P25972 (PYRE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Orotate phosphoribosyltransferase
Short name=OPRT
Short name=OPRTase
EC=2.4.2.10

Gene names

Name:	pyrE
Synonyms:	pyrX
Ordered Locus Names:	BSU15560

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	216 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) By similarity. HAMAP MF_01208
Catalytic activity	Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01208
Cofactor	Magnesium By similarity. HAMAP MF_01208
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP MF_01208
Subunit structure	Homodimer By similarity. HAMAP MF_01208
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Magnesium
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	orotate phosphoribosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 216	216	Orotate phosphoribosyltransferase HAMAP MF_01208		PRO_0000110672
Regions
	Region	126 – 134	9	5-phosphoribose 1-diphosphate binding By similarity
Sites
	Binding site	100	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	104	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	106	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	130	1	Orotate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25972 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 712042661C6E2708	FASTA	216	23,522
	10 20 30 40 50 60 MGGNQILKQI IAKHLLDIQA VFLRPNEPFT WASGILSPIY CDNRLTLSFP EVRNDVASGI 70 80 90 100 110 120 SKLVKEHFPE AEMIAGTATA GIPHAALAAD HLNLPMCYVR SKPKAHGKGN QIEGAVQEGQ 130 140 150 160 170 180 KTVVIEDLIS TGGSVLEACA ALQAAGCEVL GVVSIFTYGL PKAEEAFAKA ELPYYSLTDY 190 200 210 DTLTEVALEN GNIHSDDLKK LQTWKRNPES KDWFKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon." Quinn C.L., Stephenson B.T., Switzer R.L. J. Biol. Chem. 266:9113-9127(1991) [PubMed: 1709162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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.
[3]	"L-cysteine biosynthesis in Bacillus subtilis: identification, sequencing, and functional characterization of the gene coding for phosphoadenylylsulfate sulfotransferase." Mansilla M.C., de Mendoza D. J. Bacteriol. 179:976-981(1997) [PubMed: 9006060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-216.
[4]	"Cloning and sequencing 8 Kbp of DNA from Bacillus subtilis downstream of the pyr operon." Foulger D., Errington J. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-216. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M59757 Genomic DNA. Translation: AAA21274.1. AL009126 Genomic DNA. Translation: CAB13430.1. AJ000974 Genomic DNA. Translation: CAA04408.1.
PIR	F69686.
RefSeq	NP_389439.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P25972.
SMR	P25972. Positions 3-215.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002919; EBBACP00000002919; EBBACG00000002913.
GeneID	936714.
GenomeReviews	Gene locus BSU15560 in contig AL009126_GR.
KEGG	bsu:BSU15560.
NMPDR	fig|224308.1.peg.1558.
PATRIC	18974919. VBIBacSub10457_1651.
Organism-specific databases
GenoList	BSU15560. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002725.
HOGENOM	HBG404341.
OMA	LPMTYVR.
PhylomeDB	P25972.
ProtClustDB	PRK00455.
Enzyme and pathway databases
BioCyc	BSUB:BSU15560-MONOMER.
Family and domain databases
HAMAP	MF_01208. PyrE. [Tree]
InterPro	IPR004467. Or_phspho_trans_clade-1. IPR023031. Orotate_PribosylTferase. IPR000836. PRibTrfase. [Graphical view]
KO	K00762.
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR00336. PyrE. 1 hit.
PROSITE	PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRE_BACSU

Accession

Primary (citable) accession number: P25972

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program