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   27-MAR-2024, entry version 147.
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; Pseudomonadota; 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 /
RC   1C / 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 /
RC   1C / 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; Evidence={ECO:0000255|HAMAP-
CC         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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 208964.PA3108; -.
DR   MEROPS; C44.001; -.
DR   PaxDb; 208964-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   OrthoDB; 9801213at2; -.
DR   PhylomeDB; Q51342; -.
DR   BioCyc; PAER208964:G1FZ6-3164-MONOMER; -.
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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   NCBIfam; TIGR01134; purF; 1.
DR   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53271; PRTase-like; 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
//