Skip Header

Contribute Send feedback
Read comments (?) or add your own

A4SHC9 (PYRE_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Orotate phosphoribosyltransferase
Short name=OPRT
Short name=OPRTase
EC=2.4.2.10
Gene names
Name:pyrE
Ordered Locus Names:ASA_0102
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceInferred 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 processPyrimidine biosynthesis
   LigandMagnesium
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processnucleoside metabolic process

Inferred from electronic annotation. Source: InterPro

pyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionorotate phosphoribosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Orotate phosphoribosyltransferase HAMAP MF_01208
PRO_1000066201

Regions

Region34 – 352Orotate binding By similarity
Region72 – 7325-phosphoribose 1-diphosphate binding By similarity
Region124 – 13295-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site2615-phosphoribose 1-diphosphate By similarity
Binding site9915-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site10015-phosphoribose 1-diphosphate By similarity
Binding site10315-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site10515-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site1281Orotate By similarity
Binding site1561Orotate By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SHC9 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 08EACF9C7779CCC6

FASTA21723,803
        10         20         30         40         50         60 
MKAYQRQFIE FALEKQVLKF GEFTLKSGRK SPYFFNAGLF NSGRDLARLG RFYAAALMDG 

        70         80         90        100        110        120 
GIEFDVLFGP AYKGIPIASA TAVQLVEQHD VDVPWCFNRK EAKDHGEGGN LVGSPLKGRI 

       130        140        150        160        170        180 
MLVDDVITAG TAIRESMDLI QANGASLAGV LIALDRQEKG KGELSAIQEV ERDYGAHIIA 

       190        200        210 
IIQMGDLIAY LEEKQAEQPE LAVQLAAMQA YRAQYGI

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed: 18801193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000644 Genomic DNA. Translation: ABO88301.1.
RefSeqYP_001140049.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4SHC9.
SMRA4SHC9. Positions 1-217.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SHC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4998743.
GenomeReviewsGene locus ASA_0102 in contig CP000644_GR.
KEGGasa:ASA_0102.
PATRIC20786496. VBIAerSal2987_0113.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0461.
HOGENOMHBG404341.
OMAFAFNRKE.
PhylomeDBA4SHC9.
ProtClustDBPRK00455.

Enzyme and pathway databases

BioCycASAL382245:ASA_0102-MONOMER.

Family and domain databases

HAMAPMF_01208. PyrE.
[Tree]
InterProIPR004467. Or_phspho_trans_clade-1.
IPR023031. Orotate_PribosylTferase.
IPR000836. PRibTrfase.
[Graphical view]
KOK00762.
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR00336. PyrE. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRE_AERS4
AccessionPrimary (citable) accession number: A4SHC9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: December 14, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents