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Reviewed, UniProtKB/Swiss-Prot O50083 (RPIA_PYRHO)

Last modified June 15, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended name:
Ribose-5-phosphate isomerase A

EC=5.3.1.6
Alternative name(s):
Phosphoriboisomerase A
Short name=PRI
Gene names
Name:rpiA
Ordered Locus Names:PH1375
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
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Protein attributesHide

Sequence length229 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.
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General annotation (Comments)Hide

Catalytic activity

D-ribose 5-phosphate = D-ribulose 5-phosphate. HAMAP MF_00170

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. HAMAP MF_00170

Subunit structure

Homotetramer. HAMAP MF_00170

Sequence similarities

Belongs to the ribose 5-phosphate isomerase family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is over 90 degrees Celsius. HAMAP MF_00170

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OntologiesHide

Keywords
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processpentose-phosphate shunt, non-oxidative branch

Inferred from electronic annotation. Source: HAMAP

   Molecular functionribose-5-phosphate isomerase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...
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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 229229Ribose-5-phosphate isomerase A HAMAP MF_00170
PRO_0000158517

Secondary structure

.......................................... 229
Helix Strand Turn

Details...

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SequencesHide

Sequence LengthMass (Da)Tools
O50083-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 0E35BCB9F608D93C

FASTA22925,162
        10         20         30         40         50         60 
MNVEEMKKIA AKEALKFIED DMVIGLGTGS TTAYFIKLLG EKLKRGEISD IVGVPTSYQA 

        70         80         90        100        110        120 
KLLAIEHDIP IASLDQVDAI DVAVDGADEV DPNLNLIKGR GAALTMEKII EYRAGTFIVL 

       130        140        150        160        170        180 
VDERKLVDYL CQKMPVPIEV IPQAWKAIIE ELSIFNAKAE LRMGVNKDGP VITDNGNFII 

       190        200        210        220 
DAKFPRIDDP LDMEIELNTI PGVIENGIFA DIADIVIVGT REGVKKLER 

« Hide

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ReferencesHide

« Hide 'large scale' 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: OT3.
[2]"A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure."
Ishikawa K., Matsui I., Payan F., Cambillau C., Ishida H., Kawarabayasi Y., Kikuchi H., Roussel A.
Structure 10:877-886(2002) [PubMed: 12057201] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), CHARACTERIZATION.
+Additional computationally mapped references.
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA30481.1.
PIRA71010.
RefSeqNP_143254.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LK5X-ray1.75A/B/C/D1-229[»]
1LK7X-ray2.00A/B/C/D1-229[»]
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1502514.

Genome annotation databases

EnsemblBacteriaEBPYRT00000000157; EBPYRP00000000157; EBPYRG00000000157.
GeneID1443702.
GenomeReviewsGene locus PH1375 in contig BA000001_GR.
KEGGpho:PH1375.
NMPDRfig|70601.1.peg.1355.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG515603.
OMAVFDLNSV.
ProtClustDBPRK00702.

Enzyme and pathway databases

BioCycPHOR70601:PH1375-MONOMER.
BRENDA5.3.1.6. 74679.

Family and domain databases

HAMAPMF_00170. Rib_5P_isom_A.
[Tree]
InterProIPR014036. HTH_DeoR.
IPR004788. Ribose5P_isomerase_typA.
IPR020672. Ribose5P_isomerase_typA_subgr.
[Graphical view]
PANTHERPTHR11934. RpiA. 1 hit.
PfamPF00455. DeoR. 1 hit.
PF06026. Rib_5-P_isom_A. 1 hit.
[Graphical view]
TIGRFAMsTIGR00021. rpiA. 1 hit.
ProtoNetSearch...
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Entry informationHide

Entry nameRPIA_PYRHO
AccessionPrimary (citable) accession number: O50083
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: June 15, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents