ID E7PTP5_PSESG Unreviewed; 185 AA.
AC E7PTP5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Hypoxanthine-guanine phosphoribosyltransferase {ECO:0000313|EMBL:EGH15711.1};
DE EC=2.4.2.8 {ECO:0000313|EMBL:EGH15711.1};
GN ORFNames=Pgy4_21762 {ECO:0000313|EMBL:EGH15711.1};
OS Pseudomonas savastanoi pv. glycinea str. race 4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH15711.1, ECO:0000313|Proteomes:UP000005466};
RN [1] {ECO:0000313|EMBL:EGH15711.1, ECO:0000313|Proteomes:UP000005466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000005466};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000210};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000256|ARBA:ARBA00000210};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001442};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={ECO:0000256|ARBA:ARBA00001442};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGH15711.1}.
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DR EMBL; ADWY01001042; EGH15711.1; -; Genomic_DNA.
DR RefSeq; WP_004659884.1; NZ_AEGH01000079.1.
DR AlphaFoldDB; E7PTP5; -.
DR PATRIC; fig|875330.5.peg.5207; -.
DR HOGENOM; CLU_073615_2_0_6; -.
DR BioCyc; PSYR875330:G11XH-4211-MONOMER; -.
DR Proteomes; UP000005466; Unassembled WGS sequence.
DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR PANTHER; PTHR43340:SF1; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:EGH15711.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000313|EMBL:EGH15711.1}.
FT DOMAIN 24..169
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 185 AA; 20632 MW; 78BDED627845AAB3 CRC64;
MSADLEHIRQ IMREADCLYT EAEVDAAIAR VGAQINAELA ERNPVVFGVM NGGLIFSGKL
LTHLNFPLEA SYLHATRYRN ETTGGDLFWK AKPEVSFIDR DVLIIDDILD EGHTLGAIID
FCKHAGARAV HTAVLIDKDH DRKARPDLKA DYVGLPCIDR YIFGFGMDYK GYWRNAAGIY
AVKGM
//
