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B5EXA8

- LLDD_SALA4

UniProt

B5EXA8 - LLDD_SALA4

Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Salmonella agona (strain SL483)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (14 Oct 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

    BioCyciSENT454166:GHBA-3882-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-lactate dehydrogenaseUniRule annotation (EC:1.1.-.-UniRule annotation)
    Gene namesi
    Name:lldDUniRule annotation
    Ordered Locus Names:SeAg_B3911
    OrganismiSalmonella agona (strain SL483)
    Taxonomic identifieri454166 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000008819: 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 – 396396L-lactate dehydrogenasePRO_0000383437Add
    BLAST

    Proteomic databases

    PRIDEiB5EXA8.

    Interactioni

    Protein-protein interaction databases

    STRINGi454166.SeAg_B3911.

    Structurei

    3D structure databases

    ProteinModelPortaliB5EXA8.
    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.
    HOGENOMiHOG000217464.
    OMAiDCTLLGR.
    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.

    B5EXA8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIISAASDYR AAAQRTLPPF LFHYIDGGAY AEYTLRRNVE DLSQVALRQR    50
    VLKNMSDLSL ETTLFNETLS MPVALAPVGL CGMYARRGEV QAAAAADAKG 100
    IPFTLSTVSV CPIEEVAPTI KRPMWFQLYV LRDRGFMRNA LERAKAAGCS 150
    TLVFTVDMPT PGARYRDAHS GMSGPNAAMR RYWQAVMHPK WAWDVGLNGR 200
    PHDLGNISAY LGKPTGLEDY IGWLANNFDP SISWKDLEWI REFWDGPMVI 250
    KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD 300
    IAILADSGIR NGLDVVRMIA LGADTVLLGR AYLYALATAG KAGVANLLDL 350
    IEKEMKVAMT LTGAKSISEI SGDSLVQELG KSLPAALAPM SKGDAA 396
    Length:396
    Mass (Da):42,714
    Last modified:October 14, 2008 - v1
    Checksum:i93DD695CCB854963
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001138 Genomic DNA. Translation: ACH52956.1.
    RefSeqiYP_002148626.1. NC_011149.1.

    Genome annotation databases

    EnsemblBacteriaiACH52956; ACH52956; SeAg_B3911.
    PATRICi18486054. VBISalEnt65316_3802.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001138 Genomic DNA. Translation: ACH52956.1 .
    RefSeqi YP_002148626.1. NC_011149.1.

    3D structure databases

    ProteinModelPortali B5EXA8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 454166.SeAg_B3911.

    Proteomic databases

    PRIDEi B5EXA8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACH52956 ; ACH52956 ; SeAg_B3911 .
    PATRICi 18486054. VBISalEnt65316_3802.

    Phylogenomic databases

    eggNOGi COG1304.
    HOGENOMi HOG000217464.
    OMAi DCTLLGR.
    OrthoDBi EOG6HMXBG.

    Enzyme and pathway databases

    BioCyci SENT454166:GHBA-3882-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. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
      Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
      J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SL483.

    Entry informationi

    Entry nameiLLDD_SALA4
    AccessioniPrimary (citable) accession number: B5EXA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 37 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