Q8Y668 (PYRE_LISMO) 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
Ordered Locus Names:	lmo1831

Organism

Listeria monocytogenes

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	209 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 – 209	209	Orotate phosphoribosyltransferase HAMAP MF_01208		PRO_0000110708
Regions
	Region	122 – 130	9	5-phosphoribose 1-diphosphate binding By similarity
Sites
	Binding site	96	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	100	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	102	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	126	1	Orotate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y668 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 44EAD790390C3415	FASTA	209	22,834
	10 20 30 40 50 60 MSIEKQVAEQ LLEIKAVFLK PNEPFTWASG IKSPIYCDNR LTLGFPKVRQ FIAKSLAEKI 70 80 90 100 110 120 KQTFGEIDVV AGTATAGIPH AAWVSDLLDL PMVYVRSKAK EHGKGNQIEG PISKGQKVVV 130 140 150 160 170 180 IEDLISTGGS SLKAVEALEE AGAEVVGIAA IFTYGLAKGK QLLEESGTKL VTLTNYDELI 190 200 EVALNENYVT GEDMETLKEW KKNPEKWGK

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591981 Genomic DNA. Translation: CAC99909.1.
PIR	AG1303.
RefSeq	NP_465356.1. NC_003210.1.
3D structure databases
ProteinModelPortal	Q8Y668.
SMR	Q8Y668. Positions 1-208.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	985882.
GenomeReviews	Gene locus lmo1831 in contig AL591824_GR.
KEGG	lmo:lmo1831.
PATRIC	20312855. VBILisMon69206_1876.
Organism-specific databases
GenoList	LMO1831.
Phylogenomic databases
HOGENOM	HBG404341.
OMA	LPMTYVR.
ProtClustDB	PRK00455.
Enzyme and pathway databases
BioCyc	LMON169963:LMO1831-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_LISMO

Accession

Primary (citable) accession number: Q8Y668

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program