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Q5FNM2

- Q5FNM2_GLUOX

UniProt

Q5FNM2 - Q5FNM2_GLUOX

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Protein
Dihydrolipoyl dehydrogenase
Gene
GOX2292
Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Status
Unreviewed - 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.

Cofactori

Binds 1 FAD per subunit By similarity.

GO - Molecular functioni

  1. dihydrolipoyl dehydrogenase activity Source: UniProtKB-EC
  2. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis 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.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active centerUniRule annotation

Phylogenomic databases

HOGENOMiHOG000276708.
KOiK00382.
OMAiKSLIPGC.
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

MCDTFDLIVV GGGPGGYVAA LRASQLGMSV ALVESTHFGG VCLNWGCIPT    50
KALLRSSEIH HLLHELGTFG LSADNISFDL SKIVGRSRSI ARRMGGGIAH 100
LLKKTKVTTF DGRAKLAGRS GEAHQVAITK DGAAVATIKA PHVILATGAR 150
GRQLPGLETD GTLIWGAREA MTPKELPKRL LVIGSGAIGI EFASFYRNMG 200
SEVTIAEVAD RILIAEDPEI SAAARKAFEK QGMKIITSAK VGPLNKGENE 250
VSTTIESPTG KVDLTVDRVI CAVGIVGNVE DLGLEGTKVQ VERTHIVTDG 300
FCRTGEPGIY AIGDVAGAPW LAHKASHEGI LCVEKIAGRS PQPLHPLNIP 350
GCTYSRPQIA SVGLSEEKAI AAGHKVKVGR FPFIANGKAV AMGETDGMVK 400
TVFDATSGEL LGAHMIGAEV TEMIQGYVIT RTGELTEAEL VETVFPHPTI 450
SETMHEATLA AFDGPLHI 468
Length:468
Mass (Da):49,242
Last modified:March 1, 2005 - v1
Checksum:i475199B0B0FC0B3C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP000009 Genomic DNA. Translation: AAW62025.1 .
RefSeqi YP_192681.1. NC_006677.1.

3D structure databases

ProteinModelPortali Q5FNM2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 290633.GOX2292.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW62025 ; AAW62025 ; GOX2292 .
GeneIDi 3249911.
KEGGi gox:GOX2292.
PATRICi 32612550. VBIGluOxy81109_2608.

Phylogenomic databases

HOGENOMi HOG000276708.
KOi K00382.
OMAi KSLIPGC.
OrthoDBi EOG6QCD6D.

Enzyme and pathway databases

BioCyci GOXY290633:GHB3-2290-MONOMER.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. 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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01350. lipoamide_DH. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 70 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 By similarity.

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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