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
//
