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O58855 (PYRE_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PH1128
ORF Names:PHBP017
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length186 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 – 186186Orotate phosphoribosyltransferase HAMAP MF_01208
PRO_0000110787

Regions

Region119 – 12795-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site9315-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site9415-phosphoribose 1-diphosphate By similarity
Binding site9715-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site9915-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site1231Orotate By similarity
Binding site1511Orotate By similarity

Sequences

Sequence LengthMass (Da)Tools
O58855 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 00177DD8DEC84097

FASTA18620,430
        10         20         30         40         50         60 
MKMKDELINL IINEGCIKFG HFVLTSGKES NYYIDIKSLI TNPKALRIIA KLIKEKAEEL 

        70         80         90        100        110        120 
NLNYDKIAGP ELGAVPIATA LSLETNKPLL IVRKKKKEHG TGKVIEGNVQ KGDKVLLVED 

       130        140        150        160        170        180 
VTTTGGSVIR AAKILREHGA DVVGIFVVVD REEGAKENIE KEGFKFYPLV LVSELFKAAG 


ISKDQS

« Hide

References

[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000001 Genomic DNA. Translation: BAA30228.1.
PIRB71054.
RefSeqNP_143032.1. NC_000961.1.

3D structure databases

ProteinModelPortalO58855.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000000080; EBPYRP00000000080; EBPYRG00000000080.
GeneID1443447.
GenomeReviewsGene locus PH1128 in contig BA000001_GR.
KEGGpho:PH1128.
NMPDRfig|70601.1.peg.1100.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000023182.
HOGENOMHBG404341.
OMAGKEADYY.
PhylomeDBO58855.
ProtClustDBPRK00455.

Enzyme and pathway databases

BioCycPHOR70601:PH1128-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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRE_PYRHO
AccessionPrimary (citable) accession number: O58855
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: December 14, 2011
This is version 75 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

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