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Protein
Submitted name:

Acyl-CoA dehydrogenase

Gene

TTHA1938

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

FADUniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei134FADCombined sources1
Binding sitei274FADCombined sources1
Binding sitei342FAD; via carbonyl oxygenCombined sources1
Binding sitei346FAD; via amide nitrogenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi125 – 128FADCombined sources4
Nucleotide bindingi158 – 160FADCombined sources3
Nucleotide bindingi284 – 285FADCombined sources2
Nucleotide bindingi371 – 373FADCombined sources3

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Ligandi

FADUniRule annotationCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1929-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Acyl-CoA dehydrogenaseImported
Gene namesi
Ordered Locus Names:TTHA1938Imported
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)Imported
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1938.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WS9X-ray2.30A/B1-387[»]
2CX9X-ray2.00A/B/C/D1-387[»]
2D29X-ray1.65A/B1-387[»]
ProteinModelPortaliQ5SGZ2.
SMRiQ5SGZ2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SGZ2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 120Acyl-CoA_dh_NInterPro annotationAdd BLAST111
Domaini125 – 222Acyl-CoA_dh_MInterPro annotationAdd BLAST98
Domaini235 – 384Acyl-CoA_dh_1InterPro annotationAdd BLAST150

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C1G. Bacteria.
COG1960. LUCA.
HOGENOMiHOG000131659.
OMAiTEHNTGS.
PhylomeDBiQ5SGZ2.

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.

Q5SGZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLWFEEGAE ERQVLGPFRE FLKAEVAPGA AERDRTGAFP WDLVRKLAEF
60 70 80 90 100
GVFGALVPEA YGGAGLSTRL FARMVEAIAY YDGALALTVA SHNSLATGHI
110 120 130 140 150
LLAGSEAQKE AFLPKLASGE ALGAWGLTEP GSGSDAAALK TKAEKVEGGW
160 170 180 190 200
RLNGTKQFIT QGSVAGVYVV MARTDPPPSP ERKHQGISAF AFFRPERGLK
210 220 230 240 250
VGRKEEKLGL TASDTAQLIL EDLFVPEEAL LGERGKGFYD VLRVLDGGRI
260 270 280 290 300
GIAAMAVGLG QAALDYALAY AKGREAFGRP IAEFEGVSFK LAEAATELEA
310 320 330 340 350
ARLLYLKAAE LKDAGRPFTL EAAQAKLFAS EAAVKACDEA IQILGGYGYV
360 370 380
KDYPVERYWR DARLTRIGEG TSEILKLVIA RRLLEAV
Length:387
Mass (Da):41,532
Last modified:December 21, 2004 - v1
Checksum:i7CC9810AAB33555A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71761.1.
RefSeqiWP_011229031.1. NC_006461.1.
YP_145204.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71761; BAD71761; BAD71761.
GeneIDi3168367.
KEGGittj:TTHA1938.
PATRICi23958855. VBITheThe93045_1909.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71761.1.
RefSeqiWP_011229031.1. NC_006461.1.
YP_145204.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WS9X-ray2.30A/B1-387[»]
2CX9X-ray2.00A/B/C/D1-387[»]
2D29X-ray1.65A/B1-387[»]
ProteinModelPortaliQ5SGZ2.
SMRiQ5SGZ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71761; BAD71761; BAD71761.
GeneIDi3168367.
KEGGittj:TTHA1938.
PATRICi23958855. VBITheThe93045_1909.

Phylogenomic databases

eggNOGiENOG4105C1G. Bacteria.
COG1960. LUCA.
HOGENOMiHOG000131659.
OMAiTEHNTGS.
PhylomeDBiQ5SGZ2.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1929-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SGZ2.

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 nameiQ5SGZ2_THET8
AccessioniPrimary (citable) accession number: Q5SGZ2
Entry historyi
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.