COBQ_BRUA2
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 25-MAY-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=BAB1_1331;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; 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 EnsemblBacteria; CAJ11287; CAJ11287; 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 OMA; EIHHGVA; -.
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; 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; 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
