Q65JU3 (PYRE_BACLD) 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:	BLi01776, BL02280

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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
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_1000066203
Regions
	Region	120 – 128	9	5-phosphoribose 1-diphosphate binding By similarity
Sites
	Binding site	94	1	5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
	Binding site	98	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	124	1	Orotate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65JU3 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: CF51A3B29B7707A0	FASTA	209	22,109
	10 20 30 40 50 60 MKTDIANHLL KIKAVFLRPN EPFTWASGIL SPIYCDNRLT LSYPEVRDDI ASGLAGLIQD 70 80 90 100 110 120 KFPGAEMIAG TATAGIPHAA LAADRLSLPM CYVRSKPKAH GKGNQIEGAV VKGQKVVVIE 130 140 150 160 170 180 DLISTGGSVL EAAAALTEAG CEVLGVAAIF TYGLPKAAAA FSEAGVEYHT LTDYDTLTEA 190 200 ALAGGYITEQ DAAKLKEWKA DPESKSWMN

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU23311.1. AE017333 Genomic DNA. Translation: AAU40671.1.
RefSeq	YP_078949.1. NC_006270.3. YP_091364.1. NC_006322.1.
3D structure databases
ProteinModelPortal	Q65JU3.
SMR	Q65JU3. Positions 1-204.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65JU3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000057032; EBBACP00000055563; EBBACG00000057023. EBBACT00000060059; EBBACP00000058492; EBBACG00000060050.
GeneID	3030931. 3098083.
GenomeReviews	Gene locus BLi01776 in contig AE017333_GR. Gene locus BL02280 in contig CP000002_GR.
KEGG	bld:BLi01776. bli:BL02280.
NMPDR	fig|279010.5.peg.1718.
PATRIC	18949153. VBIBacLic203714_1780.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0461.
GeneTree	EBGT00050000002725.
HOGENOM	HBG404341.
OMA	LPMTYVR.
PhylomeDB	Q65JU3.
ProtClustDB	PRK00455.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI01776-MONOMER. BLIC279010:BL02280-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_BACLD

Accession

Primary (citable) accession number: Q65JU3
Secondary accession number(s): Q62V98

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program