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Protein

Acyl-CoA dehydrogenase, short-chain specific

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

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandFAD, 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

DrugBankiDB03059 Acetoacetyl-Coenzyme A
DB03147 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.

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
InterProiView protein in InterPro
IPR006089 Acyl-CoA_DH_CS
IPR006091 Acyl-CoA_Oxase/DH_cen-dom
IPR036250 AcylCo_DH-like_C
IPR009075 AcylCo_DH/oxidase_C
IPR013786 AcylCoA_DH/ox_N
IPR037069 AcylCoA_DH/ox_N_sf
IPR009100 AcylCoA_DH/oxidase_NM_dom
PfamiView protein in Pfam
PF00441 Acyl-CoA_dh_1, 1 hit
PF02770 Acyl-CoA_dh_M, 1 hit
PF02771 Acyl-CoA_dh_N, 1 hit
SUPFAMiSSF47203 SSF47203, 1 hit
SSF56645 SSF56645, 1 hit
PROSITEiView protein in PROSITE
PS00072 ACYL_COA_DH_1, 1 hit
PS00073 ACYL_COA_DH_2, 1 hit

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_NQMW01000006.1

Genome annotation databases

GeneIDi36311878

Similar proteinsi

Entry informationi

Entry nameiACDS_MEGEL
AccessioniPrimary (citable) accession number: Q06319
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 97 of the entry and version 1 of the sequence. See 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

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