GenomeNet

Database: UniProt
Entry: Q7MGL1
LinkDB: Q7MGL1
Original site: Q7MGL1 
ID   PURK_VIBVY              Reviewed;         377 AA.
AC   Q7MGL1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   13-FEB-2019, entry version 99.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE            Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE            EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928};
GN   Name=purK {ECO:0000255|HAMAP-Rule:MF_01928}; OrderedLocusNames=VV3219;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C.,
RA   Liao T.-L., Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L.,
RA   Shao C.-P., Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine
RT   pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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:0000255|HAMAP-Rule:MF_01928}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP +
CC         hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-
CC         ribosyl)imidazole + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.4.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01928};
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:0000255|HAMAP-Rule:MF_01928}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01928}.
DR   EMBL; BA000037; BAC95983.1; -; Genomic_DNA.
DR   RefSeq; WP_011151419.1; NC_005139.1.
DR   ProteinModelPortal; Q7MGL1; -.
DR   SMR; Q7MGL1; -.
DR   PRIDE; Q7MGL1; -.
DR   EnsemblBacteria; BAC95983; BAC95983; BAC95983.
DR   GeneID; 2626095; -.
DR   KEGG; vvy:VV3219; -.
DR   PATRIC; fig|196600.6.peg.3185; -.
DR   HOGENOM; HOG000034026; -.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   OrthoDB; 1165275at2; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01928; PurK; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 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; Complete proteome; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN         1    377       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000075019.
FT   DOMAIN       97    287       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     138    144       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     175    178       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     257    258       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING      93     93       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     133    133       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     183    183       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     206    206       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
SQ   SEQUENCE   377 AA;  41277 MW;  4444CB6A1A2F9F9D CRC64;
     MHVLVLGAGQ LARMMSLAGA PLNIQISAYD VTTGDVVHPL TLHLLGHGLE QAIEHVDVIT
     AEFEHIPHDI LAICQASGKF LPSSEAIKAG GDRRLEKTLL DHAGVRNANY YVIETREDFN
     KAIEHVGIPM VLKSALGGYD GRGQWRLKDA AQIETLWQEM AACIAATPTQ AIVAEEFVPF
     QREVSLIGAR GKEGQIEVYP LAENIHVNGV LSLSTAIDSP DLQEQAKHMF TAVAETLNYV
     GVLALEFFDV DGQLLVNEIA PRVHNSGHWT QQGAETCQFE NHLRAVCGLP LGSTKLVRET
     SMINILGEDT LPASVMAMDG CHIHWYGKEK RAGRKMGHIN VCGDYSGELQ RRLCALANVL
     DEKAFPAVHE FAKKWQA
//
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