[1]	NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 14-38 AND 375-407. TISSUE=Liver; PubMed=1438360 [NCBI, ExPASy, EBI, Israel, Japan] Goodman S.I., Kratz L.E., Frerman F.E.; "Pork and human cDNAs encoding glutaryl-CoA dehydrogenase."; Prog. Clin. Biol. Res. 375:169-173(1992).

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 + CO₂ + reduced acceptor.
COFACTOR: FAD.
PATHWAY: Amino-acid metabolism; lysine degradation .
PATHWAY: Amino-acid metabolism; tryptophan metabolism .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

HSSP

Q06319; 1BUC. [HSSP ENTRY / PDB]

SMR

P81140; 16-405.

ModBase

P81140.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004361;	Molecular function: glutaryl-CoA dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006091; 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 of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.

Pfam

PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
PF02771; Acyl-CoA_dh_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00072; ACYL_COA_DH_1; FALSE_NEG.
PS00073; ACYL_COA_DH_2; 1.

ProtoNet

P81140.

Phylogenomic databases

HOVERGEN

P81140; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 13`	`>13`	`Mitochondrion.`
`CHAIN`	`14 408`	`395`	`Glutaryl-CoA dehydrogenase, mitochondrial.`	`PRO_0000000529`
`ACT_SITE`	`384 384`		`Proton acceptor (Potential).`
`NON_TER`	`1 1`

Sequence information

Length: 408 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 45123 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: E517D565A193E146 [This is a checksum on the sequence]

        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

P81140 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools