ID   PUR1_LACCA              Reviewed;         194 AA.
AC   P35853;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 103.
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};
DE   Flags: Precursor; Fragment;
GN   Name=purF {ECO:0000255|HAMAP-Rule:MF_01931};
OS   Lacticaseibacillus casei (Lactobacillus casei).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1398079; DOI=10.1016/0378-1119(92)90076-2;
RA   Gu Z.-M., Martindale D.W., Lee B.H.;
RT   "Isolation and complete sequence of the purL gene encoding FGAM synthase II
RT   in Lactobacillus casei.";
RL   Gene 119:123-126(1992).
RN   [2]
RP   ERRATUM OF PUBMED:1398079.
RX   PubMed=8224889; DOI=10.1016/0378-1119(93)90240-4;
RA   Gu Z.-M., Martindale D.W., Lee B.H.;
RL   Gene 133:147-147(1993).
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   -!- 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; M85265; AAC36948.1; -; Genomic_DNA.
DR   PIR; PC1136; PC1136.
DR   AlphaFoldDB; P35853; -.
DR   SMR; P35853; -.
DR   STRING; 1582.AAW28_12365; -.
DR   MEROPS; C44.001; -.
DR   eggNOG; COG0034; Bacteria.
DR   UniPathway; UPA00074; UER00124.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase; Glycosyltransferase; Purine biosynthesis;
KW   Transferase.
FT   PROPEP          1..11
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029253"
FT   CHAIN           12..>194
FT                   /note="Amidophosphoribosyltransferase"
FT                   /id="PRO_0000029254"
FT   DOMAIN          12..>194
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   ACT_SITE        12
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   NON_TER         194
SQ   SEQUENCE   194 AA;  21144 MW;  4A788CBC5365D5EC CRC64;
     MPHEPKGLNE ECGVFGVWGN PNAASITHLG LHTLQHRGQE GAGIVGLTKD GMRRHYGLGL
     LSEVFTNTDQ LTPLIGRAAL GHVRYSTAGG RVLENIQPLL FRFSDEAIAL AHNGNLTNAI
     SLRRQLEDQG AIFQSTSDTE VLMHLIRRQV GQPWLTQLKT ALNEVHGGFA FVLLTEHGLY
     AAVDPHGFRP MVVG
//