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Protein

Dihydrolipoyl dehydrogenase

Gene

GOX2292

Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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

GO - Molecular functioni

  1. dihydrolipoyl dehydrogenase activity Source: UniProtKB-EC
  2. flavin adenine dinucleotide binding Source: InterPro
  3. mercury (II) reductase activity Source: InterPro
  4. mercury ion binding Source: InterPro
  5. NADP binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. detoxification of mercury ion Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Ligandi

FADUniRule annotation, Flavoprotein, NADUniRule annotation

Enzyme and pathway databases

BioCyciGOXY290633:GHB3-2290-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenaseUniRule annotation (EC:1.8.1.4UniRule annotation)
Gene namesi
Ordered Locus Names:GOX2292Imported
OrganismiGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)Imported
Taxonomic identifieri290633 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter
ProteomesiUP000006375: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi290633.GOX2292.

Structurei

3D structure databases

ProteinModelPortaliQ5FNM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.UniRule annotation

Keywords - Domaini

Redox-active centerUniRule annotation

Phylogenomic databases

HOGENOMiHOG000276708.
KOiK00382.
OMAiTMSEAVM.
OrthoDBiEOG6QCD6D.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5FNM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDTFDLIVV GGGPGGYVAA LRASQLGMSV ALVESTHFGG VCLNWGCIPT
60 70 80 90 100
KALLRSSEIH HLLHELGTFG LSADNISFDL SKIVGRSRSI ARRMGGGIAH
110 120 130 140 150
LLKKTKVTTF DGRAKLAGRS GEAHQVAITK DGAAVATIKA PHVILATGAR
160 170 180 190 200
GRQLPGLETD GTLIWGAREA MTPKELPKRL LVIGSGAIGI EFASFYRNMG
210 220 230 240 250
SEVTIAEVAD RILIAEDPEI SAAARKAFEK QGMKIITSAK VGPLNKGENE
260 270 280 290 300
VSTTIESPTG KVDLTVDRVI CAVGIVGNVE DLGLEGTKVQ VERTHIVTDG
310 320 330 340 350
FCRTGEPGIY AIGDVAGAPW LAHKASHEGI LCVEKIAGRS PQPLHPLNIP
360 370 380 390 400
GCTYSRPQIA SVGLSEEKAI AAGHKVKVGR FPFIANGKAV AMGETDGMVK
410 420 430 440 450
TVFDATSGEL LGAHMIGAEV TEMIQGYVIT RTGELTEAEL VETVFPHPTI
460
SETMHEATLA AFDGPLHI
Length:468
Mass (Da):49,242
Last modified:March 1, 2005 - v1
Checksum:i475199B0B0FC0B3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000009 Genomic DNA. Translation: AAW62025.1.
RefSeqiYP_192681.1. NC_006677.1.

Genome annotation databases

EnsemblBacteriaiAAW62025; AAW62025; GOX2292.
GeneIDi3249911.
KEGGigox:GOX2292.
PATRICi32612550. VBIGluOxy81109_2608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000009 Genomic DNA. Translation: AAW62025.1.
RefSeqiYP_192681.1. NC_006677.1.

3D structure databases

ProteinModelPortaliQ5FNM2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290633.GOX2292.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW62025; AAW62025; GOX2292.
GeneIDi3249911.
KEGGigox:GOX2292.
PATRICi32612550. VBIGluOxy81109_2608.

Phylogenomic databases

HOGENOMiHOG000276708.
KOiK00382.
OMAiTMSEAVM.
OrthoDBiEOG6QCD6D.

Enzyme and pathway databases

BioCyciGOXY290633:GHB3-2290-MONOMER.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
    Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
    Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 621HImported.

Entry informationi

Entry nameiQ5FNM2_GLUOX
AccessioniPrimary (citable) accession number: Q5FNM2
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2005
Last sequence update: March 1, 2005
Last modified: March 4, 2015
This is version 75 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

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.