962.3.
DR   STRING; 83332.Rv0255c; -.
DR   PaxDb; P9WP95; -.
DR   PRIDE; P9WP95; -.
DR   EnsemblBacteria; CCP42984; CCP42984; Rv0255c.
DR   GeneID; 886673; -.
DR   KEGG; mtu:Rv0255c; -.
DR   KEGG; mtv:RVBD_0255c; -.
DR   TubercuList; Rv0255c; -.
DR   eggNOG; ENOG4105CAA; Bacteria.
DR   eggNOG; COG1492; LUCA.
DR   KO; K02232; -.
DR   OMA; QVIIHGR; -.
DR   PhylomeDB; P9WP95; -.
DR   BioCyc; MTBH37RV:G185E-4377-MONOMER; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0015420; F:ATPase-coupled vitamin B12 transmembrane 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; 3.40.50.880; -; 1.
DR   HAMAP; MF_00028; CobQ; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017929; CobB/CobQ_GATase.
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   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Complete proteome; Glutamine amidotransferase;
KW   Reference proteome.
FT   CHAIN         1    494       Cobyric acid synthase.
FT                                /FTId=PRO_0000141312.
FT   DOMAIN      253    432       GATase cobBQ-type.
FT   ACT_SITE    334    334       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    424    424       {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
//