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Reviewed, UniProtKB/Swiss-Prot Q9YAW4 (GYAR_AERPE)

Last modified June 16, 2009. Version 49. 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

Names and origin

Protein namesRecommended name:
    Glyoxylate reductase
    EC=1.1.1.26
Gene names
Name: gyaR
Ordered Locus Names: APE_1831.1
OrganismAeropyrum pernix [Complete proteome] [HAMAP]
Taxonomic identifier56636 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Glycolate + NAD+ = glyoxylate + NADH. HAMAP MF_00776

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Glyoxylate reductase HAMAP MF_00776
PRO_0000075946

Regions

Nucleotide binding159 – 1624NADP By similarity
Nucleotide binding181 – 1833NADP By similarity
Nucleotide binding240 – 2423NADP By similarity
Nucleotide binding290 – 2923NADP By similarity

Sites

Active site2421 By similarity
Active site2711 By similarity
Active site2901Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YAW4-1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 0CD5EE38E1AA6163

FASTA33537,757
        10         20         30         40         50         60 
MKRPRVFVTR EVFPEALELL SKYYDVEVWD KYQPPPYETL LSKAREADAL YTLLTDRIDC 

        70         80         90        100        110        120 
DLLSQAPRLR IVAQMAVGFD NIDVECATRL GIYVTNTPGV LTEATAEFTW ALILAAARRV 

       130        140        150        160        170        180 
VEADHFVRWG EWWRLRTGWH PMMMLGVELR GKTLGILGMG RIGSRVAEIG KAFGMRIIYH 

       190        200        210        220        230        240 
SRSRKREIEK ELGAEYRSLE DLLRESDILS IHLPLTDETR HLIGESELKL MKKTAILVNT 

       250        260        270        280        290        300 
GRGAIVDTGA LVKALREGWI AAAALDVFEE EPLNPNHPLT AFKNVVLAPH AASATRETRL 

       310        320        330 
RMAMMAAENL VAFAQGKVPP NLVNREVVKV RQPGF 

« Hide

References

[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K1.

Cross-references

Sequence databases

BA000002 Genomic DNA. Translation: BAA80834.2.
PIRE72568.
RefSeqNP_148197.2.

3D structure databases

HSSPHSSP built from PDB template 1HL3 based on UniProtKB Q9Z2F5.
ModBaseSearch...

Genome annotation databases

GeneID1446271.
GenomeReviewsGene locus APE_1831.1 in contig BA000002_GR.
KEGGape:APE_1831.1.
NMPDRfig|272557.1.peg.1305.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9YAW4.
OMAQ9YAW4. DHIDVKY.

Enzyme and pathway databases

BRENDA1.1.1.26. 256344.

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...

Entry information

Entry nameGYAR_AERPE
AccessionPrimary (citable) accession number: Q9YAW4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: June 16, 2009
This is version 49 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

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