ID A0A0S7EKN4_9FLAO Unreviewed; 188 AA.
AC A0A0S7EKN4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01184};
DE Short=XPRTase {ECO:0000256|HAMAP-Rule:MF_01184};
DE EC=2.4.2.22 {ECO:0000256|HAMAP-Rule:MF_01184};
GN Name=xpt_2 {ECO:0000313|EMBL:SUA32186.1};
GN Synonyms=xpt {ECO:0000256|HAMAP-Rule:MF_01184}, xpt_1
GN {ECO:0000313|EMBL:STZ49869.1};
GN ORFNames=AS202_02215 {ECO:0000313|EMBL:ALU25041.1}, NCTC11180_03381
GN {ECO:0000313|EMBL:STZ49869.1}, NCTC11180_03874
GN {ECO:0000313|EMBL:SUA32186.1};
OS Myroides odoratimimus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=76832 {ECO:0000313|EMBL:ALU25041.1, ECO:0000313|Proteomes:UP000069030};
RN [1] {ECO:0000313|EMBL:ALU25041.1, ECO:0000313|Proteomes:UP000069030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR63039 {ECO:0000313|EMBL:ALU25041.1,
RC ECO:0000313|Proteomes:UP000069030};
RX PubMed=26984839; DOI=10.1631/jzus.B1500068;
RA Hu S., Yuan S., Qu H., Jiang T., Zhou Y., Wang M., Ming D.;
RT "Antibiotic resistance mechanisms of Myroides sp.";
RL J. Zhejiang Univ. Sci. B 17:188-199(2016).
RN [2] {ECO:0000313|EMBL:STZ49869.1, ECO:0000313|Proteomes:UP000254940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11180 {ECO:0000313|EMBL:STZ49869.1,
RC ECO:0000313|Proteomes:UP000254940};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts the preformed base xanthine, a product of nucleic
CC acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be
CC reused for RNA or DNA synthesis. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57464, ChEBI:CHEBI:58017; EC=2.4.2.22;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01184};
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC from xanthine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01184}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. Xpt subfamily. {ECO:0000256|HAMAP-Rule:MF_01184}.
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DR EMBL; CP013690; ALU25041.1; -; Genomic_DNA.
DR EMBL; UGQP01000001; STZ49869.1; -; Genomic_DNA.
DR EMBL; UGQP01000002; SUA32186.1; -; Genomic_DNA.
DR RefSeq; WP_006259458.1; NZ_UGQP01000002.1.
DR AlphaFoldDB; A0A0S7EKN4; -.
DR STRING; 76832.AS202_02215; -.
DR GeneID; 66973671; -.
DR KEGG; mod:AS202_02215; -.
DR eggNOG; COG0503; Bacteria.
DR UniPathway; UPA00602; UER00658.
DR Proteomes; UP000069030; Chromosome.
DR Proteomes; UP000254940; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0046110; P:xanthine metabolic process; IEA:InterPro.
DR GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01184; XPRTase; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR010079; Xanthine_PRibTrfase.
DR NCBIfam; TIGR01744; XPRTase; 1.
DR PANTHER; PTHR43864; HYPOXANTHINE/GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43864:SF1; HYPOXANTHINE_GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01184};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01184,
KW ECO:0000313|EMBL:ALU25041.1};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_01184};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01184}.
FT BINDING 20
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
FT BINDING 27
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
FT BINDING 127..131
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
FT BINDING 155
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
SQ SEQUENCE 188 AA; 20983 MW; 34929F41E1BC6FCB CRC64;
MELLRERILQ DGRCFEGGIL KVDSFINHQM DPVLMKSIGV EFVRRFAGTN VNKIMTIEAS
GIAPAIMTGY LLNLPVVFAK KKKPSTMENM LHTQIHSFTK DRTYDVVISN DFLQPTDNVL
FVDDFLAYGN AALGVLDLIK QSGANLVGMG FIIEKAFQDG RKLIEEQGVR VESLAIIEDL
SNCTITIR
//
