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Protein

Glyoxylate reductase

Gene

gyaR

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalytic activityi

Glycolate + NAD+ = glyoxylate + NADH.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei242UniRule annotation1
Active sitei271UniRule annotation1
Active sitei290Proton donorUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 162NADPUniRule annotation4
Nucleotide bindingi181 – 183NADPUniRule annotation3
Nucleotide bindingi240 – 242NADPUniRule annotation3
Nucleotide bindingi290 – 292NADPUniRule annotation3

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandNAD

Names & Taxonomyi

Protein namesi
Recommended name:
Glyoxylate reductaseUniRule annotation (EC:1.1.1.26UniRule annotation)
Gene namesi
Name:gyaRUniRule annotation
Ordered Locus Names:APE_1831.1
OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Taxonomic identifieri272557 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
Proteomesi
  • UP000002518 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000759461 – 335Glyoxylate reductaseAdd BLAST335

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272557.APE_1831.1

Structurei

3D structure databases

ProteinModelPortaliQ9YAW4
SMRiQ9YAW4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG01755 Archaea
COG1052 LUCA
HOGENOMiHOG000136700
KOiK00015
OMAiKWIAHNG
OrthoDBiPOG093Z0DW1

Family and domain databases

HAMAPiMF_00776 GyaR, 1 hit
InterProiView protein in InterPro
IPR006139 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
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00389 2-Hacid_dh, 1 hit
PF02826 2-Hacid_dh_C, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00065 D_2_HYDROXYACID_DH_1, 1 hit
PS00670 D_2_HYDROXYACID_DH_2, 1 hit
PS00671 D_2_HYDROXYACID_DH_3, 1 hit

Sequencei

Sequence statusi: Complete.

Q9YAW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRPRVFVTR EVFPEALELL SKYYDVEVWD KYQPPPYETL LSKAREADAL
60 70 80 90 100
YTLLTDRIDC DLLSQAPRLR IVAQMAVGFD NIDVECATRL GIYVTNTPGV
110 120 130 140 150
LTEATAEFTW ALILAAARRV VEADHFVRWG EWWRLRTGWH PMMMLGVELR
160 170 180 190 200
GKTLGILGMG RIGSRVAEIG KAFGMRIIYH SRSRKREIEK ELGAEYRSLE
210 220 230 240 250
DLLRESDILS IHLPLTDETR HLIGESELKL MKKTAILVNT GRGAIVDTGA
260 270 280 290 300
LVKALREGWI AAAALDVFEE EPLNPNHPLT AFKNVVLAPH AASATRETRL
310 320 330
RMAMMAAENL VAFAQGKVPP NLVNREVVKV RQPGF
Length:335
Mass (Da):37,757
Last modified:May 10, 2004 - v2
Checksum:i0CD5EE38E1AA6163
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA Translation: BAA80834.2
PIRiE72568

Genome annotation databases

EnsemblBacteriaiBAA80834; BAA80834; APE_1831.1
KEGGiape:APE_1831.1
PATRICifig|272557.25.peg.1228

Similar proteinsi

Entry informationi

Entry nameiGYAR_AERPE
AccessioniPrimary (citable) accession number: Q9YAW4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: March 28, 2018
This is version 98 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health