Skip Header

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

Glutaryl-CoA dehydrogenase

Gene

Acd

Organism
Desulfococcus multivorans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydrogenation of Glutaryl-CoA to glutaconyl-CoA.1 Publication

Catalytic activityi

Glutaryl-CoA + acceptor = (E)-glutaconyl-CoA + reduced acceptor.1 Publication

Cofactori

FAD2 Publications

Enzyme regulationi

Inhibited by glutaconyl-CoA.1 Publication

Kineticsi

  1. KM=25 µM for glutaryl-CoA
  1. Vmax=11 mmol/min/mg enzyme

Pathwayi: benzoyl-CoA degradation

This protein is involved in the pathway benzoyl-CoA degradation, which is part of Aromatic compound metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway benzoyl-CoA degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei87Substrate1 Publication1
Binding sitei91Substrate1 Publication1
Binding sitei135FAD1 Publication1
Binding sitei135Substrate; via carbonyl oxygen1 Publication1
Binding sitei181Substrate1 Publication1
Binding sitei271FAD1 Publication1
Binding sitei340FAD; via carbonyl oxygen1 Publication1
Binding sitei344FAD; via amide nitrogen1 Publication1
Active sitei367Proton acceptorCurated1
Binding sitei385Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi126 – 129FAD1 Publication4
Nucleotide bindingi159 – 161FAD1 Publication3
Nucleotide bindingi281 – 284FAD1 Publication4
Nucleotide bindingi367 – 371FAD1 Publication5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

FAD, Flavoprotein, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.3.99.32. 1889.
UniPathwayiUPA00739.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaryl-CoA dehydrogenase (EC:1.3.99.32)
Short name:
GDH(Des)
Gene namesi
Name:Acd
OrganismiDesulfococcus multivorans
Taxonomic identifieri897 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi80A → E: Loses the FAD cofactor and dehydrogenase activity. 1 Publication1
Mutagenesisi88V → S: A residual dehydrogenase activity is observed. 1 Publication1
Mutagenesisi366V → Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004187641 – 389Glutaryl-CoA dehydrogenaseAdd BLAST389

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1389
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 23Combined sources17
Turni24 – 27Combined sources4
Helixi28 – 34Combined sources7
Turni39 – 42Combined sources4
Helixi43 – 48Combined sources6
Turni49 – 52Combined sources4
Beta strandi54 – 56Combined sources3
Helixi58 – 60Combined sources3
Helixi68 – 82Combined sources15
Helixi84 – 93Combined sources10
Turni94 – 97Combined sources4
Helixi98 – 104Combined sources7
Helixi107 – 118Combined sources12
Beta strandi133 – 135Combined sources3
Helixi137 – 139Combined sources3
Beta strandi143 – 146Combined sources4
Beta strandi148 – 161Combined sources14
Turni162 – 165Combined sources4
Beta strandi167 – 175Combined sources9
Helixi177 – 182Combined sources6
Beta strandi183 – 189Combined sources7
Turni191 – 193Combined sources3
Beta strandi197 – 201Combined sources5
Beta strandi212 – 223Combined sources12
Helixi224 – 226Combined sources3
Beta strandi227 – 230Combined sources4
Turni231 – 233Combined sources3
Helixi234 – 270Combined sources37
Helixi278 – 280Combined sources3
Helixi282 – 310Combined sources29
Helixi317 – 342Combined sources26
Helixi343 – 347Combined sources5
Helixi352 – 359Combined sources8
Helixi362 – 365Combined sources4
Beta strandi366 – 368Combined sources3
Helixi370 – 381Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MPIX-ray2.05A/B/C/D1-389[»]
3MPJX-ray2.10A/B/D/E/F/G1-389[»]
ProteinModelPortaliC3UVB0.
SMRiC3UVB0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiC3UVB0.

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Phylogenomic databases

KOiK16173.

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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C3UVB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFNLSKELQ MLQKEVRNFV NKKIVPFADQ WDNENHFPYE EAVRPMGELG
60 70 80 90 100
FFGTVIPEEY GGEGMDQGWL AAMIVTEEIA RGSSALRVQL NMEVLGCAYT
110 120 130 140 150
ILTYGSEALK KKYVPKLSSA EFLGGFGITE PDAGSDVMAM SSTAEDKGDH
160 170 180 190 200
WLLNGSKTWI SNAAQADVLI YYAYTDKAAG SRGLSAFVIE PRNFPGIKTS
210 220 230 240 250
NLEKLGSHAS PTGELFLDNV KVPKENILGK PGDGARIVFG SLNHTRLSAA
260 270 280 290 300
AGGVGLAQAC LDAAIKYCNE RRQFGKPIGD FQMNQDMIAQ MAVEVEAARL
310 320 330 340 350
LAYKAAAAKD EGRLNNGLDV AMAKYAAGEA VSKCANYAMR ILGAYGYSTE
360 370 380
YPVARFYRDA PTYYMVEGSA NICKMIIALD QLGVRKANR
Length:389
Mass (Da):42,382
Last modified:June 16, 2009 - v1
Checksum:iF479601F35A96975
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ688103 Genomic DNA. Translation: ACP50614.1.

Genome annotation databases

KEGGiag:ACP50614.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ688103 Genomic DNA. Translation: ACP50614.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MPIX-ray2.05A/B/C/D1-389[»]
3MPJX-ray2.10A/B/D/E/F/G1-389[»]
ProteinModelPortaliC3UVB0.
SMRiC3UVB0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:ACP50614.

Phylogenomic databases

KOiK16173.

Enzyme and pathway databases

UniPathwayiUPA00739.
BRENDAi1.3.99.32. 1889.

Miscellaneous databases

EvolutionaryTraceiC3UVB0.

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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACD_DESML
AccessioniPrimary (citable) accession number: C3UVB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: June 16, 2009
Last modified: November 2, 2016
This is version 39 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.