XPT_BACSU
ID XPT_BACSU Reviewed; 194 AA.
AC P42085;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Xanthine phosphoribosyltransferase;
DE Short=XPRTase;
DE EC=2.4.2.22;
GN Name=xpt; OrderedLocusNames=BSU22070;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=168;
RX PubMed=9098051; DOI=10.1128/jb.179.8.2540-2550.1997;
RA Christiansen L.C., Schou S., Nygaard P., Saxild H.H.;
RT "Xanthine metabolism in Bacillus subtilis: characterization of the xpt-pbuX
RT operon and evidence for purine- and nitrogen-controlled expression of genes
RT involved in xanthine salvage and catabolism.";
RL J. Bacteriol. 179:2540-2550(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT artificial chromosomes for sequencing.";
RL Microbiology 142:3005-3015(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GUANINE
RP TETRAPHOSPHATE.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of xanthine phosphoribosyltransferase from Bacillus
RT subtilis.";
RL Submitted (FEB-2005) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GMP, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168;
RX PubMed=16716072; DOI=10.1021/bi060287y;
RA Arent S., Kadziola A., Larsen S., Neuhard J., Jensen K.F.;
RT "The extraordinary specificity of xanthine phosphoribosyltransferase from
RT Bacillus subtilis elucidated by reaction kinetics, ligand binding, and
RT crystallography.";
RL Biochemistry 45:6615-6627(2006).
CC -!- FUNCTION: Converts the preformed base xanthine, a product of nucleic
CC acid breakdown, to xanthosine 5'-monophosphate (XMP), so that it can be
CC reused for RNA or DNA synthesis.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 uM for xanthine {ECO:0000269|PubMed:16716072};
CC KM=281 uM for guanine {ECO:0000269|PubMed:16716072};
CC KM=1250 uM for hypoxanthine {ECO:0000269|PubMed:16716072};
CC pH dependence:
CC Optimum pH is 6-9. {ECO:0000269|PubMed:16716072};
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC from xanthine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16716072, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Repressed during growth on purines as a nitrogen source.
CC {ECO:0000269|PubMed:9098051}.
CC -!- MISCELLANEOUS: Highly specific for xanthine, with a strong
CC discrimination against hypoxanthine and guanine as substrates.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. Xpt subfamily. {ECO:0000305}.
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DR EMBL; X83878; CAA58758.1; -; Genomic_DNA.
DR EMBL; L77246; AAA96611.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14124.1; -; Genomic_DNA.
DR PIR; S51309; S51309.
DR RefSeq; NP_390089.1; NC_000964.3.
DR RefSeq; WP_003230744.1; NZ_JNCM01000036.1.
DR PDB; 1Y0B; X-ray; 1.80 A; A/B/C/D=1-194.
DR PDB; 2FXV; X-ray; 2.05 A; A/B=1-194.
DR PDB; 6W1I; X-ray; 1.80 A; A/B/C/D=2-194.
DR PDBsum; 1Y0B; -.
DR PDBsum; 2FXV; -.
DR PDBsum; 6W1I; -.
DR AlphaFoldDB; P42085; -.
DR SMR; P42085; -.
DR STRING; 224308.BSU22070; -.
DR DrugBank; DB04022; Guanosine tetraphosphate.
DR jPOST; P42085; -.
DR PaxDb; P42085; -.
DR PRIDE; P42085; -.
DR DNASU; 939064; -.
DR EnsemblBacteria; CAB14124; CAB14124; BSU_22070.
DR GeneID; 939064; -.
DR KEGG; bsu:BSU22070; -.
DR PATRIC; fig|224308.179.peg.2411; -.
DR eggNOG; COG0503; Bacteria.
DR InParanoid; P42085; -.
DR OMA; HQVDPVL; -.
DR PhylomeDB; P42085; -.
DR BioCyc; BSUB:BSU22070-MON; -.
DR BRENDA; 2.4.2.22; 658.
DR UniPathway; UPA00602; UER00658.
DR EvolutionaryTrace; P42085; -.
DR PRO; PR:P42085; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosyltransferase; Purine salvage;
KW Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="Xanthine phosphoribosyltransferase"
FT /id="PRO_0000139697"
FT BINDING 20
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT BINDING 27
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT BINDING 128..132
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT BINDING 156
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT HELIX 1..11
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1Y0B"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1Y0B"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1Y0B"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1Y0B"
FT TURN 46..50
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1Y0B"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:1Y0B"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:1Y0B"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1Y0B"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:1Y0B"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 146..156
FT /evidence="ECO:0007829|PDB:1Y0B"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:1Y0B"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1Y0B"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1Y0B"
SQ SEQUENCE 194 AA; 21038 MW; 86DE53F467A52EDE CRC64;
MEALKRKIEE EGVVLSDQVL KVDSFLNHQI DPLLMQRIGD EFASRFAKDG ITKIVTIESS
GIAPAVMTGL KLGVPVVFAR KHKSLTLTDN LLTASVYSFT KQTESQIAVS GTHLSDQDHV
LIIDDFLANG QAAHGLVSIV KQAGASIAGI GIVIEKSFQP GRDELVKLGY RVESLARIQS
LEEGKVSFVQ EVHS
