P42085 (XPT_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Xanthine phosphoribosyltransferase
Short name=XPRTase
EC=2.4.2.22

Gene names

Name:	xpt
Ordered Locus Names:	BSU22070

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so that it can be reused for RNA or DNA synthesis. HAMAP-Rule MF_01184
Catalytic activity	XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine. HAMAP-Rule MF_01184
Pathway	Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1. HAMAP-Rule MF_01184
Subunit structure	Homodimer. Ref.5
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_01184.
Induction	Repressed during growth on purines as a nitrogen source. Ref.1
Miscellaneous	Highly specific for xanthine, with a strong discrimination against hypoxanthine and guanine as substrates. HAMAP-Rule MF_01184
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family. Xpt subfamily.
Biophysicochemical properties	Kinetic parameters: KM=2.2 µM for xanthine Ref.5 KM=281 µM for guanine KM=1250 µM for hypoxanthine pH dependence: Optimum pH is 6-9.

Ontologies

Keywords
Biological process	Purine salvage
Cellular component	Cytoplasm
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	XMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway purine ribonucleoside salvage Inferred from electronic annotation. Source: HAMAP xanthine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	xanthine phosphoribosyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 194

194

Xanthine phosphoribosyltransferase HAMAP-Rule MF_01184

PRO_0000139697

Regions

Region

128 – 132

5

5-phospho-alpha-D-ribose 1-diphosphate binding HAMAP-Rule MF_01184

Sites

Binding site

20

1

Xanthine; via amide nitrogen and carbonyl oxygen

Binding site

27

1

Xanthine

Binding site

156

1

Xanthine

Secondary structure

1

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194

Helix Strand Turn

Details...

Helix

1 – 11

11

Beta strand

13 – 15

3

Turn

16 – 18

3

Beta strand

19 – 21

3

Turn

23 – 26

4

Beta strand

27 – 30

4

Helix

32 – 45

14

Turn

46 – 50

5

Beta strand

53 – 57

5

Turn

58 – 61

4

Helix

62 – 72

11

Beta strand

76 – 82

7

Beta strand

89 – 98

10

Turn

99 – 102

4

Beta strand

103 – 110

8

Helix

111 – 113

3

Beta strand

119 – 129

11

Helix

131 – 142

12

Beta strand

146 – 156

11

Helix

161 – 167

7

Beta strand

172 – 180

9

Turn

182 – 184

3

Sequences

	Sequence		Length	Mass (Da)
	P42085 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 86DE53F467A52EDE	FASTA	194	21,038
	10 20 30 40 50 60 MEALKRKIEE EGVVLSDQVL KVDSFLNHQI DPLLMQRIGD EFASRFAKDG ITKIVTIESS 70 80 90 100 110 120 GIAPAVMTGL KLGVPVVFAR KHKSLTLTDN LLTASVYSFT KQTESQIAVS GTHLSDQDHV 130 140 150 160 170 180 LIIDDFLANG QAAHGLVSIV KQAGASIAGI GIVIEKSFQP GRDELVKLGY RVESLARIQS 190 LEEGKVSFVQ EVHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Xanthine metabolism in Bacillus subtilis: characterization of the xpt-pbuX operon and evidence for purine- and nitrogen-controlled expression of genes involved in xanthine salvage and catabolism." Christiansen L.C., Schou S., Nygaard P., Saxild H.H. J. Bacteriol. 179:2540-2550(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: 168.
[2]	"Organization of the Bacillus subtilis 168 chromosome between kdg and the attachment site of the SP beta prophage: use of long accurate PCR and yeast artificial chromosomes for sequencing." Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D. Microbiology 142:3005-3015(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Crystal structure of xanthine phosphoribosyltransferase from Bacillus subtilis." Midwest center for structural genomics (MCSG) Submitted (FEB-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GUANINE TETRAPHOSPHATE.
[5]	"The extraordinary specificity of xanthine phosphoribosyltransferase from Bacillus subtilis elucidated by reaction kinetics, ligand binding, and crystallography." Arent S., Kadziola A., Larsen S., Neuhard J., Jensen K.F. Biochemistry 45:6615-6627(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GMP, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X83878 Genomic DNA. Translation: CAA58758.1.
L77246 Genomic DNA. Translation: AAA96611.1.
AL009126 Genomic DNA. Translation: CAB14124.1.

PIR

S51309.

RefSeq

NP_390089.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y0B	X-ray	1.80	A/B/C/D	1-194	[»]
2FXV	X-ray	2.05	A/B	1-194	[»]

ProteinModelPortal

P42085.

SMR

P42085. Positions 1-191.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU22070.

Proteomic databases

PaxDb

P42085.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14124; CAB14124; BSU22070.

GeneID

939064.

KEGG

bsu:BSU22070.

PATRIC

18976221. VBIBacSub10457_2301.

Organism-specific databases

GenoList

BSU22070. [Micado]

Phylogenomic databases

eggNOG

COG0503.

HOGENOM

HOG000036777.

KO

K03816.

OMA

ATVYSFT.

ProtClustDB

PRK09219.

Enzyme and pathway databases

BioCyc

BSUB:BSU22070-MONOMER.

UniPathway

UPA00602; UER00658.

Family and domain databases

HAMAP

MF_01184. XPRTase.

InterPro

IPR000836. PRibTrfase_dom.
IPR010079. Xanthine_PRibTrfase.
[Graphical view]

Pfam

PF00156. Pribosyltran. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01744. XPRTase. 1 hit.

PROSITE

PS00103. PUR_PYR_PR_TRANSFER. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P42085.

Entry information

Entry name

XPT_BACSU

Accession

Primary (citable) accession number: P42085

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program