PUR1_RHIEC
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 25-MAY-2022, entry version 135.
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}; OrderedLocusNames=RHE_CH01428;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; 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 STRING; 347834.RHE_CH01428; -.
DR MEROPS; C44.001; -.
DR EnsemblBacteria; ABC90231; ABC90231; RHE_CH01428.
DR GeneID; 61479888; -.
DR KEGG; ret:RHE_CH01428; -.
DR eggNOG; COG0034; Bacteria.
DR HOGENOM; CLU_022389_3_3_5; -.
DR OMA; ENAQPTF; -.
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; -; 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; PF13537; GATase_7; 1.
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; 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
