COBQ_BRUAB
ID COBQ_BRUAB Reviewed; 483 AA.
AC Q57CI7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BruAb1_1312;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(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; AE017223; AAX74647.1; -; Genomic_DNA.
DR RefSeq; WP_002966865.1; NC_006932.1.
DR AlphaFoldDB; Q57CI7; -.
DR SMR; Q57CI7; -.
DR EnsemblBacteria; AAX74647; AAX74647; BruAb1_1312.
DR GeneID; 3787903; -.
DR KEGG; bmb:BruAb1_1312; -.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000540; 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_1000002349"
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
