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)

Q53560

- DHLE_BACLI

UniProt

Q53560 - DHLE_BACLI

Protein

Leucine dehydrogenase

Gene

ldh

Organism
Bacillus licheniformis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the reversible deamination of L-leucine to 4-methyl-2-oxopentanoate. Can also use other substrates such as L-isoleucine, L-valine and L-2-aminobutyrate. The 2-oxo analogs of branched-chain and straight-chain amino acids serve as good substrates for the reverse reaction.1 Publication

    Catalytic activityi

    L-leucine + H2O + NAD+ = 4-methyl-2-oxopentanoate + NH3 + NADH.1 Publication

    Kineticsi

    1. KM=2.1 mM for L-leucine1 Publication
    2. KM=3.3 mM for L-isoleucine1 Publication
    3. KM=12.5 mM for L-valine1 Publication
    4. KM=0.31 mM for NAD+1 Publication
    5. KM=1.0 mM for 4-methyl-2-oxopentanoate1 Publication
    6. KM=3.8 mM for 2-oxoisovalerate1 Publication
    7. KM=2.4 mM for 2-oxovalerate1 Publication
    8. KM=0.25 mM for NADH1 Publication
    9. KM=330 mM for NH31 Publication

    pH dependencei

    Optimum pH is 10.3 for the oxidative deamination of L-leucine.1 Publication

    Temperature dependencei

    Thermostable. Retains full activity on heating at 65 degrees Celsius for 1 hour, but loses the activity completely on heating at 70 degrees Celsius for 1 hour.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei80 – 801PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi180 – 1867NADSequence Analysis

    GO - Molecular functioni

    1. leucine dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. leucine catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Branched-chain amino acid catabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00363; UER00858.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucine dehydrogenase (EC:1.4.1.9)
    Short name:
    LeuDH
    Gene namesi
    Name:ldh
    OrganismiBacillus licheniformis
    Taxonomic identifieri1402 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 364364Leucine dehydrogenasePRO_0000182802Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ53560.
    SMRiQ53560. Positions 1-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006095. Glu/Leu/Phe/Val_DH.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
    PfamiPF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000188. Phe_leu_dh. 1 hit.
    PRINTSiPR00082. GLFDHDRGNASE.
    SMARTiSM00839. ELFV_dehydrog. 1 hit.
    [Graphical view]
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q53560-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELFRYMEQY DYEQLVFCQD KQSGLKAIIA IHDTTLGPAL GGTRMWTYES    50
    EEAAIEDALR LARGMTYKNA AAGLNLGGGK TVIIGDPRKD KNEEMFRAFG 100
    RYIQGLNGRY ITAEDVGTTV EDMDIIHDET DFVTGISPAF GSSGNPSPVT 150
    AYGVYKGMKA AAKAAFGTDS LEGKTVAVQG VGNVAYNLCR HLHEEGAKLI 200
    VTDINKEAVE RAVAEFGARA VDPDDIYSQE CDIYAPCALG ATINDDTIPQ 250
    LKAKVIAGAA NNQLKETRHG DQIHDMGIVY APDYVINAGG VINVADELYG 300
    YNSERALKKV EGIYGNIERV LEISKRDRIP TYLAADRLAE ERIERMRQSR 350
    SQFLQNGHHI LSRR 364
    Length:364
    Mass (Da):40,040
    Last modified:November 1, 1996 - v1
    Checksum:iA13A967F6E84F873
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81735 Genomic DNA. Translation: AAB36205.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81735 Genomic DNA. Translation: AAB36205.1 .

    3D structure databases

    ProteinModelPortali Q53560.
    SMRi Q53560. Positions 1-364.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00363 ; UER00858 .

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR006095. Glu/Leu/Phe/Val_DH.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11606:SF3. PTHR11606:SF3. 1 hit.
    Pfami PF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000188. Phe_leu_dh. 1 hit.
    PRINTSi PR00082. GLFDHDRGNASE.
    SMARTi SM00839. ELFV_dehydrog. 1 hit.
    [Graphical view ]
    PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene cloning, purification, and characterization of thermostable and halophilic leucine dehydrogenase from a halophilic thermophile, Bacillus licheniformis TSN9."
      Nagata S., Bakthavatsalam S., Galkin A.G., Asada H., Sakai S., Esaki N., Soda K., Ohshima T., Nagasaki S., Misono H.
      Appl. Microbiol. Biotechnol. 44:432-438(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT.
      Strain: TSN9.

    Entry informationi

    Entry nameiDHLE_BACLI
    AccessioniPrimary (citable) accession number: Q53560
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3