ID A6V2W6_PSEA7 Unreviewed; 501 AA.
AC A6V2W6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 01-MAY-2013, entry version 40.
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; GIPFELG; -.
DR ProtClustDB; PRK09246; -.
DR BioCyc; PAER381754:GHMY-2081-MONOMER; -.
DR UniPathway; UPA00074; UER00124.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA: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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