Reviewed, UniProtKB/Swiss-Prot Q06319 (ACDS_MEGEL)

Names and origin

Protein names	Recommended name:     Acyl-CoA dehydrogenase, short-chain specific     EC=1.3.99.2 Alternative name(s):     SCAD     Butyryl-CoA dehydrogenase       Short name=BCAD
Organism	Megasphaera elsdenii
Taxonomic identifier	907 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Clostridiales › Veillonellaceae › Megasphaera

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 structure	Homotetramer.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro butyryl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 383

383

Acyl-CoA dehydrogenase, short-chain specific

PRO_0000201190

Sites

Active site

367

1

Proton acceptor

Experimental info

Mutagenesis

367

1

E → Q: Loss of activity.

Secondary structure

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383

Helix Strand Turn

Details...

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

Beta strand

124 – 127

4

Beta strand

133 – 135

3

Helix

137 – 139

3

Beta strand

143 – 146

4

Beta strand

152 – 162

11

Turn

163 – 166

4

Beta strand

168 – 176

9

Beta strand

178 – 181

4

Beta strand

184 – 191

8

Beta strand

197 – 202

6

Beta strand

205 – 207

3

Beta strand

213 – 223

11

Helix

225 – 227

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	Q06319-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 3D68AAE34D9BBAB8	FASTA	383	41,408
	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

References

[1]	"Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii." Becker D.F., Fuchs J.A., Banfield D.K., Funk W.D., Macgillivray R.T.A., Stankovich M.T. Biochemistry 32:10736-10742(1993) [PubMed: 8399220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-50.
[2]	"Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii." Djordjevic S., Pace C.P., Stankovich M.T., Kim J.-J.P. Biochemistry 34:2163-2171(1995) [PubMed: 7857927] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

L04528 Unassigned DNA. Translation: AAA03594.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BUC	X-ray	2.50	A/B	1-383	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11937.

BRENDA

1.3.99.2. 1234.

Family and domain databases

InterPro

IPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_M.
IPR013786. AcylCoA_DH/ox_N.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]

Gene3D

G3DSA: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.

Pfam

PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]

PROSITE

PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ACDS_MEGEL

Accession

Primary (citable) accession number: Q06319

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)