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Q5FNM2

- Q5FNM2_GLUOX

UniProt

Q5FNM2 - Q5FNM2_GLUOX

Protein

Dihydrolipoyl dehydrogenase

Gene

GOX2292

Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 FAD per subunit.UniRule annotation
    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

    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.
    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: October 1, 2014
    This is version 71 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
    The active site is a redox-active disulfide bond By similarity.

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3