NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2777793 [NCBI, ExPASy, EBI, Israel, Japan]
Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.;
"Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family.";
J. Biol. Chem. 264:16321-16331(1989).

[2]

X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 27-412 IN COMPLEX WITH ACETOACETYL-COA AND FAD, AND HOMOTETRAMERIZATION.
DOI=10.1074/jbc.M111296200; PubMed=11812788 [NCBI, ExPASy, EBI, Israel, Japan]
Battaile K.P., Molin-Case J., Paschke R., Wang M., Bennett D., Vockley J., Kim J.-J.P.;
"Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.";
J. Biol. Chem. 277:12200-12207(2002).

Comments

CATALYTIC ACTIVITY: Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor.
COFACTOR: FAD.
PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.
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

J05030; AAA40669.1; ALT_INIT; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

B34252; B34252.

NP_071957.1; -.

3D structure databases

PDB

1JQI; X-ray; 2.25 A; A/B=25-412.

[ExPASy / RCSB / EBI]

PDBsum

1JQI; -.

ModBase

P15651.

Protein-protein interaction databases

IntAct

P15651; -.

Organism-specific databases

RGD

620514; Acads.

Gene expression databases

ArrayExpress

P15651; -.

GermOnline

ENSRNOG00000001177; Rattus norvegicus.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004085;	Molecular function: butyryl-CoA dehydrogenase activity (inferred from electronic annotation from EC).
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; 1.
PS00073; ACYL_COA_DH_2; 1.

BLOCKS

P15651.

Genome annotation databases

Ensembl

ENSRNOG00000001177; Rattus norvegicus. [Contig view]

GeneID

64304; -.

KEGG

rno:64304; -.

Phylogenomic databases

HOVERGEN

P15651; -.

Other

ProtoNet

P15651.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 24`	`24`	`Mitochondrion.`
`CHAIN`	`25 412`	`388`	`Short-chain specific acyl-CoA dehydrogenase, mitochondrial.`	`PRO_0000000501`
`NP_BIND`	`152 161`	`10`	`FAD.`
`NP_BIND`	`185 187`	`3`	`FAD.`
`NP_BIND`	`365 369`	`5`	`FAD.`
`NP_BIND`	`394 396`	`3`	`FAD.`
`REGION`	`269 272`	`4`	`Substrate binding.`
`REGION`	`392 393`	`2`	`Substrate binding.`
`ACT_SITE`	`392 392`		`Proton acceptor.`
`BINDING`	`161 161`		`Substrate; via carbonyl oxygen.`
`BINDING`	`297 297`		`FAD.`
`HELIX`	`36 52`	`17`
`TURN`	`53 56`	`4`
`HELIX`	`57 63`	`7`
`HELIX`	`68 77`	`10`
`TURN`	`78 80`	`3`
`STRAND`	`81 84`	`4`
`HELIX`	`86 88`	`3`
`HELIX`	`95 108`	`14`
`HELIX`	`110 121`	`12`
`HELIX`	`124 130`	`7`
`HELIX`	`133 139`	`7`
`HELIX`	`141 143`	`3`
`STRAND`	`144 147`	`4`
`STRAND`	`150 153`	`4`
`STRAND`	`159 162`	`4`
`STRAND`	`169 172`	`4`
`STRAND`	`174 187`	`14`
`TURN`	`188 191`	`4`
`STRAND`	`193 201`	`9`
`HELIX`	`203 208`	`6`
`STRAND`	`209 218`	`10`
`STRAND`	`222 224`	`3`
`STRAND`	`230 232`	`3`
`STRAND`	`238 249`	`12`
`HELIX`	`250 252`	`3`
`STRAND`	`253 256`	`4`
`HELIX`	`260 296`	`37`
`STRAND`	`298 303`	`6`
`HELIX`	`304 306`	`3`
`HELIX`	`308 336`	`29`
`HELIX`	`342 367`	`26`
`HELIX`	`368 371`	`4`
`HELIX`	`378 385`	`8`
`HELIX`	`386 389`	`4`
`TURN`	`390 392`	`3`
`HELIX`	`395 410`	`16`

Sequence information

Length: 412 AA [This is the length of the unprocessed precursor]

Molecular weight: 44765 Da [This is the MW of the unprocessed precursor]

CRC64: 3E4A052FC99B8E14 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAALLARAG GSLGRALRAR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL 

        70         80         90        100        110        120 
DKEHLFPTSQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI ALEEISRGCA STGVIMSVNN 

       130        140        150        160        170        180 
SLYLGPILKF GSSQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN 

       190        200        210        220        230        240 
GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN 

       250        260        270        280        290        300 
LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRHAF 

       310        320        330        340        350        360 
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL AASEAATAIS 

       370        380        390        400        410 
HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS

P15651 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