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Database: UniProt/TrEMBL
Entry: A6V2W6_PSEA7
LinkDB: A6V2W6_PSEA7
Original site: A6V2W6_PSEA7 
ID   A6V2W6_PSEA7            Unreviewed;       501 AA.
AC   A6V2W6;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   13-NOV-2013, entry version 43.
DE   RecName: Full=Amidophosphoribosyltransferase;
DE            Short=ATase;
DE            EC=2.4.2.14;
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
GN   Name=purF; OrderedLocusNames=PSPA7_2025;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 5-phospho-beta-D-ribosylamine + diphosphate +
CC       L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate
CC       + H(2)O.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 1/2.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       purine/pyrimidine phosphoribosyltransferase family.
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DR   EMBL; CP000744; ABR80710.1; -; Genomic_DNA.
DR   RefSeq; YP_001347401.1; NC_009656.1.
DR   ProteinModelPortal; A6V2W6; -.
DR   SMR; A6V2W6; 2-487.
DR   STRING; 381754.PSPA7_2025; -.
DR   EnsemblBacteria; ABR80710; ABR80710; PSPA7_2025.
DR   GeneID; 5355007; -.
DR   KEGG; pap:PSPA7_2025; -.
DR   PATRIC; 19825833; VBIPseAer80442_1945.
DR   eggNOG; COG0034; -.
DR   HOGENOM; HOG000033687; -.
DR   KO; K00764; -.
DR   OMA; CDACFTG; -.
DR   OrthoDB; EOG6KT2Q1; -.
DR   ProtClustDB; PRK09246; -.
DR   BioCyc; PAER381754:GHMY-2025-MONOMER; -.
DR   UniPathway; UPA00074; UER00124.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   InterPro; IPR005854; Amd_phspho_trans.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR000583; GATase_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   Pfam; PF00310; GATase_2; 2.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   TIGRFAMs; TIGR01134; purF; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycosyltransferase; Magnesium; Metal-binding;
KW   Purine biosynthesis; Transferase.
FT   ACT_SITE      2      2       For GATase activity (By similarity).
SQ   SEQUENCE   501 AA;  55385 MW;  8662A2B440E4937D CRC64;
     MCGIVGIVGK SNVNQALYDA LTVLQHRGQD AAGIVTCHDD KLYLRKDNGL VRDVFQQRHM
     QRLIGSVGIG HVRYPTAGSS SSAEAQPFYV NSPYGITLAH NGNLTNVEQL AKEIYESDLR
     HVNTNSDSEV LLNVFAHELA VRNKLQPTEE DIFAAVSGVH DRCVGGYAVV AMITGHGIVG
     FRDPNAIRPI VFGQRHTENG VEYMIASESV ALDVLGFTLI RDLAPGEAVY ITEEGKLYTR
     QCARAPKYAP CIFEHVYLAR PDSIMDGISV YKARLRMGEK LADKILRERP EHDIDVVIPI
     PDTSRTAALE LANRLGVKFR EGFVKNRYIG RTFIMPGQAA RKKSVRQKLN AIELEFRGKN
     VMLVDDSIVR GTTCKQIIQM AREAGAKNVY FCSAAPAVRY PNVYGIDMPS AHELIAHNRS
     TEDVSKLIGA DWLVYQDLPD LIDAVGGGKI KIDRFDCAVF DGEYVTGDVN EAYLNRIEQA
     RNDATKAKSQ AVSAIIDLYN D
//
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