PUR1_PSEAE
ID PUR1_PSEAE Reviewed; 501 AA.
AC Q51342; Q9HZB1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931};
GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931}; OrderedLocusNames=PA3108;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 286-501.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7704274; DOI=10.1099/13500872-141-2-431;
RA Foglino M., Borne F., Bally M., Ball G., Patte J.-C.;
RT "A direct sulfhydrylation pathway is used for methionine biosynthesis in
RT Pseudomonas aeruginosa.";
RL Microbiology 141:431-439(1995).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-
CC Rule:MF_01931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01931};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931}.
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DR EMBL; AE004091; AAG06496.1; -; Genomic_DNA.
DR EMBL; U10904; AAA83434.1; -; Genomic_DNA.
DR PIR; G83256; G83256.
DR RefSeq; NP_251798.1; NC_002516.2.
DR RefSeq; WP_003091383.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q51342; -.
DR SMR; Q51342; -.
DR STRING; 287.DR97_4825; -.
DR MEROPS; C44.001; -.
DR PaxDb; Q51342; -.
DR PRIDE; Q51342; -.
DR EnsemblBacteria; AAG06496; AAG06496; PA3108.
DR GeneID; 880477; -.
DR KEGG; pae:PA3108; -.
DR PATRIC; fig|208964.12.peg.3260; -.
DR PseudoCAP; PA3108; -.
DR HOGENOM; CLU_022389_2_1_6; -.
DR InParanoid; Q51342; -.
DR OMA; ENAQPTF; -.
DR PhylomeDB; Q51342; -.
DR BioCyc; PAER208964:G1FZ6-3164-MON; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase; Glycosyltransferase; Magnesium; Metal-binding;
KW Purine biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..501
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000139641"
FT DOMAIN 2..234
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT CONFLICT 286..290
FT /note="LRERP -> PPRAS (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="A -> R (in Ref. 2; AAA83434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 55370 MW; 58A3D8AD41905794 CRC64;
MCGIVGIVGK SNVNQALYDA LTVLQHRGQD AAGIVTCHDD KLYLRKDNGL VRDVFQQRHM
QRLIGSVGIG HVRYPTAGSS SSAEAQPFYV NSPYGITLAH NGNLTNVEQL AKEIYESDLR
HVNTNSDSEV LLNVFAHELA VRNKLQPTEE DIFAAVSCVH DRCVGGYAVV AMITGHGIVG
FRDPNAIRPI VFGQRHTENG VEYMIASESV ALDVLGFTLI RDLAPGEAVY ITEEGKLYTR
QCAKAPKYAP CIFEHVYLAR PDSIMDGISV YKARLRMGEK LADKILRERP DHDIDVVIPI
PDTSRTAALE LANRLGVKFR EGFVKNRYIG RTFIMPGQAA RKKSVRQKLN AIELEFRGKN
VMLVDDSIVR GTTCKQIIQM AREAGAKNVY FCSAAPAVRY PNVYGIDMPS AHELIAHNRS
TEDVSKLIGA DWLVYQDLPD LIDAVGGGKI KIDHFDCAVF DGEYVTGDVN EAYLNRIEQA
RNDATKAKSQ AVSAIIDLYN D
