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Q06319

- ACDS_MEGEL

UniProt

Q06319 - ACDS_MEGEL

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Protein

Acyl-CoA dehydrogenase, short-chain specific

Gene
N/A
Organism
Megasphaera elsdenii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Has an optimum specificity for 4-carbon length fatty acyl-CoAs.

Catalytic activityi

Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

FAD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei367 – 3671Proton acceptor

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: InterPro
  2. butyryl-CoA dehydrogenase activity Source: UniProtKB-EC
  3. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. fatty acid metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11937.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA dehydrogenase, short-chain specific (EC:1.3.8.1)
Alternative name(s):
Butyryl-CoA dehydrogenase
Short name:
BCAD
SCAD
OrganismiMegasphaera elsdenii
Taxonomic identifieri907 [NCBI]
Taxonomic lineageiBacteriaFirmicutesNegativicutesSelenomonadalesVeillonellaceaeMegasphaera

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi367 – 3671E → Q: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 383383Acyl-CoA dehydrogenase, short-chain specificPRO_0000201190Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
383
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2216
Turni23 – 275
Helixi28 – 347
Helixi39 – 468
Helixi50 – 523
Helixi57 – 593
Helixi62 – 654
Helixi69 – 8214
Helixi84 – 9613
Helixi98 – 1047
Helixi107 – 1126
Helixi114 – 1196
Beta strandi124 – 1274
Beta strandi133 – 1353
Helixi137 – 1393
Beta strandi143 – 1464
Beta strandi152 – 16211
Turni163 – 1664
Beta strandi168 – 1769
Beta strandi178 – 1814
Beta strandi184 – 1918
Beta strandi197 – 2026
Beta strandi213 – 22311
Helixi225 – 2273
Beta strandi228 – 2303
Helixi235 – 27137
Helixi279 – 2813
Helixi283 – 31230
Helixi317 – 34226
Helixi343 – 3475
Helixi353 – 3608
Helixi361 – 3644
Turni365 – 3673
Helixi370 – 38112

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BUCX-ray2.50A/B1-383[»]
ProteinModelPortaliQ06319.
SMRiQ06319. Positions 1-383.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06319.

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06319 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDFNLTDIQQ DFLKLAHDFG EKKLAPTVTE RDHKGIYDKE LIDELLSLGI
60 70 80 90 100
TGAYFEEKYG GSGDDGGDVL SYILAVEELA KYDAGVAITL SATVSLCANP
110 120 130 140 150
IWQFGTEAQK EKFLVPLVEG TKLGAFGLTE PNAGTDASGQ QTIATKNDDG
160 170 180 190 200
TYTLNGSKIF ITNGGAADIY IVFAMTDKSK GNHGITAFIL EDGTPGFTYG
210 220 230 240 250
KKEDKMGIHT SQTMELVFQD VKVPAENMLG EEGKGFKIAM MTLDGGRIGV
260 270 280 290 300
AAQALGIAEA ALADAVEYSK QRVQFGKPLC KFQSISFKLA DMKMQIEAAR
310 320 330 340 350
NLVYKAACKK QEGKPFTVDA AIAKRVASDV AMRVTTEAVQ IFGGYGYSEE
360 370 380
YPVARHMRDA KITQIYEGTN EVQLMVTGGA LLR
Length:383
Mass (Da):41,408
Last modified:October 1, 1996 - v1
Checksum:i3D68AAE34D9BBAB8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04528 Unassigned DNA. Translation: AAA03594.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04528 Unassigned DNA. Translation: AAA03594.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BUC X-ray 2.50 A/B 1-383 [» ]
ProteinModelPortali Q06319.
SMRi Q06319. Positions 1-383.
ModBasei Search...
MobiDBi Search...

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-11937.

Miscellaneous databases

EvolutionaryTracei Q06319.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiACDS_MEGEL
AccessioniPrimary (citable) accession number: Q06319
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3