ID XPT_STRA1 Reviewed; 193 AA.
AC Q3K111;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 50.
DE RecName: Full=Xanthine phosphoribosyltransferase;
DE Short=XPRTase;
DE EC=2.4.2.22;
GN Name=xpt; OrderedLocusNames=SAK_1171;
OS Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS SS700).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=205921;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27591 / A909 / CDC SS700;
RX PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S.,
RA DeBoy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I.,
RA Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A.,
RA Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N.,
RA Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J.,
RA Smith S., Utterback T.R., White O., Rubens C.E., Grandi G.,
RA Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R.,
RA Fraser C.M.;
RT "Genome analysis of multiple pathogenic isolates of Streptococcus
RT agalactiae: implications for the microbial 'pan-genome'.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
CC -!- FUNCTION: Converts the preformed base xanthine, a product of
CC nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so
CC it can be reused for RNA or DNA synthesis (By similarity).
CC -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose
CC 1-diphosphate + xanthine.
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway;
CC XMP from xanthine: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. Xpt subfamily.
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DR EMBL; CP000114; ABA46348.1; -; Genomic_DNA.
DR RefSeq; YP_329792.1; NC_007432.1.
DR HSSP; P42085; 2FXV.
DR ProteinModelPortal; Q3K111; -.
DR SMR; Q3K111; 1-190.
DR STRING; 205921.SAK_1171; -.
DR EnsemblBacteria; ABA46348; ABA46348; SAK_1171.
DR GeneID; 3686007; -.
DR KEGG; sak:SAK_1171; -.
DR PATRIC; 19633609; VBIStrAga82541_1114.
DR eggNOG; COG0503; -.
DR HOGENOM; HOG000036777; -.
DR KO; K03816; -.
DR OMA; ATVYSFT; -.
DR ProtClustDB; PRK09219; -.
DR BioCyc; SAGA205921:GHD7-1186-MONOMER; -.
DR UniPathway; UPA00602; UER00658.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:HAMAP.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:HAMAP.
DR GO; GO:0046110; P:xanthine metabolic process; IEA:InterPro.
DR GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01184; XPRTase; 1; -.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR010079; Xanthine_PRibTrfase.
DR Pfam; PF00156; Pribosyltran; 1.
DR TIGRFAMs; TIGR01744; XPRTase; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage;
KW Transferase.
FT CHAIN 1 193 Xanthine phosphoribosyltransferase.
FT /FTId=PRO_0000339759.
FT REGION 128 132 5-phospho-alpha-D-ribose 1-diphosphate
FT binding (By similarity).
FT BINDING 20 20 Xanthine; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 27 27 Xanthine (By similarity).
FT BINDING 156 156 Xanthine (By similarity).
SQ SEQUENCE 193 AA; 20765 MW; B3698AD92685519B CRC64;
MKLLEERILK DGDVLGENIL KVDSFLTHQV DFELMQEIGK VFADKYKEAG ITKVVTIEAS
GIAPAVYAAQ ALGVPMIFAK KAKNITMTEG ILTAEVYSFT KQVTSQVSIV SRFLSNDDTV
LIIDDFLANG QAAKGLLEII GQAGAKVAGI GIVIEKSFQD GRDLLEKTGV PVTSLARIKA
FENGRVVFAE ADA
//
