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 01-MAY-2013, entry version 93.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase;
DE Short=N5-CAIR synthase;
DE EC=6.3.4.18;
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase;
GN Name=purK; 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) (By similarity).
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.
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 -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the PurK/PurT family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; L42023; AAC23264.1; -; Genomic_DNA.
DR PIR; H64132; H64132.
DR RefSeq; NP_439758.1; 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; HWYEKEV; -.
DR ProtClustDB; PRK06019; -.
DR UniPathway; UPA00074; UER00942.
DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA: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 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; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 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.
FT NP_BIND 158 161 ATP (By similarity).
FT NP_BIND 244 245 ATP (By similarity).
FT BINDING 85 85 ATP (By similarity).
FT BINDING 125 125 ATP (By similarity).
FT BINDING 136 136 ATP (By similarity).
FT BINDING 166 166 ATP (By similarity).
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
//
