Reviewed, UniProtKB/Swiss-Prot Q7W3H5 (PYRE_BORPA)

Names and origin

Protein names

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

Gene names

Name:	pyrE
Ordered Locus Names:	BPP4060

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01208
Cofactor	Magnesium By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP MF_01208
Subunit structure	Homodimer By similarity.
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
Gene Ontology (GO)
Biological process	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP orotate 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 – 224	224	Orotate phosphoribosyltransferase HAMAP MF_01208		PRO_0000110676
Regions
	Region	37 – 38	2	Orotate binding By similarity
	Region	75 – 76	2	5-phosphoribose 1-diphosphate binding By similarity
	Region	130 – 138	9	5-phosphoribose 1-diphosphate binding By similarity
Sites
	Binding site	29	1	5-phosphoribose 1-diphosphate By similarity
	Binding site	105	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	106	1	5-phosphoribose 1-diphosphate By similarity
	Binding site	109	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	111	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	134	1	Orotate By similarity
	Binding site	162	1	Orotate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7W3H5-1 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: F0AEC0575A49F4FE	FASTA	224	23,284
	10 20 30 40 50 60 MSASASTAAD FVRFALDEGV LRFGSFKVKS GRISPYFFNA GLFNSGRSVG ALAGFYAQAL 70 80 90 100 110 120 VDSGVAFDML FGPAYKGIPL ATATSVALAG HAAMAGRDVP FAFNRKEAKD HGEGGTLVGA 130 140 150 160 170 180 PLTGKVVIID DVITAGTSVR ESVEIIRAAG AEPAAVLIAL DRMERAGPDD ALSPHSAVQD 190 200 210 220 VARTYGIPVV SIASLADIMT LLQDDAQFAE HRAAVQAYRS KYGV

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640435 Genomic DNA. Translation: CAE39343.1. Different initiation.
RefSeq	NP_886204.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1668116.
GenomeReviews	Gene locus BPP4060 in contig BX470249_GR.
KEGG	bpa:BPP4060.
NMPDR	fig|257311.1.peg.3838.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7W3H5.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP4060-MON.
BRENDA	2.4.2.10. 263123.
Family and domain databases
HAMAP	MF_01208. [Tree]
InterPro	IPR004467. Or_phspho_trans. IPR002375. Pr/py_Pribosyl_transf_CS. IPR000836. PRibTrfase. [Graphical view]
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_BORPA

Accession

Primary (citable) accession number: Q7W3H5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	September 1, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)