NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-50.
DOI=10.1021/bi00091a026; PubMed=8399220 [NCBI, ExPASy, EBI, Israel, Japan]
Becker D.F., Fuchs J.A., Banfield D.K., Funk W.D., Macgillivray R.T.A., Stankovich M.T.;
"Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii.";
Biochemistry 32:10736-10742(1993).

[2]

X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1021/bi00007a009; PubMed=7857927 [NCBI, ExPASy, EBI, Israel, Japan]
Djordjevic S., Pace C.P., Stankovich M.T., Kim J.-J.P.;
"Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii.";
Biochemistry 34:2163-2171(1995).

Comments

FUNCTION: Has an optimum specificity for 4-carbon length fatty acyl-CoAs.
CATALYTIC ACTIVITY: Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor.
COFACTOR: FAD.
SUBUNIT: Homotetramer.
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

L04528; AAA03594.1; -; Unassigned_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1BUC; X-ray; 2.50 A; A/B=1-383.

[ExPASy / RCSB / EBI]

PDBsum

1BUC; -.

ModBase

Q06319.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11937; -.

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.

Other

Q06319; -.

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 383`	`383`	`Acyl-CoA dehydrogenase, short-chain specific.`	`PRO_0000201190`
`ACT_SITE`	`367 367`		`Proton acceptor.`
`MUTAGEN`	`367 367`		`E->Q: Loss of activity.`
`HELIX`	`7 22`	`16`
`TURN`	`23 27`	`5`
`HELIX`	`28 34`	`7`
`HELIX`	`39 46`	`8`
`HELIX`	`50 52`	`3`
`HELIX`	`57 59`	`3`
`HELIX`	`62 65`	`4`
`HELIX`	`69 82`	`14`
`HELIX`	`84 96`	`13`
`HELIX`	`98 104`	`7`
`HELIX`	`107 112`	`6`
`HELIX`	`114 119`	`6`
`STRAND`	`124 127`	`4`
`STRAND`	`133 135`	`3`
`HELIX`	`137 139`	`3`
`STRAND`	`143 146`	`4`
`STRAND`	`152 162`	`11`
`TURN`	`163 166`	`4`
`STRAND`	`168 176`	`9`
`STRAND`	`178 181`	`4`
`STRAND`	`184 191`	`8`
`STRAND`	`197 202`	`6`
`STRAND`	`205 207`	`3`
`STRAND`	`213 223`	`11`
`HELIX`	`225 227`	`3`
`STRAND`	`228 230`	`3`
`HELIX`	`235 271`	`37`
`HELIX`	`279 281`	`3`
`HELIX`	`283 312`	`30`
`HELIX`	`317 342`	`26`
`HELIX`	`343 347`	`5`
`HELIX`	`353 360`	`8`
`HELIX`	`361 364`	`4`
`TURN`	`365 367`	`3`
`HELIX`	`370 381`	`12`

Sequence information

Length: 383 AA [This is the length of the unprocessed precursor]

Molecular weight: 41408 Da [This is the MW of the unprocessed precursor]

CRC64: 3D68AAE34D9BBAB8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDFNLTDIQQ DFLKLAHDFG EKKLAPTVTE RDHKGIYDKE LIDELLSLGI TGAYFEEKYG 

        70         80         90        100        110        120 
GSGDDGGDVL SYILAVEELA KYDAGVAITL SATVSLCANP IWQFGTEAQK EKFLVPLVEG 

       130        140        150        160        170        180 
TKLGAFGLTE PNAGTDASGQ QTIATKNDDG TYTLNGSKIF ITNGGAADIY IVFAMTDKSK 

       190        200        210        220        230        240 
GNHGITAFIL EDGTPGFTYG KKEDKMGIHT SQTMELVFQD VKVPAENMLG EEGKGFKIAM 

       250        260        270        280        290        300 
MTLDGGRIGV AAQALGIAEA ALADAVEYSK QRVQFGKPLC KFQSISFKLA DMKMQIEAAR 

       310        320        330        340        350        360 
NLVYKAACKK QEGKPFTVDA AIAKRVASDV AMRVTTEAVQ IFGGYGYSEE YPVARHMRDA 

       370        380 
KITQIYEGTN EVQLMVTGGA LLR

Q06319 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