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Database: UniProt
Entry: O66608
LinkDB: O66608
Original site: O66608 
ID   PURK_AQUAE              Reviewed;         365 AA.
AC   O66608;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   13-FEB-2019, entry version 122.
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=aq_245;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06567.1; -; Genomic_DNA.
DR   PIR; D70322; D70322.
DR   RefSeq; NP_213168.1; NC_000918.1.
DR   RefSeq; WP_010880106.1; NC_000918.1.
DR   PDB; 2Z04; X-ray; 2.35 A; A/B=1-365.
DR   PDBsum; 2Z04; -.
DR   ProteinModelPortal; O66608; -.
DR   SMR; O66608; -.
DR   STRING; 224324.aq_245; -.
DR   EnsemblBacteria; AAC06567; AAC06567; aq_245.
DR   GeneID; 1192842; -.
DR   KEGG; aae:aq_245; -.
DR   PATRIC; fig|224324.8.peg.200; -.
DR   eggNOG; ENOG4105CY8; Bacteria.
DR   eggNOG; COG0026; LUCA.
DR   HOGENOM; HOG000034026; -.
DR   InParanoid; O66608; -.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   OrthoDB; 1165275at2; -.
DR   BioCyc; AAEO224324:G1G15-181-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   EvolutionaryTrace; O66608; -.
DR   Proteomes; UP000000798; 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: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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN         1    365       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000074993.
FT   DOMAIN       97    279       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     137    143       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     168    171       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     249    250       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING      93     93       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     132    132       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     176    176       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     199    199       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   STRAND        3      7       {ECO:0000244|PDB:2Z04}.
FT   HELIX        11     20       {ECO:0000244|PDB:2Z04}.
FT   HELIX        21     23       {ECO:0000244|PDB:2Z04}.
FT   STRAND       26     30       {ECO:0000244|PDB:2Z04}.
FT   STRAND       32     35       {ECO:0000244|PDB:2Z04}.
FT   HELIX        37     41       {ECO:0000244|PDB:2Z04}.
FT   STRAND       42     46       {ECO:0000244|PDB:2Z04}.
FT   HELIX        48     50       {ECO:0000244|PDB:2Z04}.
FT   HELIX        51     57       {ECO:0000244|PDB:2Z04}.
FT   STRAND       59     66       {ECO:0000244|PDB:2Z04}.
FT   HELIX        70     76       {ECO:0000244|PDB:2Z04}.
FT   TURN         77     79       {ECO:0000244|PDB:2Z04}.
FT   STRAND       80     82       {ECO:0000244|PDB:2Z04}.
FT   HELIX        85     90       {ECO:0000244|PDB:2Z04}.
FT   HELIX        93    101       {ECO:0000244|PDB:2Z04}.
FT   TURN        102    104       {ECO:0000244|PDB:2Z04}.
FT   STRAND      110    112       {ECO:0000244|PDB:2Z04}.
FT   HELIX       115    118       {ECO:0000244|PDB:2Z04}.
FT   STRAND      129    132       {ECO:0000244|PDB:2Z04}.
FT   STRAND      166    169       {ECO:0000244|PDB:2Z04}.
FT   STRAND      174    183       {ECO:0000244|PDB:2Z04}.
FT   STRAND      189    191       {ECO:0000244|PDB:2Z04}.
FT   STRAND      194    200       {ECO:0000244|PDB:2Z04}.
FT   STRAND      203    212       {ECO:0000244|PDB:2Z04}.
FT   HELIX       215    227       {ECO:0000244|PDB:2Z04}.
FT   STRAND      232    240       {ECO:0000244|PDB:2Z04}.
FT   STRAND      246    254       {ECO:0000244|PDB:2Z04}.
FT   HELIX       257    261       {ECO:0000244|PDB:2Z04}.
FT   HELIX       262    265       {ECO:0000244|PDB:2Z04}.
FT   STRAND      266    268       {ECO:0000244|PDB:2Z04}.
FT   HELIX       270    278       {ECO:0000244|PDB:2Z04}.
FT   STRAND      288    290       {ECO:0000244|PDB:2Z04}.
FT   STRAND      292    299       {ECO:0000244|PDB:2Z04}.
FT   HELIX       302    304       {ECO:0000244|PDB:2Z04}.
FT   HELIX       307    310       {ECO:0000244|PDB:2Z04}.
FT   STRAND      316    320       {ECO:0000244|PDB:2Z04}.
FT   STRAND      330    337       {ECO:0000244|PDB:2Z04}.
FT   HELIX       341    353       {ECO:0000244|PDB:2Z04}.
SQ   SEQUENCE   365 AA;  41988 MW;  C8E859448888AA42 CRC64;
     MLTVGILGGG QLGWMTILEG RKLGFKFHVL EDKENAPACR VADRCFRTGQ ISEFVDSCDI
     ITYEFEHIKD EVLEKCESKL IPNPQALYVK KSRIREKLFL KKHGFPVPEF LVIKRDEIID
     ALKSFKLPVV IKAEKLGYDG KGQYRIKKLE DANQVVKNHD KEESFIIEEF VKFEAEISCI
     GVRDREGKTY FYPQPFNKHE EGILIYNYVP YAKLKEAEEI TKRLMELLDI VGVFTVEFFL
     LKDGRVLINE FAPRVHNTGH WTLDGAYTSQ FENLLRAITE MPLGSTELKL PSGMVNILGK
     SYEEIPLKEI LSVEGAKLYW YGKEKKPRRK VGHVNVVGRS KEEVVEKVER VFTLLKGSRE
     KLPAP
//
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