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Database: UniProt
Entry: O06457
LinkDB: O06457
Original site: O06457 
ID   PURK_SACS2              Reviewed;         365 AA.
AC   O06457;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   13-FEB-2019, entry version 117.
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};
GN   OrderedLocusNames=SSO1065;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /
OS   P2) (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=9311113; DOI=10.1111/j.1574-6968.1997.tb12640.x;
RA   Soerensen I.S., Dandanell G.;
RT   "Identification and sequence analysis of Sulfolobus solfataricus purE
RT   and purK genes.";
RL   FEMS Microbiol. Lett. 154:173-180(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
RA   Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
RA   De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
RA   Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
RA   Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
RA   Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; Y13143; CAA73603.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK41328.1; -; Genomic_DNA.
DR   PIR; A90259; A90259.
DR   RefSeq; WP_009989884.1; NC_002754.1.
DR   ProteinModelPortal; O06457; -.
DR   SMR; O06457; -.
DR   STRING; 273057.SSO1065; -.
DR   EnsemblBacteria; AAK41328; AAK41328; SSO1065.
DR   GeneID; 27427381; -.
DR   KEGG; sso:SSO1065; -.
DR   PATRIC; fig|273057.12.peg.1062; -.
DR   eggNOG; arCOG01597; Archaea.
DR   eggNOG; COG0026; LUCA.
DR   HOGENOM; HOG000034026; -.
DR   InParanoid; O06457; -.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   OrthoDB; 57699at2157; -.
DR   BioCyc; SSOL273057:G1FZF-1100-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000001974; 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   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN         1    365       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000075020.
FT   DOMAIN      106    286       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     148    154       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     177    180       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     256    257       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     102    102       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     143    143       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     185    185       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
SQ   SEQUENCE   365 AA;  42360 MW;  A9EE75D029EE199C CRC64;
     MFSVLDWKPK IGILGGGQLG WMIVLEGRKY PFTFYVLEND KNAPACRIAD RCFSPQDYKE
     FVDSSDVITF EFEHVYEKAL EYAEYSGKLL PRLNSVELKR ERYKEKLFYR QHNLPTPRFY
     VAEDGEEALK ILREEFNNVG VIKESKGGYD GKGQYFIFND VEKYQFLREK KEKMVVEEYV
     KFDFEASIII ARDKRGVFIS YPPTYNYNEK GILVYNYGPY NNQNIVEIAR RLSEELDYVG
     IMGVEVFVVN GKVLINEFAP RVHNTGHYTL DGALISQFEQ HLRAIIGMEL GPSTILSPSG
     MVNILGTDKI PVEVLKYGKV YWYSKSEVRK RRKMGHVNVV GNNLEEVKQK IDKIMQLIYT
     NGLDL
//
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