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Reviewed, UniProtKB/Swiss-Prot Q9C4M5 (GYAR_THELI)

Last modified June 16, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 origin

Protein namesRecommended name:
    Glyoxylate reductase
    EC=1.1.1.26
Gene names
Name: gyaR
Synonyms: gr
OrganismThermococcus litoralis
Taxonomic identifier2265 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

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Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Glycolate + NAD+ = glyoxylate + NADH. HAMAP MF_00776

Subunit structure

Homodimer. Ref.1

Subcellular location

Cytoplasm. HAMAP MF_00776

Sequence similarities

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

biophysicochemical properties

Kinetic parameters:

KM=0.73 mM for glyoxylate HAMAP MF_00776

KM=1.3 mM for hydroxypyruvate

KM=0.067 mM for NADH

pH dependence:

Optimum pH is 6.5.

Temperature dependence:

Optimum temperature is 90 degrees Celsius. Extremely thermostable.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyoxylate reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Glyoxylate reductase HAMAP MF_00776
PRO_0000075951

Regions

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

Sites

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

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Sequences

Sequence LengthMass (Da)Tools
Q9C4M5-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E277D769D82B9763

FASTA33136,808
        10         20         30         40         50         60 
MKPKVFITRQ IPENGIKMIE KFYEIELWKD PKAPPRGVLL EKVREVDALV TLVTDKVDKE 

        70         80         90        100        110        120 
LLENAPKLKI IAQYAVGYDN IDIEEATKRG IYVTNTPGVL TDATADLAFA LLLAVARRIV 

       130        140        150        160        170        180 
EADAFVRSGE WKKSEVGWHP LMFLGYGLKG KTLGIVGFGR IGQALAKRAK GFGMKIIYYS 

       190        200        210        220        230        240 
RTRKPEAEEE IGAEYVDFET LLKESDFISL HVPLTKETYH MIGEKELKLM KPNAILINTS 

       250        260        270        280        290        300 
RGAVVDTNAL IKALKEGWIA GAGLDVFEEE PYYNEELFKL KNVVLAPHIG SATHEAREGM 

       310        320        330 
AELVAKNLIA FAKGEIPPNL VNKDVLTSSP P

« Hide

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References

[1]"A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litoralis. Characterization, gene cloning, nucleotide sequence and expression in Escherichia coli."
Ohshima T., Nunoura-Kominato N., Kudome T., Sakuraba H.
Eur. J. Biochem. 268:4740-4747(2001) [PubMed: 11532010] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, CHARACTERIZATION, SUBUNIT.
Strain: DSM 5473.

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Cross-references

Sequence databases

AB033995 Genomic DNA. Translation: BAB40320.1.

3D structure databases

HSSPHSSP built from PDB template 1GDH based on UniProtKB P36234.
SMRQ9C4M5. Positions 1-331.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.26. 74708.

Family and domain databases

HAMAPMF_00776.
[Tree]
InterProIPR006139. D-isomer_2_OHA_DH.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[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. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGYAR_THELI
AccessionPrimary (citable) accession number: Q9C4M5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 40 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 documents

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