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P81140 (GCDH_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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 CO2 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 + CO2 + 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 termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionflavin adenine dinucleotide binding

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 Ref.1
Chain14 – 408395Glutaryl-CoA dehydrogenase, mitochondrial
PRO_0000000529

Regions

Nucleotide binding147 – 15610FAD By similarity
Nucleotide binding147 – 1504FAD By similarity
Nucleotide binding182 – 1843FAD By similarity
Nucleotide binding357 – 3615FAD By similarity
Nucleotide binding386 – 3883FAD By similarity
Region107 – 1082Substrate binding By similarity
Region257 – 2648Substrate binding By similarity

Sites

Active site3841Proton acceptor By similarity
Binding site1561FAD By similarity
Binding site1561Substrate; via carbonyl oxygen By similarity
Binding site2641Substrate By similarity
Binding site2891FAD By similarity
Binding site3001FAD By similarity
Binding site3851Substrate; via amide nitrogen By similarity
Binding site3861FAD By similarity
Binding site4041FAD; via carbonyl oxygen By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P81140 [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.
+Additional computationally mapped references.

Cross-references

3D structure databases

ProteinModelPortalP81140.
SMRP81140. Positions 16-405.
ModBaseSearch...

Protein-protein interaction databases

STRINGP81140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

GeneTreeENSGT00590000082906.
HOVERGENHBG001939.
OrthoDBEOG4FBHSZ.

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.
[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]
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 1 hit.
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: July 27, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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