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Reviewed, UniProtKB/Swiss-Prot P81140 (GCDH_PIG)

Last modified November 25, 2008. Version 57. 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

Names and origin

Protein namesRecommended name:
    Glutaryl-CoA dehydrogenase, mitochondrial
      Short name=GCD
    EC=1.3.99.7
Gene names
Name: GCDH
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length408 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor.

Catalytic activity

Glutaryl-CoA + acceptor = crotonoyl-CoA + CO(2) + reduced acceptor.

Cofactor

FAD.

Pathway

Amino-acid metabolism; lysine degradation.

Amino-acid metabolism; tryptophan metabolism.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords

   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing

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

electron carrier activity

Inferred from electronic annotation. Source: InterPro

glutaryl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 13›13Mitochondrion
Chain14 – 408395Glutaryl-CoA dehydrogenase, mitochondrial
PRO_0000000529

Sites

Active site3841Proton acceptor Potential

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P81140-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E517D565A193E146

FASTA40845,123
        10         20         30         40         50         60 
KGGKTQGRSA KSSRPEFDWR DPLVLEEQLT ADEILIRDTF RTYCQEHLMP RIVLANRNEV 

        70         80         90        100        110        120 
FHREIISEMG ELGVLGPTIK GYGCAGVSSV AYGLLARELE RVDSGYRSAM SVQSSLVMHP 

       130        140        150        160        170        180 
IYAYGSEEQQ QQKYLPRLAK GELLGCFGLT EPNHGSDPGS METRALHNPS NRSYTLNGAK 

       190        200        210        220        230        240 
TWITNSPVAD LFVVWARCED NCIRGFLLEK GMRGLSAPKI EGKFSLRASA TGMIIMDDVE 

       250        260        270        280        290        300 
VPEENVLPKA SSLAVPFGCL NNARYGISWG VLGAAEFCLH TARQYTLDRI QFGVPLAKNQ 

       310        320        330        340        350        360 
LIQRKLADML TEITLGLHAC LQLGRLKDQD KVTPEMVSLL KRNNCGKALD IARQARDMLG 

       370        380        390        400 
GNGISDEYHV IRHAMNLEAV NTYEGTHDIH ALILGRAITG IQAFTTDK 

« Hide

References

[1]"Pork and human cDNAs encoding glutaryl-CoA dehydrogenase."
Goodman S.I., Kratz L.E., Frerman F.E.
Prog. Clin. Biol. Res. 375:169-173(1992) [PubMed: 1438360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 14-38 AND 375-407.
Tissue: Liver.

Cross-references

3D structure databases

HSSPHSSP built from PDB template 1BUC based on UniProtKB Q06319.
SMRP81140. Positions 16-405.
ModBaseSearch...

Phylogenomic databases

HOVERGENP81140.

Family and domain databases

InterProIPR006091. Acyl-CoA_DHase/Oxase_M.
IPR006089. Acyl-CoA_DHase_CS.
IPR006092. Acyl-CoA_DHase_N.
IPR006090. Acyl-CoA_Oxase/DHase_1.
IPR013786. AcylCoA_DH/ox_N.
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...

Entry information

Entry nameGCDH_PIG
AccessionPrimary (citable) accession number: P81140
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 25, 2008
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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