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Reviewed, UniProtKB/Swiss-Prot O58320 (GYAR_PYRHO)

Last modified November 25, 2008. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Glyoxylate reductase
    EC=1.1.1.26
Gene names
Name: gyaR
Ordered Locus Names: PH0597
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Glycolate + NAD(+) = glyoxylate + NADH.

Subunit structure

Homodimer By similarity.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GyaR subfamily.

Ontologies

Keywords

   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: HAMAP

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

glyoxylate reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Glyoxylate reductase
PRO_0000075949

Regions

Nucleotide binding158 – 1614NADP
Nucleotide binding180 – 1823NADP
Nucleotide binding239 – 2413NADP
Nucleotide binding288 – 2903NADP

Sites

Active site2411 By similarity
Active site2701 By similarity
Active site2881Proton donor By similarity

Secondary structure

............................................................. 334
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O58320-1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: C0056A354ECBE202

FASTA33438,000
        10         20         30         40         50         60 
MKPKVFITRE IPEVGIKMLE DEFEVEVWGD EKEIPREILL KKVKEVDALV TMLSERIDKE 

        70         80         90        100        110        120 
VFENAPKLRI VANYAVGYDN IDIEEATKRG IYVTNTPDVL TDATADLAFA LLLATARHVV 

       130        140        150        160        170        180 
KGDRFVRSGE WKKRGVAWHP KWFLGYDVYG KTIGIIGLGR IGQAIAKRAK GFNMRILYYS 

       190        200        210        220        230        240 
RTRKEEVERE LNAEFKPLED LLRESDFVVL AVPLTRETYH LINEERLKLM KKTAILINIA 

       250        260        270        280        290        300 
RGKVVDTNAL VKALKEGWIA GAGLDVFEEE PYYNEELFKL DNVVLTPHIG SASFGAREGM 

       310        320        330 
AELVAKNLIA FKRGEIPPTL VNREVIKIRK PGFE 

« Hide

References

« 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]"Crystal structure of glyoxylate reductase (ph0597) from Pyrococcus horikoshii OT3, complexed with nadp (i41)."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADP.
Strain: OT3.

Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA29686.1. Different initiation.
PIRA71175.
RefSeqNP_142561.2.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2DBQX-ray1.70A1-334[»]
2DBRX-ray2.61A/B/C/D/E/F1-334[»]
2DBZX-ray2.45A/B1-334[»]
ModBaseSearch...

Genome annotation databases

GeneID1442932.
GenomeReviewsGene locus PH0597 in contig BA000001_GR.
KEGGpho:PH0597.
NMPDRfig|70601.1.peg.585.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO58320.

Family and domain databases

HAMAPMF_00776.
[Tree]
InterProIPR006139. D-isomer_2_OHA_DHase.
IPR006140. D-isomer_2_OHA_DHase_NAD-bd.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. False negative.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGYAR_PYRHO
AccessionPrimary (citable) accession number: O58320
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: November 25, 2008
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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