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Protein

Acyl-CoA dehydrogenase, short-chain specific

Gene
N/A
Organism
Megasphaera elsdenii
Status
Reviewed-Annotation score: 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.
A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.By similarity

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei367Proton acceptor1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaFirmicutesNegativicutesVeillonellalesVeillonellaceaeMegasphaera

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi367E → Q: Loss of activity. 1

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002011901 – 383Acyl-CoA dehydrogenase, short-chain specificAdd BLAST383

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi1064535.MELS_2128.

Structurei

Secondary structure

1383
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 22Combined sources16
Turni23 – 27Combined sources5
Helixi28 – 34Combined sources7
Helixi39 – 46Combined sources8
Helixi50 – 52Combined sources3
Helixi57 – 59Combined sources3
Helixi62 – 65Combined sources4
Helixi69 – 82Combined sources14
Helixi84 – 96Combined sources13
Helixi98 – 104Combined sources7
Helixi107 – 112Combined sources6
Helixi114 – 119Combined sources6
Beta strandi124 – 127Combined sources4
Beta strandi133 – 135Combined sources3
Helixi137 – 139Combined sources3
Beta strandi143 – 146Combined sources4
Beta strandi152 – 162Combined sources11
Turni163 – 166Combined sources4
Beta strandi168 – 176Combined sources9
Beta strandi178 – 181Combined sources4
Beta strandi184 – 191Combined sources8
Beta strandi197 – 202Combined sources6
Beta strandi213 – 223Combined sources11
Helixi225 – 227Combined sources3
Beta strandi228 – 230Combined sources3
Helixi235 – 271Combined sources37
Helixi279 – 281Combined sources3
Helixi283 – 312Combined sources30
Helixi317 – 342Combined sources26
Helixi343 – 347Combined sources5
Helixi353 – 360Combined sources8
Helixi361 – 364Combined sources4
Turni365 – 367Combined sources3
Helixi370 – 381Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BUCX-ray2.50A/B1-383[»]
ProteinModelPortaliQ06319.
SMRiQ06319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06319.

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4105C1G. Bacteria.
COG1960. LUCA.

Family and domain databases

Gene3Di1.10.540.10. 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.
RefSeqiWP_014017064.1. NZ_JRPS01000018.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04528 Unassigned DNA. Translation: AAA03594.1.
RefSeqiWP_014017064.1. NZ_JRPS01000018.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BUCX-ray2.50A/B1-383[»]
ProteinModelPortaliQ06319.
SMRiQ06319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1064535.MELS_2128.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C1G. Bacteria.
COG1960. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11937.

Miscellaneous databases

EvolutionaryTraceiQ06319.

Family and domain databases

Gene3Di1.10.540.10. 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]
ProtoNetiSearch...

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 2, 2016
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.