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A9IN89

- LLDD_BART1

UniProt

A9IN89 - LLDD_BART1

Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Bartonella tribocorum (strain CIP 105476 / IBS 506)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain.UniRule annotation

    Catalytic activityi

    (S)-lactate + an oxidized electron acceptor = pyruvate + a reduced electron acceptor.UniRule annotation

    Cofactori

    FMN.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei24 – 241SubstrateUniRule annotation
    Binding sitei106 – 1061FMNUniRule annotation
    Binding sitei127 – 1271FMNUniRule annotation
    Binding sitei129 – 1291SubstrateUniRule annotation
    Binding sitei155 – 1551FMNUniRule annotation
    Binding sitei164 – 1641SubstrateUniRule annotation
    Binding sitei251 – 2511FMNUniRule annotation
    Active sitei275 – 2751Proton acceptorUniRule annotation
    Binding sitei278 – 2781SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi306 – 33025FMNUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. FMN binding Source: InterPro
    2. L-lactate dehydrogenase (cytochrome) activity Source: InterPro

    GO - Biological processi

    1. lactate oxidation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BioCyciBTRI382640:GJEK-263-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-lactate dehydrogenaseUniRule annotation (EC:1.1.-.-UniRule annotation)
    Gene namesi
    Name:lldDUniRule annotation
    Ordered Locus Names:BT_0300
    OrganismiBartonella tribocorum (strain CIP 105476 / IBS 506)
    Taxonomic identifieri382640 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
    ProteomesiUP000001592: Chromosome

    Subcellular locationi

    Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 383383L-lactate dehydrogenasePRO_0000383414Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi382640.Btr_0300.

    Structurei

    3D structure databases

    ProteinModelPortaliA9IN89.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 380380FMN hydroxy acid dehydrogenaseUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.UniRule annotation
    Contains 1 FMN hydroxy acid dehydrogenase domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1304.
    KOiK00101.
    OMAiDANESML.
    OrthoDBiEOG6HMXBG.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01559. L_lact_dehydr.
    InterProiIPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    IPR020920. L-lactate_DHase_bac.
    [Graphical view]
    PfamiPF01070. FMN_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A9IN89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIIASTFDYR KAAKRRLPPF LFHYIDGGAY AEETLRRNCS DLQALALRQR    50
    ILRQVGGVDL SIKLFEQRLD LPIVLAPVGL TGMYARRGEV QAAHAATAKG 100
    IPFTLSSVSV CPIAEVQEAV GGGFWFQLYV LKDRGFMRDA LERAWASGVR 150
    TLVFTVDMPI PGARYRDAHS GMSGPYAGLR RFLQAFTHPH WAWNVGIMGR 200
    PHDLGNVSTY LEKKIALDDY VGWLGANFDP SIGWHDLQWI RDFWKGKMIL 250
    KGILDPEDAR EAVQFGADGI VVSNHGGRQL DGVLSTARAL PAIAEAVKND 300
    LVILADSGVR SGLDVVRMIA QGADAVMIGR AFVYALAAAG EKGVAHLLDL 350
    FANEMRVAMT LTGAQTLKEI TCESLVNTDA FKQ 383
    Length:383
    Mass (Da):41,985
    Last modified:February 5, 2008 - v1
    Checksum:i8D5A792088C79878
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM260525 Genomic DNA. Translation: CAK00766.1.
    RefSeqiYP_001608761.1. NC_010161.1.

    Genome annotation databases

    GeneIDi5830085.
    KEGGibtr:Btr_0300.
    PATRICi20548332. VBIBarTri113218_0327.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM260525 Genomic DNA. Translation: CAK00766.1 .
    RefSeqi YP_001608761.1. NC_010161.1.

    3D structure databases

    ProteinModelPortali A9IN89.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 382640.Btr_0300.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5830085.
    KEGGi btr:Btr_0300.
    PATRICi 20548332. VBIBarTri113218_0327.

    Phylogenomic databases

    eggNOGi COG1304.
    KOi K00101.
    OMAi DANESML.
    OrthoDBi EOG6HMXBG.

    Enzyme and pathway databases

    BioCyci BTRI382640:GJEK-263-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01559. L_lact_dehydr.
    InterProi IPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    IPR020920. L-lactate_DHase_bac.
    [Graphical view ]
    Pfami PF01070. FMN_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
      Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
      Nat. Genet. 39:1469-1476(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CIP 105476 / IBS 506.

    Entry informationi

    Entry nameiLLDD_BART1
    AccessioniPrimary (citable) accession number: A9IN89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 44 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3