COBQ_BRUA4
ID COBQ_BRUA4 Reviewed; 483 AA.
AC A6X034;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Oant_1872;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS14588.1; -; Genomic_DNA.
DR RefSeq; WP_012091854.1; NC_009667.1.
DR AlphaFoldDB; A6X034; -.
DR SMR; A6X034; -.
DR STRING; 439375.Oant_1872; -.
DR EnsemblBacteria; ABS14588; ABS14588; Oant_1872.
DR KEGG; oan:Oant_1872; -.
DR PATRIC; fig|439375.7.peg.1972; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR PhylomeDB; A6X034; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002301; Chromosome 1.
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_1000002368"
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; 51728 MW; 2B64AB3B98224765 CRC64;
MARAIMFQGT GSDVGKSVLV AGLCRVARNR GLNVRPFKPQ NMSNNAAVSD DGGEIGRAQW
LQALACGVPS SVHMNPVLLK PQTDMGSQVI VQGQVRGEAR GRYYQELKPQ LMAAVMESFA
RVSEGADLVL VEGAGSPAEI NLRAGDIANM GFATQADVPV VLVGDIDRGG VIASLVGTHT
ILSEQDRAMV RGFLINKFRG DISLFDDGLA AITRFTGWRS FGVVPWLKAV SRLPAEDSVV
LERAVRGDKK SLVVAVPMLP RIANFDDLDP LKAEPDVEVV MVPPGSSIPG DAGLVVLPGT
KSTIADMQAV RDNGWDRQLS AHVKRGGHVL GICGGFQMLG HHISDPAGIE GHVRDIDGLG
LLDIETVMEP EKVVRNVQAT ALLHNVPLEG YEIHIGRTTG PDMGWPFARI GEHDDGAISP
DGRIMGTYLH GVFNADEFRR RFLQNLGVQS SSVNYRAGVE AALDELAEGL EACLDIDALF
NLK