ID   PUR1_RHIEC              Reviewed;         496 AA.
AC   P77935; Q2KAA5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   27-MAR-2024, entry version 142.
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;
GN   Name=purF {ECO:0000255|HAMAP-Rule:MF_01931};
GN   OrderedLocusNames=RHE_CH01428;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE3;
RA   Soberon M., Lopez O., Girard L., Miranda J., Morera C.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; U65392; AAB06461.1; -; Genomic_DNA.
DR   EMBL; CP000133; ABC90231.1; -; Genomic_DNA.
DR   RefSeq; WP_011424763.1; NC_007761.1.
DR   AlphaFoldDB; P77935; -.
DR   SMR; P77935; -.
DR   MEROPS; C44.001; -.
DR   KEGG; ret:RHE_CH01428; -.
DR   eggNOG; COG0034; Bacteria.
DR   HOGENOM; CLU_022389_3_3_5; -.
DR   OrthoDB; 9801213at2; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000001936; Chromosome.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; 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   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; PF13537; GATase_7; 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; Purine biosynthesis;
KW   Reference proteome; Transferase.
FT   PROPEP          1..21
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029261"
FT   CHAIN           22..496
FT                   /note="Amidophosphoribosyltransferase"
FT                   /id="PRO_0000029262"
FT   DOMAIN          22..241
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   ACT_SITE        22
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   CONFLICT        193..194
FT                   /note="RD -> SH (in Ref. 1; AAB06461)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="P -> S (in Ref. 1; AAB06461)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315
FT                   /note="L -> G (in Ref. 1; AAB06461)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="Y -> YEY (in Ref. 1; AAB06461)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        407
FT                   /note="P -> R (in Ref. 1; AAB06461)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412..417
FT                   /note="IDTPDA -> SIRPTP (in Ref. 1; AAB06461)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  54162 MW;  EA8F1F6F9189915C CRC64;
     MNQSHSFPTD DPLDGDTLHE ECGVFGILGH PDAAALTALG LHALQHRGQE AAGIVSFDGK
     RFYQERHMGL VGDHYTNPMT LARLPGSISI GHTRYSTTGE VAMRNVQPLF AELEEGGIAI
     AHNGNFTNGL TLRRQIIATG AICQSTSDTE VVLHLIARSR HASTSDRFID AIRQMEGGYS
     MLAMTRTKLI AARDPTGIRP LVMGELDGKP IFCSETCALD IIGAKFIRDV ENGEVIICEI
     QPDGSISIDA RKPSKPQPER LCLFEYVYFA RPDSVVGGRN VYTTRKNMGM NLAKESPVDA
     DVVVPVPDGG TPAALGYAQE SGIPFEYGII RNHYVGRTFI EPTQQIRAFG VKLKHSANRA
     MIEGKRVVLV DDSIVRGTTS LKIVQMIREA GAREVHIRVA SPMIFFPDFY GIDTPDADKL
     LANQYADVEA MAKYIGADSL AFLSINGLYR AVGGEDRNPA RPQFTDHYFT GDYPTRLLDK
     NGESMGNKLS MLASNG
//