Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5LRA7

- Q5LRA7_RUEPO

UniProt

Q5LRA7 - Q5LRA7_RUEPO

Protein

Dihydrolipoyl dehydrogenase

Gene

SPO2222

Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Feb 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 FAD per subunit.UniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: TIGR
    2. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    OxidoreductaseUniRule annotation

    Keywords - Ligandi

    FADUniRule annotation, Flavoprotein, NADUniRule annotation, PyruvateImported

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyl dehydrogenaseUniRule annotation (EC:1.8.1.4UniRule annotation)
    Gene namesi
    Ordered Locus Names:SPO2222Imported
    OrganismiRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)Imported
    Taxonomic identifieri246200 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
    ProteomesiUP000001023: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic pyruvate dehydrogenase complex Source: TIGR

    Interactioni

    Protein-protein interaction databases

    STRINGi246200.SPO2222.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5LRA7.
    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.
    OMAiKLKIPGC.
    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.

    Q5LRA7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQSYDVIV IGAGPGGYVA AIRAAQLGLK ACVVEREHLG GICLNWGCIP    50
    TKALLRSSEV FHLMERAKEF GLKADNIGYD LDAVVKRSRG VAKQLSGGIG 100
    HLMKKNKIDV VMGEATIPAK GKVSVKTDKG TQELTAKNII LATGARAREL 150
    PGLEADGDLV WTYKHALQPV RMPKKLLVIG SGAIGIEFAS FYNTLGADTT 200
    VVEVMDRVLP VEDAEISAFA KKSFVKQGMK IMEKSMVKQL DRAKGKVTAH 250
    IETGGKVEKL EFDTVISAVG IVGNVENLGL EALGVKIDRT HVVTDAYCRT 300
    GVEGLYAIGD IAGAPWLAHK ASHEGVMVAE LIAGKHAHPV KPESIAGCTY 350
    CHPQVASVGY TEAKAKELGY DIKVGRFPFI GNGKAIALGE VEGMIKTIFD 400
    AKTGELLGAH MVGAEVTEMI QGYVVGRQLE TTEEDLMHTV FPHPTLSEMM 450
    HESVLDAYGR VIHM 464
    Length:464
    Mass (Da):49,696
    Last modified:February 1, 2005 - v1
    Checksum:i590944C589FBCDA7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000031 Genomic DNA. Translation: AAV95488.1.
    RefSeqiYP_167448.1. NC_003911.12.

    Genome annotation databases

    EnsemblBacteriaiAAV95488; AAV95488; SPO2222.
    GeneIDi3194814.
    KEGGisil:SPO2222.
    PATRICi23377797. VBIRuePom114501_2250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000031 Genomic DNA. Translation: AAV95488.1 .
    RefSeqi YP_167448.1. NC_003911.12.

    3D structure databases

    ProteinModelPortali Q5LRA7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246200.SPO2222.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV95488 ; AAV95488 ; SPO2222 .
    GeneIDi 3194814.
    KEGGi sil:SPO2222.
    PATRICi 23377797. VBIRuePom114501_2250.

    Phylogenomic databases

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

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700808 / DSM 15171 / DSS-3Imported.

    Entry informationi

    Entry nameiQ5LRA7_RUEPO
    AccessioniPrimary (citable) accession number: Q5LRA7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 1, 2005
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    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