Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q06319

- ACDS_MEGEL

UniProt

Q06319 - ACDS_MEGEL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Acyl-CoA dehydrogenase, short-chain specific

Gene
N/A
Organism
Megasphaera elsdenii
Status
Reviewed - Annotation score: 3 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

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 – 2216Combined sources
Turni23 – 275Combined sources
Helixi28 – 347Combined sources
Helixi39 – 468Combined sources
Helixi50 – 523Combined sources
Helixi57 – 593Combined sources
Helixi62 – 654Combined sources
Helixi69 – 8214Combined sources
Helixi84 – 9613Combined sources
Helixi98 – 1047Combined sources
Helixi107 – 1126Combined sources
Helixi114 – 1196Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi133 – 1353Combined sources
Helixi137 – 1393Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi152 – 16211Combined sources
Turni163 – 1664Combined sources
Beta strandi168 – 1769Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi184 – 1918Combined sources
Beta strandi197 – 2026Combined sources
Beta strandi213 – 22311Combined sources
Helixi225 – 2273Combined sources
Beta strandi228 – 2303Combined sources
Helixi235 – 27137Combined sources
Helixi279 – 2813Combined sources
Helixi283 – 31230Combined sources
Helixi317 – 34226Combined sources
Helixi343 – 3475Combined sources
Helixi353 – 3608Combined sources
Helixi361 – 3644Combined sources
Turni365 – 3673Combined sources
Helixi370 – 38112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

Q06319-1 [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:
EMBLi
GenBanki
DDBJi
Links Updated
L04528 Unassigned DNA. Translation: AAA03594.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04528 Unassigned DNA. Translation: AAA03594.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 84 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