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Database: UniProt/TrEMBL
Entry: B7V5W6_PSEA8
LinkDB: B7V5W6_PSEA8
Original site: B7V5W6_PSEA8 
ID   B7V5W6_PSEA8            Unreviewed;       360 AA.
AC   B7V5W6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   26-NOV-2014, entry version 41.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|RuleBase:RU361200};
DE            Short=N5-CAIR synthase {ECO:0000256|RuleBase:RU361200};
DE            EC=6.3.4.18 {ECO:0000256|RuleBase:RU361200};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|RuleBase:RU361200};
GN   Name=purK {ECO:0000313|EMBL:CAW30574.1};
GN   OrderedLocusNames=PLES_58201 {ECO:0000313|EMBL:CAW30574.1};
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722 {ECO:0000313|EMBL:CAW30574.1, ECO:0000313|Proteomes:UP000001527};
RN   [1] {ECO:0000313|EMBL:CAW30574.1, ECO:0000313|Proteomes:UP000001527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58 {ECO:0000313|EMBL:CAW30574.1,
RC   ECO:0000313|Proteomes:UP000001527};
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L.,
RA   Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D.,
RA   Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L.,
RA   Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants
RT   of in vivo competitiveness in the Liverpool epidemic strain of
RT   Pseudomonas aeruginosa.";
RL   Genome Res. 19:12-23(2009).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-
CC       aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-
CC       carboxyaminoimidazole ribonucleotide (N5-CAIR).
CC       {ECO:0000256|RuleBase:RU361200}.
CC   -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole
CC       + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-
CC       ribosyl)imidazole. {ECO:0000256|RuleBase:RU361200}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
CC       {ECO:0000256|RuleBase:RU361200}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361200}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family.
CC       {ECO:0000256|RuleBase:RU361200}.
CC   -!- SIMILARITY: Contains ATP-grasp domain.
CC       {ECO:0000256|SAAS:SAAS00098872}.
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DR   EMBL; FM209186; CAW30574.1; -; Genomic_DNA.
DR   RefSeq; YP_002443398.1; NC_011770.1.
DR   ProteinModelPortal; B7V5W6; -.
DR   SMR; B7V5W6; 13-358.
DR   STRING; 557722.PLES_58201; -.
DR   EnsemblBacteria; CAW30574; CAW30574; PLES_58201.
DR   GeneID; 7179422; -.
DR   KEGG; pag:PLES_58201; -.
DR   PATRIC; 19821593; VBIPseAer113719_5983.
DR   eggNOG; COG0026; -.
DR   HOGENOM; HOG000034026; -.
DR   KO; K01589; -.
DR   OMA; DCILEGW; -.
DR   OrthoDB; EOG6QZMX7; -.
DR   BioCyc; PAER557722:GHJW-5916-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   InterPro; IPR005875; AIR_COase_ATPase-su.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01161; purK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU361200,
KW   ECO:0000256|SAAS:SAAS00098858};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001527};
KW   Ligase {ECO:0000256|RuleBase:RU361200};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361200,
KW   ECO:0000256|SAAS:SAAS00098850};
KW   Purine biosynthesis {ECO:0000256|RuleBase:RU361200,
KW   ECO:0000256|SAAS:SAAS00098833}.
SQ   SEQUENCE   360 AA;  38496 MW;  88FBBEA510DE2B54 CRC64;
     MKIGVIGGGQ LGRMLALAGT PLGMNFAFLD PAPDACAASL GEHIRADYGD QEHLRQLADE
     VDLVTFEFES VPAETVAFLS QFVPVYPNAE SLRIARDRWF EKSMFKDLGI PTPDFADVQS
     QADLDAAAAA IGLPAVLKTR TLGYDGKGQK VLRQPADVQG AFAELGSVPC ILEGFVPFTG
     EVSLVAVRAR DGETRFYPLV HNTHDSGILK LSVASSGHPL QALAEDYVGR VLARLDYVGV
     LAFEFFEVDG GLKANEIAPR VHNSGHWTIE GAECSQFENH LRAVAGLPLG STAKVGESAM
     LNFIGAVPPV AQVVAVADCH LHHYGKAFKN GRKVGHATLR CADRATLQAR IAEVEALIEA
//
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