XPT_STRP6
ID XPT_STRP6 Reviewed; 193 AA.
AC Q5XC74;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01184};
DE Short=XPRTase {ECO:0000255|HAMAP-Rule:MF_01184};
DE EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01184};
GN Name=xpt {ECO:0000255|HAMAP-Rule:MF_01184}; OrderedLocusNames=M6_Spy0854;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
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:0000255|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:0000255|HAMAP-Rule:MF_01184};
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC from xanthine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01184}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01184}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. Xpt subfamily. {ECO:0000255|HAMAP-Rule:MF_01184}.
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DR EMBL; CP000003; AAT86989.1; -; Genomic_DNA.
DR RefSeq; WP_002984677.1; NC_006086.1.
DR AlphaFoldDB; Q5XC74; -.
DR SMR; Q5XC74; -.
DR EnsemblBacteria; AAT86989; AAT86989; M6_Spy0854.
DR GeneID; 57852624; -.
DR GeneID; 66900766; -.
DR KEGG; spa:M6_Spy0854; -.
DR HOGENOM; CLU_099015_0_0_9; -.
DR OMA; HQVDPVL; -.
DR UniPathway; UPA00602; UER00658.
DR Proteomes; UP000001167; Chromosome.
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 Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01744; XPRTase; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT CHAIN 1..193
FT /note="Xanthine phosphoribosyltransferase"
FT /id="PRO_0000339775"
FT BINDING 20
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
FT BINDING 27
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
FT BINDING 128..132
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
FT BINDING 156
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
SQ SEQUENCE 193 AA; 20994 MW; 18EF4E8911544286 CRC64;
MQLLEERILT DGNILGENIL KVDNFLTHQV DYRLMKAIGK VFAQKYAEAG ITKVVTIEAS
GIAPAVYAAE AMDVPMIFAK KHKNITMTEG ILTAEVYSFT KQVTSTVSIA GKFLSKEDKV
LIIDDFLANG QAAKGLIEII GQAGAQVVGV GIVIEKSFQD GRRLIEDMGI EVTSLARIKN
FENGNLNFLE ADA