ID   COBQ_BRUA2              Reviewed;         483 AA.
AC   Q2YQK2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BAB1_1331;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR   EMBL; AM040264; CAJ11287.1; -; Genomic_DNA.
DR   RefSeq; WP_002966865.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YQK2; -.
DR   SMR; Q2YQK2; -.
DR   STRING; 359391.BAB1_1331; -.
DR   GeneID; 3787903; -.
DR   KEGG; bmf:BAB1_1331; -.
DR   PATRIC; fig|359391.11.peg.781; -.
DR   HOGENOM; CLU_019250_2_2_5; -.
DR   PhylomeDB; Q2YQK2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002719; Chromosome I.
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; cd05389; CobQ_N; 1.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT   CHAIN           1..483
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002348"
FT   DOMAIN          251..438
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   483 AA;  51631 MW;  D1D82C55DBD33DB8 CRC64;
     MARAIMFQGT GSDVGKSVLV AGLCRVARNR GLKVRPFKPQ NMSNNAAVSD DGGEIGRAQW
     LQALACGVPS SVHMNPVLLK PQTDMGSQLI VQGQVRGEAR GRYYQELKPQ LMAAVMESFA
     KVGDGADLVL VEGAGSPAEI NLRAGDIANM GFATHADVPV VLVGDIDRGG VIASLVGTHT
     ILPQEDRAMV RGFLINKFRG DISLFDDGLA AITRFTGWRS FGVVPWLKAV SRLPAEDSVV
     LERAVRGDKK ALIVAVPMLP RIANFDDLDP LKAEPAVEVV MVPPGSSLPA DAGLVVLPGT
     KSTIADLLAL RENGWDRELV AHVKRGGHVL GICGGFQMLG RRISDPAGIE GNVRDIEGLG
     LLDIETMTEP EKVVRNVEAV SLLHDEPLEG YEIHIGRTSG PDMARPFARI GDHDDGAVSP
     DGRIMGTYLH GIFSADRFRH HFLRALGVEG GQMNYRESVE EALGELAEGL EASLDIDGLF
     ALA
//