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Protein

Dihydrolipoyl dehydrogenase

Gene

TTHA0233

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.UniRule annotation

Cofactori

FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121FADCombined sources
Binding sitei48 – 481FADCombined sources
Binding sitei53 – 531FADCombined sources
Binding sitei272 – 2721FADCombined sources
Binding sitei309 – 3091FADCombined sources
Binding sitei440 – 4401FAD; via carbonyl oxygenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 172FADCombined sources
Nucleotide bindingi36 – 372FADCombined sources
Nucleotide bindingi43 – 442FADCombined sources
Nucleotide bindingi114 – 1152FADCombined sources
Nucleotide bindingi315 – 3173FADCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

GlycolysisSAAS annotation

Keywords - Ligandi

FADUniRule annotationCombined sources, Flavoprotein, NADUniRule annotation, Nucleotide-bindingCombined sources, PyruvateImported

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-242-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenaseUniRule annotation (EC:1.8.1.4UniRule annotation)
Gene namesi
Ordered Locus Names:TTHA0233Imported
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)Imported
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 49Combined sources

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0233.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQ6X-ray1.60A/B1-464[»]
2EQ8X-ray1.94A/B/D/E1-464[»]
2EQ9X-ray2.09A/B/D/E/G/H/J/K1-464[»]
ProteinModelPortaliQ5SLR0.
SMRiQ5SLR0. Positions 4-463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLR0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 324318FAD/NAD-binding_domInterPro annotationAdd
BLAST
Domaini342 – 450109Pyr_redox_dimInterPro annotationAdd
BLAST

Keywords - Domaini

Redox-active centerUniRule annotation

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276708.
KOiK00382.
OMAiKRVMDST.
PhylomeDBiQ5SLR0.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SLR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPMKTYDLI VIGTGPGGYH AAIRAAQLGL KVLAVEAGEV GGVCLNVGCI
60 70 80 90 100
PTKALLHAAE TLHHLKVAEG FGLKAKPELD LKKLGGWRDQ VVKKLTGGVG
110 120 130 140 150
TLLKGNGVEL LRGFARLVGP KEVEVGGERY GAKSLILATG SEPLELKGFP
160 170 180 190 200
FGEDVWDSTR ALKVEEGLPK RLLVIGGGAV GLELGQVYRR LGAEVTLIEY
210 220 230 240 250
MPEILPQGDP ETAALLRRAL EKEGIRVRTK TKAVGYEKKK DGLHVRLEPA
260 270 280 290 300
EGGEGEEVVV DKVLVAVGRK PRTEGLGLEK AGVKVDERGF IRVNARMETS
310 320 330 340 350
VPGVYAIGDA ARPPLLAHKA MREGLIAAEN AAGKDSAFDY QVPSVVYTSP
360 370 380 390 400
EWAGVGLTEE EAKRAGYKVK VGKFPLAASG RALTLGGAEG MVKVVGDEET
410 420 430 440 450
DLLLGVFIVG PQAGELIAEA ALALEMGATL TDLALTVHPH PTLSESLMEA
460
AEAFHKQAIH ILNR
Length:464
Mass (Da):49,084
Last modified:December 21, 2004 - v1
Checksum:iE4B03C80109B5E9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70056.1.
RefSeqiWP_011227797.1. NC_006461.1.
YP_143499.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70056; BAD70056; BAD70056.
GeneIDi3169717.
KEGGittj:TTHA0233.
PATRICi23955409. VBITheThe93045_0232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70056.1.
RefSeqiWP_011227797.1. NC_006461.1.
YP_143499.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQ6X-ray1.60A/B1-464[»]
2EQ8X-ray1.94A/B/D/E1-464[»]
2EQ9X-ray2.09A/B/D/E/G/H/J/K1-464[»]
ProteinModelPortaliQ5SLR0.
SMRiQ5SLR0. Positions 4-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70056; BAD70056; BAD70056.
GeneIDi3169717.
KEGGittj:TTHA0233.
PATRICi23955409. VBITheThe93045_0232.

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276708.
KOiK00382.
OMAiKRVMDST.
PhylomeDBiQ5SLR0.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-242-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SLR0.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ5SLR0_THET8
AccessioniPrimary (citable) accession number: Q5SLR0
Entry historyi
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: September 7, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.UniRule annotation

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.