P37472 (HPRT_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hypoxanthine-guanine phosphoribosyltransferase
Short name=HGPRT
Short name=HGPRTase
EC=2.4.2.8

Gene names

Name:	hprT
Synonyms:	hpt
Ordered Locus Names:	BSU00680

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.
Cofactor	Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein By similarity.
Pathway	Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Keywords
Biological process	Purine salvage
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	GMP salvage Inferred from Biological aspect of Ancestor. Source: RefGenome IMP salvage Inferred from Biological aspect of Ancestor. Source: RefGenome adenine salvage Inferred from Biological aspect of Ancestor. Source: RefGenome guanine salvage Inferred from Biological aspect of Ancestor. Source: RefGenome hypoxanthine metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome purine ribonucleoside salvage Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	guanine phosphoribosyltransferase activity Inferred from electronic annotation. Source: EC hypoxanthine phosphoribosyltransferase activity Inferred from Biological aspect of Ancestor. Source: RefGenome magnesium ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 180	180	Hypoxanthine-guanine phosphoribosyltransferase		PRO_0000139602
Regions
	Nucleotide binding	99 – 108	10	IMP By similarity
	Nucleotide binding	158 – 159	2	IMP By similarity
Sites
	Active site	103	1	Proton acceptor By similarity
	Metal binding	159	1	Magnesium By similarity
	Binding site	131	1	IMP By similarity
	Binding site	153	1	IMP; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37472 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 5D247BB644A57D92	FASTA	180	20,239
	10 20 30 40 50 60 MMKHDIEKVL ISEEEIQKKV KELGAELTSE YQDTFPLAIG VLKGALPFMA DLIKHIDTYL 70 80 90 100 110 120 EMDFMDVSSY GNSTVSSGEV KIIKDLDTSV EGRDILIIED IIDSGLTLSY LVELFRYRKA 130 140 150 160 170 180 KSIKIVTLLD KPSGRKADIK ADFVGFEVPD AFVVGYGLDY AERYRNLPYI GVLKPAVYES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"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: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D26185 Genomic DNA. Translation: BAA05303.1. AL009126 Genomic DNA. Translation: CAB11844.1.
PIR	S66098.
RefSeq	NP_387949.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P37472.
SMR	P37472. Positions 1-178.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003119; EBBACP00000003119; EBBACG00000003112.
GeneID	936945.
GenomeReviews	Gene locus BSU00680 in contig AL009126_GR.
KEGG	bsu:BSU00680.
NMPDR	fig|224308.1.peg.68.
PATRIC	18971611. VBIBacSub10457_0069.
Organism-specific databases
GenoList	BSU00680. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000000815.
HOGENOM	HBG536385.
OMA	DAFVVGY.
PhylomeDB	P37472.
ProtClustDB	CLSK886566.
Enzyme and pathway databases
BioCyc	BSUB:BSU00680-MONOMER.
Family and domain databases
InterPro	IPR005904. Hxn_phspho_trans. IPR000836. PRibTrfase. [Graphical view]
KO	K00760.
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01203. HGPRTase. 1 hit.
PROSITE	PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HPRT_BACSU

Accession

Primary (citable) accession number: P37472

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program