位置:首页 > 蛋白库 > XPT_STRPN
XPT_STRPN
ID   XPT_STRPN               Reviewed;         193 AA.
AC   Q97P00;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=SP_1847;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=132.1US00S, and 94.1Nd00S;
RX   PubMed=16189113; DOI=10.1128/aac.49.10.4315-4326.2005;
RA   Stanhope M.J., Walsh S.L., Becker J.A., Italia M.J., Ingraham K.A.,
RA   Gwynn M.N., Mathie T., Poupard J.A., Miller L.A., Brown J.R.,
RA   Amrine-Madsen H.;
RT   "Molecular evolution perspectives on intraspecific lateral DNA transfer of
RT   topoisomerase and gyrase loci in Streptococcus pneumoniae, with
RT   implications for fluoroquinolone resistance development and spread.";
RL   Antimicrob. Agents Chemother. 49:4315-4326(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005672; AAK75919.1; -; Genomic_DNA.
DR   EMBL; DQ174854; AAZ92655.1; -; Genomic_DNA.
DR   EMBL; DQ174892; AAZ92693.1; -; Genomic_DNA.
DR   PIR; F95215; F95215.
DR   RefSeq; WP_000770419.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97P00; -.
DR   SMR; Q97P00; -.
DR   STRING; 170187.SP_1847; -.
DR   EnsemblBacteria; AAK75919; AAK75919; SP_1847.
DR   KEGG; spn:SP_1847; -.
DR   eggNOG; COG0503; Bacteria.
DR   OMA; HQVDPVL; -.
DR   PhylomeDB; Q97P00; -.
DR   BioCyc; SPNE170187:G1FZB-1877-MON; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000000585; 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_0000339763"
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;  21034 MW;  A81BF6CDE5F3C3D5 CRC64;
     MKLLEERILK DGHILGDNIL KVDSFLTHQV DFSLMREIGK VFAEKFATTG ITKVVTIEAS
     GIAPAVFTAE ALNVPMIFAK KAKNITMNEG ILTAQVYSFT KQVTSTVSIA EKFLSPEDKV
     LIIDDFLANG QAAKGLIQII EQAGATVQAI GIVIEKSFQD GRDLLEKAGY PVLSLARLDC
     FENGQVVFKE ADL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024