COBQ_PSEE4
ID COBQ_PSEE4 Reviewed; 487 AA.
AC Q1IDJ9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PSEEN1383;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK14260.1; -; Genomic_DNA.
DR RefSeq; WP_011532676.1; NC_008027.1.
DR AlphaFoldDB; Q1IDJ9; -.
DR SMR; Q1IDJ9; -.
DR STRING; 384676.PSEEN1383; -.
DR EnsemblBacteria; CAK14260; CAK14260; PSEEN1383.
DR KEGG; pen:PSEEN1383; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000658; Chromosome.
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..487
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332369"
FT DOMAIN 248..435
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 427
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 487 AA; 52015 MW; 8F116AF714700DA1 CRC64;
MTTLMVQGTT SDAGKSTLVT ALCRWLLRQG VAVVPFKPQN MALNSAVTAD GGEIGRAQAV
QAQACRLAPH TDMNPVLLKP NSDTGAQVIV HGRAVTSMNA VAYHDYKVIA MQAVLASHER
LRQAYPVVMV EGAGSPAEIN LRAGDIANMG FAEAVDCPVI LIADINRGGV FAHLVGTLEL
LSPSEQARVK GFVINRFRGD IALLQPGLDW LEQRTGKPVL GVLPYVTDLH LEAEDAIDVR
QAVKGERVLK VIVPVLPRIS NHTDFDPLRL HPQVDLQFIG PGQPIPPADL IILPGSKSVR
ADLSQLRERG WDSAIARHLR YGGKLIGICG GLQMLGHEVH DPLGLEGAAG SSAGLGLLDY
STVLEAEKQL RNVAGTLGLE QAPVSGYEIH AGVTHGPGLE HPAVQLDDGR NDGAISADGQ
ILATYLHGLF EGSQSCAALL RWAGLADAQA IDYEALRERD IERLADLVEQ HLDTERLRQL
CGVTADA
