ID   COBQ_BRUC2              Reviewed;         483 AA.
AC   A9M5X3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BCAN_A1335;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000872; ABX62378.1; -; Genomic_DNA.
DR   RefSeq; WP_004690938.1; NC_010103.1.
DR   AlphaFoldDB; A9M5X3; -.
DR   SMR; A9M5X3; -.
DR   EnsemblBacteria; ABX62378; ABX62378; BCAN_A1335.
DR   GeneID; 55590980; -.
DR   KEGG; bcs:BCAN_A1335; -.
DR   HOGENOM; CLU_019250_2_0_5; -.
DR   OMA; EIHHGVA; -.
DR   PhylomeDB; A9M5X3; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001385; 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; 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..483
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000074395"
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;  51719 MW;  21C12C4FBF7436CA CRC64;
     MARAIMFQGT GSDVGKSVLV AGLCRVARNR GLKVRPFKPQ NMSNNAAVSD DGGEIGRAQW
     LQALACGVPS SVHMNPVLLK PQTDMGSQLI VQGQVRGEAR GRYYQELKPQ LMAAVMESFA
     KVGDGADLVL VEGAGSPAEI NLRAGDIANM GFATHADVPV VLVGDIDRGG VIASLVGTHT
     ILPQEDRAMV RGFLINKFRG DISLFDDGLA AITRFTGWRS FGVVPWLKAV SRLPAEDSVI
     LERAVRGDKK ALIVAVPMLP RIANFDDLDP LKAEPAVEVV MVPPGSSLPA DAGLVVLPGT
     KSTIADLLAL RENGWDRELV AHVKRGGHVL GICGGFQMLG RRISDPAGIE GNVRDIEGLG
     LLDIETMMEP EKVVRNVEAV SLLHDEPLEG YEIHIGRTSG PDMARPFARI GDHDDGAVSP
     DGRIMGTYLH GVFSADRFRH HFLRALGVEG GQMNYRESVE EALDELAEGL EASLDIDGLF
     ALA