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Database: UniProt
Entry: Q4L574
LinkDB: Q4L574
Original site: Q4L574 
ID   PURK_STAHJ              Reviewed;         374 AA.
AC   Q4L574;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   13-FEB-2019, entry version 100.
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=SH1892;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE05201.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AP006716; BAE05201.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029376687.1; NC_007168.1.
DR   ProteinModelPortal; Q4L574; -.
DR   SMR; Q4L574; -.
DR   STRING; 279808.SH1892; -.
DR   PRIDE; Q4L574; -.
DR   EnsemblBacteria; BAE05201; BAE05201; SH1892.
DR   GeneID; 24247466; -.
DR   KEGG; sha:SH1892; -.
DR   eggNOG; ENOG4105CY8; Bacteria.
DR   eggNOG; COG0026; LUCA.
DR   HOGENOM; HOG000034029; -.
DR   KO; K01589; -.
DR   OrthoDB; 1165275at2; -.
DR   BioCyc; SHAE279808:G1G27-1874-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000000543; Chromosome.
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:0051287; F:NAD 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   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
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.
FT   CHAIN         1    374       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000075011.
FT   DOMAIN      112    296       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     153    159       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     183    186       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     266    267       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     108    108       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     148    148       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     191    191       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     214    214       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
SQ   SEQUENCE   374 AA;  42583 MW;  1E36AEF46296E436 CRC64;
     MNFNKLKFGD TIGIIGGGQL GKMMAQSAQK MGFKVICLDP NPDSPCKSVA HEFITAAYDD
     EEALHELGEK SDVITYEFEN ISAEQLIRLT QKFNIPQGYQ AIQLLQDRLT EKQTLQKAGS
     KIVPFLPIKE EKDLNVVINQ LGYPFIVKTR FGGYDGKGQV LVKNEESIQE AKDLISQQEC
     VAEQFLDIAL EVSLTVTIGN QKQITYFPLQ ENEHRNQILF KTIVPARSDK EQEARDEVNK
     IINEVHFVGT FTVEFFIDKS NNLYVNEIAP RPHNSGHYSI EACDYSQFDT HILAVTGQNL
     PKEIEILKPA VMMNLLGRDL DLLEDKFANH PEWHVHIYGK PERKPNRKMG HMTILTNNVD
     ETEKAMLKQF EGRE
//
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