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Protein

Glyoxylate reductase

Gene

gyaR

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Glycolate + NAD+ = glyoxylate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei241 – 2411By similarity
Active sitei270 – 2701By similarity
Active sitei288 – 2881Proton donorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 1614NADP1 Publication
Nucleotide bindingi180 – 1823NADP1 Publication
Nucleotide bindingi239 – 2413NADP1 Publication
Nucleotide bindingi288 – 2903NADP1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-593-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyoxylate reductase (EC:1.1.1.26)
Gene namesi
Name:gyaR
Ordered Locus Names:PH0597
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Glyoxylate reductasePRO_0000075949Add
BLAST

Proteomic databases

PRIDEiO58320.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi70601.PH0597.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi13 – 208Combined sources
Beta strandi23 – 275Combined sources
Beta strandi30 – 323Combined sources
Helixi36 – 427Combined sources
Turni43 – 453Combined sources
Beta strandi47 – 515Combined sources
Helixi59 – 635Combined sources
Beta strandi70 – 767Combined sources
Helixi83 – 886Combined sources
Beta strandi92 – 943Combined sources
Beta strandi98 – 1003Combined sources
Helixi101 – 11717Combined sources
Helixi119 – 1279Combined sources
Helixi130 – 1334Combined sources
Turni140 – 1434Combined sources
Beta strandi152 – 1565Combined sources
Helixi160 – 17112Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi181 – 1844Combined sources
Helixi185 – 1917Combined sources
Beta strandi193 – 1953Combined sources
Helixi198 – 2047Combined sources
Beta strandi206 – 2105Combined sources
Turni216 – 2205Combined sources
Helixi224 – 2296Combined sources
Beta strandi235 – 2384Combined sources
Helixi242 – 2443Combined sources
Helixi247 – 2559Combined sources
Beta strandi258 – 2658Combined sources
Beta strandi268 – 2714Combined sources
Helixi275 – 2795Combined sources
Beta strandi283 – 2853Combined sources
Helixi294 – 31219Combined sources
Helixi325 – 3284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DBQX-ray1.70A1-334[»]
2DBRX-ray2.61A/B/C/D/E/F1-334[»]
2DBZX-ray2.45A/B1-334[»]
ProteinModelPortaliO58320.
SMRiO58320. Positions 1-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58320.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG01755. Archaea.
COG1052. LUCA.
HOGENOMiHOG000136700.
KOiK00015.
OMAiKSIGPDW.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_00776. GyaR.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR023519. Glyoxylate_reductase_GyaR.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O58320-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPKVFITRE IPEVGIKMLE DEFEVEVWGD EKEIPREILL KKVKEVDALV
60 70 80 90 100
TMLSERIDKE VFENAPKLRI VANYAVGYDN IDIEEATKRG IYVTNTPDVL
110 120 130 140 150
TDATADLAFA LLLATARHVV KGDRFVRSGE WKKRGVAWHP KWFLGYDVYG
160 170 180 190 200
KTIGIIGLGR IGQAIAKRAK GFNMRILYYS RTRKEEVERE LNAEFKPLED
210 220 230 240 250
LLRESDFVVL AVPLTRETYH LINEERLKLM KKTAILINIA RGKVVDTNAL
260 270 280 290 300
VKALKEGWIA GAGLDVFEEE PYYNEELFKL DNVVLTPHIG SASFGAREGM
310 320 330
AELVAKNLIA FKRGEIPPTL VNREVIKIRK PGFE
Length:334
Mass (Da):38,000
Last modified:May 10, 2004 - v2
Checksum:iC0056A354ECBE202
GO

Sequence cautioni

The sequence BAA29686.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29686.1. Different initiation.
PIRiA71175.
RefSeqiWP_010884698.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29686; BAA29686; BAA29686.
GeneIDi1442932.
KEGGipho:PH0597.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29686.1. Different initiation.
PIRiA71175.
RefSeqiWP_010884698.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DBQX-ray1.70A1-334[»]
2DBRX-ray2.61A/B/C/D/E/F1-334[»]
2DBZX-ray2.45A/B1-334[»]
ProteinModelPortaliO58320.
SMRiO58320. Positions 1-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0597.

Proteomic databases

PRIDEiO58320.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA29686; BAA29686; BAA29686.
GeneIDi1442932.
KEGGipho:PH0597.

Phylogenomic databases

eggNOGiarCOG01755. Archaea.
COG1052. LUCA.
HOGENOMiHOG000136700.
KOiK00015.
OMAiKSIGPDW.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-593-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO58320.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_00776. GyaR.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR023519. Glyoxylate_reductase_GyaR.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  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: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Entry informationi

Entry nameiGYAR_PYRHO
AccessioniPrimary (citable) accession number: O58320
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: December 9, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.