[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Heart ventricle; NIH - Mammalian Gene Collection (MGC) project; Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
CATALYTIC ACTIVITY: Glutaryl-CoA + acceptor = crotonoyl-CoA + CO₂ + reduced acceptor.
COFACTOR: FAD (By similarity).
PATHWAY: Amino-acid metabolism; lysine degradation .
PATHWAY: Amino-acid metabolism; tryptophan metabolism .
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
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

Sequence databases

EMBL

BC112822; AAI12823.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001039404.1; -.

UniGene

Bt.43227

3D structure databases

SMR

Q2KHZ9; 47-436.

ModBase

Q2KHZ9.

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

Q2KHZ9.

Genome annotation databases

Ensembl

ENSBTAG00000016211; Bos taurus. [Contig view]

GeneID

506310; -.

KEGG

bta:506310; -.

Phylogenomic databases

HOVERGEN

Q2KHZ9; -.

Other

UniRef

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

Keywords

FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 44`	`44`	`Mitochondrion (Potential).`
`CHAIN`	`45 438`	`394`	`Glutaryl-CoA dehydrogenase, mitochondrial.`	`PRO_0000281992`
`ACT_SITE`	`414 414`		`Proton acceptor (Potential).`

Sequence information

Length: 438 AA [This is the length of the unprocessed precursor]

Molecular weight: 48472 Da [This is the MW of the unprocessed precursor]

CRC64: C420C9901292CDEC [This is a checksum on the sequence]

        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

Q2KHZ9 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