Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q2KHZ9 (GCDH_BOVIN)

Last modified January 19, 2010. Version 39. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Glutaryl-CoA dehydrogenase, mitochondrial
      Short name=GCD
    EC=1.3.99.7
Gene names
Name: GCDH
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Hide | Top

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

Hide | Top

General annotation (Comments)

Function

Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO2 in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor By similarity.

Catalytic activity

Glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor.

Cofactor

FAD By similarity.

Pathway

Amino-acid metabolism; lysine degradation.

Amino-acid metabolism; tryptophan metabolism.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Hide | Top

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

glutaryl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Mitochondrion Potential
Chain45 – 438394Glutaryl-CoA dehydrogenase, mitochondrial
PRO_0000281992

Regions

Nucleotide binding177 – 18610FAD By similarity
Nucleotide binding177 – 1804FAD By similarity
Nucleotide binding212 – 2143FAD By similarity
Nucleotide binding387 – 3915FAD By similarity
Nucleotide binding416 – 4183FAD By similarity
Region138 – 1392Substrate binding By similarity
Region287 – 2948Substrate binding By similarity

Sites

Active site4141Proton acceptor By similarity
Binding site1861FAD By similarity
Binding site1861Substrate; via carbonyl oxygen By similarity
Binding site2941Substrate By similarity
Binding site3191FAD By similarity
Binding site3301FAD By similarity
Binding site4151Substrate; via amide nitrogen By similarity
Binding site4161FAD By similarity
Binding site4341FAD; via carbonyl oxygen By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q2KHZ9-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: C420C9901292CDEC

FASTA43848,472
        10         20         30         40         50         60 
MALRGVYAQL LNRGPGLRVF RSWSSATAQT EKGEKTQSRS AKPSRPEFDW RDPLLLEEQL 

        70         80         90        100        110        120 
TADEILIRDT FRTYCQERLM PRILLANRNE VFHREIISEM GELGMLGPTI QGYSCAGVSS 

       130        140        150        160        170        180 
VAYGLLAREL ERVDSGYRSA MSVQSSLVMY PIYAYGSEEQ KQKYLPRLAK GELLGCFGLT 

       190        200        210        220        230        240 
EPNHGSDPSG METRARHNPS SRSYILSGSK TWITNSPVAD LLIVWARCED SCIRGFLLEK 

       250        260        270        280        290        300 
GMRGLSTPRI EGKFSLRASS TGMIIMDDVE VPEENVLPGV SGLAGPFGCL NNARYGITWG 

       310        320        330        340        350        360 
VLGAAEFCLH TARQYTLDRI QFGVPLAKNQ LIQKKLADML TEITLGLHAC LQLGRLKDQD 

       370        380        390        400        410        420 
KAAPEMVSLL KRNNCGKALD IARQARDMLG GNGISDEYHV IRHVMNLESV NTYEGTHDIH 

       430 
ALILGRAITG IQAFVAGK

« Hide

Hide | Top

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Heart ventricle.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC112822 mRNA. Translation: AAI12823.1.
IPIIPI00690025.
RefSeqNP_001039404.1.
UniGeneBt.43227

3D structure databases

SMRQ2KHZ9. Positions 47-436.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2KHZ9.

Genome annotation databases

EnsemblENSBTAT00000045996; ENSBTAP00000043333; ENSBTAG00000016211; Bos taurus. [Genome view]
GeneID506310.
KEGGbta:506310.

Organism-specific databases

CTD506310.

Phylogenomic databases

eggNOGmaNOG08865.
HOVERGENQ2KHZ9.
InParanoidQ2KHZ9.
OMAVARDMHG.
OrthoDBEOG9577S9.

Enzyme and pathway databases

BRENDA1.3.99.7. 251.

Family and domain databases

InterProIPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. False negative.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameGCDH_BOVIN
AccessionPrimary (citable) accession number: Q2KHZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 7, 2006
Last modified: January 19, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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