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Database: UniProt
Entry: P43850
LinkDB: P43850
Original site: P43850 
ID   PURK_HAEIN              Reviewed;         362 AA.
AC   P43850;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   26-NOV-2014, 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};
GN   OrderedLocusNames=HI_1616;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole
CC       + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-
CC       ribosyl)imidazole. {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   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01928}.
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DR   EMBL; L42023; AAC23264.1; -; Genomic_DNA.
DR   PIR; H64132; H64132.
DR   RefSeq; NP_439758.1; NC_000907.1.
DR   RefSeq; WP_005693629.1; NC_000907.1.
DR   ProteinModelPortal; P43850; -.
DR   STRING; 71421.HI1616; -.
DR   EnsemblBacteria; AAC23264; AAC23264; HI_1616.
DR   GeneID; 950468; -.
DR   KEGG; hin:HI1616; -.
DR   PATRIC; 20191963; VBIHaeInf48452_1689.
DR   eggNOG; COG0026; -.
DR   KO; K01589; -.
DR   OMA; IAPAHIT; -.
DR   OrthoDB; EOG6QZMX7; -.
DR   PhylomeDB; P43850; -.
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:UniProtKB-UniPathway.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   HAMAP; MF_01928; PurK; 1.
DR   InterPro; IPR005875; AIR_COase_ATPase-su.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
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; Complete proteome; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN         1    362       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000074998.
FT   DOMAIN       89    274       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     130    136       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     158    161       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     244    245       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING      85     85       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     125    125       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     166    166       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
SQ   SEQUENCE   362 AA;  41273 MW;  90CE70504784B452 CRC64;
     MQNSTLYPTV YVLGNGQLGR MLRYAGAPLD IYVEPLAFNA PVFDLPENAI ITAEIERWEK
     TPLTELLGNH KNFVNQHIFG LLADRFTQKS LLDELNLSTS PWCLLKDKNQ WNDLFQTVGE
     KVVVKRRTGG YDGRGQWIIR DENRADITDD LFGEVIAEKF IPFDYEVSIV GARFKNGEKR
     FYPVTHNLQQ NGILRYSVVD CAFPQQSVQQ KQAETMLGKI MDKLGYVGVM AMECFVVGDK
     LLINELAPRV HNSGHWTQLG CSISQFELHL RALLNLPTPE LQTFAPSVMI NLIGTNHNPK
     WLNIPFAQLH WYGKEVRIGR KVGHINLSHP NKAVIIQQLE KLCTELPEDY QSGLNWAIEK
     LK
//
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