Orotate phosphoribosyltransferase - Escherichia coli (strain K12)

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P0A7E3 (PYRE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	b3642, JW3617

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. Ref.7
Catalytic activity	Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01208
Cofactor	Magnesium By similarity.
Enzyme regulation	Inhibited by sulfate and phosphate ions. Ref.7
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP-Rule MF_01208
Subunit structure	Homodimer. Ref.1 Ref.7
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' pyrimidine nucleobase biosynthetic process Inferred from mutant phenotype PubMed 8501045. Source: EcoCyc pyrimidine nucleotide biosynthetic process Inferred from mutant phenotype PubMed 8501045. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from direct assay PubMed 9222315. Source: EcoliWiki
Molecular_function	magnesium ion binding Inferred from direct assay PubMed 2419315. Source: EcoCyc orotate phosphoribosyltransferase activity Inferred from direct assay PubMed 9222315. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed HAMAP-Rule MF_01208

Chain

2 – 213

212

Orotate phosphoribosyltransferase HAMAP-Rule MF_01208

PRO_0000110694

Regions

Region

34 – 35

Orotate binding By similarity

Region

72 – 73

5-phosphoribose 1-diphosphate binding HAMAP-Rule MF_01208

Region

124 – 132

5-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site

5-phosphoribose 1-diphosphate By similarity

Binding site

5-phosphoribose 1-diphosphate; shared with dimeric partner

Binding site

100

5-phosphoribose 1-diphosphate

Binding site

103

5-phosphoribose 1-diphosphate; shared with dimeric partner

Binding site

105

5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity

Binding site

128

Orotate By similarity

Binding site

156

Orotate By similarity

Experimental info

Sequence conflict

133

Missing Ref.1

Sequence conflict

133

Missing Ref.2

Secondary structure

213

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7E3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F618A6D0A119B9D4
Show »

FASTA

213

23,567

        10         20         30         40         50         60 
MKPYQRQFIE FALSKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLALLG RFYAEALVDS 

        70         80         90        100        110        120 
GIEFDLLFGP AYKGIPIATT TAVALAEHHD LDLPYCFNRK EAKDHGEGGN LVGSALQGRV 

       130        140        150        160        170        180 
MLVDDVITAG TAIRESMEII QANGATLAGV LISLDRQERG RGEISAIQEV ERDYNCKVIS 

       190        200        210 
IITLKDLIAY LEEKPEMAEH LAAVKAYREE FGV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Escherichia coli pyrE gene and of the DNA in front of the protein-coding region." Poulsen P., Jensen K.F., Valentin-Hansen P., Carlsson P., Lundberg L.G. Eur. J. Biochem. 135:223-229(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, SUBUNIT. Strain: K12.
[2]	"Structure of the Escherichia coli pyrE operon and control of pyrE expression by a UTP modulated intercistronic attentuation." Poulsen P., Bonekamp F., Jensen K.F. EMBO J. 3:1783-1790(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[7]	"A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase." Henriksen A., Aghajari N., Jensen K.F., Gajhede M. Biochemistry 35:3803-3809(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH DIPHOSPHATE ANALOG, FUNCTION, ENZYME REGULATION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00781 Genomic DNA. Translation: CAA25358.1.
V01578 Genomic DNA. Translation: CAA24899.1.
L10328 Genomic DNA. Translation: AAA61995.1.
U00096 Genomic DNA. Translation: AAC76666.1.
AP009048 Genomic DNA. Translation: BAE77650.1.

PIR

XJEC. D65165.

RefSeq

NP_418099.1. NC_000913.2.
YP_491791.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ORO	X-ray	2.40	A/B	1-213	[»]

ProteinModelPortal

P0A7E3.

SMR

P0A7E3. Positions 1-213.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7E3. 1 interaction.

STRING

511145.b3642.

Proteomic databases

PRIDE

P0A7E3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76666; AAC76666; b3642.
BAE77650; BAE77650; BAE77650.

GeneID

12930578.
948157.

KEGG

ecj:Y75_p3532.
eco:b3642.

PATRIC

32122771. VBIEscCol129921_3762.

Organism-specific databases

EchoBASE

EB0801.

EcoGene

EG10808. pyrE.

Phylogenomic databases

eggNOG

COG0461.

HOGENOM

HOG000037974.

K00762.

OMA

MKAYQRQ.

ProtClustDB

PRK00455.

Enzyme and pathway databases

BioCyc

EcoCyc:OROPRIBTRANS-MONOMER.
ECOL316407:JW3617-MONOMER.
MetaCyc:OROPRIBTRANS-MONOMER.

UniPathway

UPA00070; UER00119.

Gene expression databases

Genevestigator

P0A7E3.

Family and domain databases

HAMAP

MF_01208. PyrE.

InterPro

IPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
[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...

Other

EvolutionaryTrace

P0A7E3.

Entry information

Entry name

PYRE_ECOLI

Accession

Primary (citable) accession number: P0A7E3
Secondary accession number(s): P00495, Q2M7V6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents