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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei87 – 871Substrate1 Publication
Binding sitei91 – 911Substrate1 Publication
Binding sitei135 – 1351FAD1 Publication
Binding sitei135 – 1351Substrate; via carbonyl oxygen1 Publication
Binding sitei181 – 1811Substrate1 Publication
Binding sitei271 – 2711FAD1 Publication
Binding sitei340 – 3401FAD; via carbonyl oxygen1 Publication
Binding sitei344 – 3441FAD; via amide nitrogen1 Publication
Active sitei367 – 3671Proton acceptorCurated
Binding sitei385 – 3851Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi126 – 1294FAD1 Publication
Nucleotide bindingi159 – 1613FAD1 Publication
Nucleotide bindingi281 – 2844FAD1 Publication
Nucleotide bindingi367 – 3715FAD1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801A → E: Loses the FAD cofactor and dehydrogenase activity. 1 Publication
Mutagenesisi88 – 881V → S: A residual dehydrogenase activity is observed. 1 Publication
Mutagenesisi366 – 3661V → Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 389389Glutaryl-CoA dehydrogenasePRO_0000418764Add
BLAST

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1
389
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2317Combined sources
Turni24 – 274Combined sources
Helixi28 – 347Combined sources
Turni39 – 424Combined sources
Helixi43 – 486Combined sources
Turni49 – 524Combined sources
Beta strandi54 – 563Combined sources
Helixi58 – 603Combined sources
Helixi68 – 8215Combined sources
Helixi84 – 9310Combined sources
Turni94 – 974Combined sources
Helixi98 – 1047Combined sources
Helixi107 – 11812Combined sources
Beta strandi133 – 1353Combined sources
Helixi137 – 1393Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi148 – 16114Combined sources
Turni162 – 1654Combined sources
Beta strandi167 – 1759Combined sources
Helixi177 – 1826Combined sources
Beta strandi183 – 1897Combined sources
Turni191 – 1933Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi212 – 22312Combined sources
Helixi224 – 2263Combined sources
Beta strandi227 – 2304Combined sources
Turni231 – 2333Combined sources
Helixi234 – 27037Combined sources
Helixi278 – 2803Combined sources
Helixi282 – 31029Combined sources
Helixi317 – 34226Combined sources
Helixi343 – 3475Combined sources
Helixi352 – 3598Combined sources
Helixi362 – 3654Combined sources
Beta strandi366 – 3683Combined sources
Helixi370 – 38112Combined sources

3D structure databases

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

Publicationsi

  1. "Decarboxylating and nondecarboxylating glutaryl-coenzyme A dehydrogenases in the aromatic metabolism of obligately anaerobic bacteria."
    Wischgoll S., Taubert M., Peters F., Jehmlich N., von Bergen M., Boll M.
    J. Bacteriol. 191:4401-4409(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, COFACTOR, ENZYME REGULATION.
    Strain: ATCC 33890 / DSM 2059 / 1be1.
  2. "Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme A dehydrogenases."
    Wischgoll S., Demmer U., Warkentin E., Gunther R., Boll M., Ermler U.
    Biochemistry 49:5350-5357(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FAD AND SUBSTRATE, COFACTOR, MUTAGENESIS OF ALA-80; VAL-88 AND VAL-366.
    Strain: ATCC 33890 / DSM 2059 / 1be1.

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: May 11, 2016
This is version 38 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.