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Protein

L-lactate dehydrogenase

Gene

ldh

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of lactate to pyruvate.UniRule annotation1 Publication

Catalytic activityi

(S)-lactate + NAD+ = pyruvate + NADH.UniRule annotation1 Publication

Enzyme regulationi

Allosterically activated by fructose 1,6-bisphosphate (FBP).UniRule annotation

Kineticsi

Kcat is 884 sec(-1) for pyruvate as substrate.1 Publication
  1. KM=0.21 mM for pyruvate1 Publication

    Temperature dependencei

    Optimum temperature is 48 degrees Celsius.1 Publication

    Pathwayi: pyruvate fermentation to lactate

    This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. L-lactate dehydrogenase (ldh)
    This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei11NAD; via amide nitrogenUniRule annotation1
    Binding sitei32NADUniRule annotation1
    Binding sitei37NADUniRule annotation1
    Binding sitei79SubstrateUniRule annotation1
    Binding sitei85SubstrateUniRule annotation1
    Binding sitei138NADUniRule annotation1
    Binding sitei148Allosteric activatorUniRule annotation1
    Binding sitei163Allosteric activatorUniRule annotation1
    Active sitei170Proton acceptorUniRule annotation1
    Binding sitei225SubstrateUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi76 – 77NADUniRule annotation2

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionAllosteric enzyme, Oxidoreductase
    LigandNAD

    Enzyme and pathway databases

    BRENDAi1.1.1.27 1856
    UniPathwayiUPA00554; UER00611

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-lactate dehydrogenase1 PublicationUniRule annotation (EC:1.1.1.27UniRule annotation1 Publication)
    Short name:
    L-LDH1 PublicationUniRule annotation
    Alternative name(s):
    2-ketoacid:NAD-dependent dehydrogenase1 Publication
    Gene namesi
    Name:ldh1 PublicationUniRule annotation
    Ordered Locus Names:DR_2364
    OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
    Taxonomic identifieri243230 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
    Proteomesi
    • UP000002524 Componenti: Chromosome I

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001683411 – 304L-lactate dehydrogenaseAdd BLAST304

    Proteomic databases

    PRIDEiP50933

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi243230.DR_2364

    Structurei

    Secondary structure

    1304
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 6Combined sources5
    Helixi10 – 21Combined sources12
    Beta strandi26 – 31Combined sources6
    Helixi35 – 45Combined sources11
    Beta strandi56 – 60Combined sources5
    Helixi62 – 65Combined sources4
    Beta strandi69 – 73Combined sources5
    Helixi89 – 106Combined sources18
    Beta strandi108 – 114Combined sources7
    Beta strandi116 – 118Combined sources3
    Helixi119 – 129Combined sources11
    Beta strandi135 – 137Combined sources3
    Helixi141 – 155Combined sources15
    Helixi159 – 161Combined sources3
    Beta strandi166 – 171Combined sources6
    Beta strandi174 – 176Combined sources3
    Helixi178 – 180Combined sources3
    Helixi188 – 195Combined sources8
    Helixi201 – 211Combined sources11
    Helixi227 – 241Combined sources15
    Beta strandi246 – 253Combined sources8
    Turni255 – 257Combined sources3
    Beta strandi258 – 268Combined sources11
    Beta strandi271 – 275Combined sources5
    Helixi282 – 296Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2V6BX-ray2.50A/B/C/D1-304[»]
    ProteinModelPortaliP50933
    SMRiP50933
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50933

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni117 – 120Substrate bindingUniRule annotation4
    Regioni143 – 146Substrate bindingUniRule annotation4

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. LDH family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4105C80 Bacteria
    COG0039 LUCA
    HOGENOMiHOG000213793
    InParanoidiP50933
    KOiK00016
    OMAiRQPGQTR
    OrthoDBiPOG091H02EQ

    Family and domain databases

    Gene3Di3.90.110.10, 1 hit
    HAMAPiMF_00488 Lactate_dehydrog, 1 hit
    InterProiView protein in InterPro
    IPR001557 L-lactate/malate_DH
    IPR011304 L-lactate_DH
    IPR018177 L-lactate_DH_AS
    IPR022383 Lactate/malate_DH_C
    IPR001236 Lactate/malate_DH_N
    IPR015955 Lactate_DH/Glyco_Ohase_4_C
    IPR036291 NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF02866 Ldh_1_C, 1 hit
    PF00056 Ldh_1_N, 1 hit
    PIRSFiPIRSF000102 Lac_mal_DH, 1 hit
    PRINTSiPR00086 LLDHDRGNASE
    SUPFAMiSSF51735 SSF51735, 1 hit
    SSF56327 SSF56327, 1 hit
    TIGRFAMsiTIGR01771 L-LDH-NAD, 1 hit
    PROSITEiView protein in PROSITE
    PS00064 L_LDH, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P50933-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKVGVVGTGF VGSTAAFALV LRGSCSELVL VDRDEDRAQA EAEDIAHAAP
    60 70 80 90 100
    VSHGTRVWHG GHSELADAQV VILTAGANQK PGESRLDLLE KNADIFRELV
    110 120 130 140 150
    PQITRAAPDA VLLVTSNPVD LLTDLATQLA PGQPVIGSGT VLDSARFRHL
    160 170 180 190 200
    MAQHAGVDGT HAHGYVLGEH GDSEVLAWSS AMVAGMPVAD FMQAQNLPWN
    210 220 230 240 250
    EQVRAKIDEG TRNAAASIIE GKRATYYGIG AALARITEAV LRDRRAVLTV
    260 270 280 290 300
    SAPTPEYGVS LSLPRVVGRQ GVLSTLHPKL TGDEQQKLEQ SAGVLRGFKQ

    QLGL
    Length:304
    Mass (Da):32,164
    Last modified:May 30, 2000 - v2
    Checksum:iF4CF3298673010CD
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti270Q → R in BAA21471 (Ref. 2) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB005539 Genomic DNA Translation: BAA21471.1
    AE000513 Genomic DNA Translation: AAF11912.1
    PIRiE75282
    RefSeqiNP_296085.1, NC_001263.1
    WP_010888990.1, NZ_CP015081.1

    Genome annotation databases

    EnsemblBacteriaiAAF11912; AAF11912; DR_2364
    GeneIDi1799712
    KEGGidra:DR_2364
    PATRICifig|243230.17.peg.2598

    Similar proteinsi

    Entry informationi

    Entry nameiLDH_DEIRA
    AccessioniPrimary (citable) accession number: P50933
    Secondary accession number(s): O32512
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 30, 2000
    Last modified: May 23, 2018
    This is version 133 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

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