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Protein

L-lactate dehydrogenase A chain

Gene

Ldha

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-lactate + NAD+ = pyruvate + NADH.

Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. L-lactate dehydrogenase A chain (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhal6b), L-lactate dehydrogenase B chain (Ldhb), L-lactate dehydrogenase C chain (Ldhc), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhc)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991NADBy similarity
Binding sitei106 – 1061SubstrateBy similarity
Binding sitei138 – 1381NAD or substrateBy similarity
Binding sitei169 – 1691SubstrateBy similarity
Active sitei193 – 1931Proton acceptorBy similarity
Binding sitei248 – 2481SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 5729NADBy similarityAdd
BLAST

GO - Molecular functioni

  • identical protein binding Source: RGD
  • kinase binding Source: RGD
  • lactate dehydrogenase activity Source: RGD
  • L-lactate dehydrogenase activity Source: RGD
  • NAD binding Source: RGD

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • lactate metabolic process Source: RGD
  • NAD metabolic process Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • post-embryonic organ development Source: RGD
  • response to cAMP Source: RGD
  • response to drug Source: RGD
  • response to estrogen Source: RGD
  • response to glucose Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to hypoxia Source: RGD
  • response to nutrient Source: RGD
  • response to organic cyclic compound Source: RGD
  • substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11604.
ReactomeiR-RNO-70268. Pyruvate metabolism.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase A chain (EC:1.1.1.27)
Short name:
LDH-A
Alternative name(s):
LDH muscle subunit
Short name:
LDH-M
Gene namesi
Name:Ldha
Synonyms:Ldh-1, Ldh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2996. Ldha.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2176824.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 332331L-lactate dehydrogenase A chainPRO_0000168419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei5 – 51N6-acetyllysine; alternateBy similarity
Modified residuei5 – 51N6-succinyllysine; alternateBy similarity
Modified residuei14 – 141N6-acetyllysineBy similarity
Modified residuei57 – 571N6-acetyllysineBy similarity
Modified residuei81 – 811N6-acetyllysineBy similarity
Modified residuei118 – 1181N6-acetyllysine; alternateBy similarity
Modified residuei118 – 1181N6-succinyllysine; alternateBy similarity
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei213 – 2131PhosphoserineCombined sources
Modified residuei224 – 2241N6-acetyllysineBy similarity
Modified residuei232 – 2321N6-acetyllysineBy similarity
Modified residuei239 – 2391PhosphotyrosineCombined sources
Modified residuei243 – 2431N6-acetyllysineBy similarity
Modified residuei309 – 3091PhosphothreonineCombined sources
Modified residuei318 – 3181N6-acetyllysine; alternateBy similarity
Modified residuei318 – 3181N6-succinyllysine; alternateBy similarity
Modified residuei322 – 3221PhosphothreonineCombined sources

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP04642.
PRIDEiP04642.

PTM databases

iPTMnetiP04642.
PhosphoSiteiP04642.

Expressioni

Gene expression databases

ExpressionAtlasiP04642. baseline.
GenevisibleiP04642. RN.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • identical protein binding Source: RGD
  • kinase binding Source: RGD

Protein-protein interaction databases

BioGridi246686. 3 interactions.
IntActiP04642. 5 interactions.
MINTiMINT-4568905.
STRINGi10116.ENSRNOP00000017468.

Chemistry

BindingDBiP04642.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85Combined sources
Beta strandi9 – 113Combined sources
Beta strandi20 – 267Combined sources
Helixi30 – 4112Combined sources
Beta strandi46 – 516Combined sources
Helixi55 – 6713Combined sources
Helixi68 – 714Combined sources
Beta strandi76 – 794Combined sources
Helixi83 – 864Combined sources
Beta strandi89 – 946Combined sources
Helixi106 – 1094Combined sources
Helixi110 – 12718Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi137 – 1393Combined sources
Helixi140 – 15112Combined sources
Helixi155 – 1573Combined sources
Beta strandi158 – 1603Combined sources
Helixi164 – 17815Combined sources
Helixi182 – 1843Combined sources
Beta strandi189 – 1913Combined sources
Helixi201 – 2033Combined sources
Helixi211 – 2144Combined sources
Turni216 – 2194Combined sources
Helixi228 – 24518Combined sources
Helixi250 – 26415Combined sources
Beta strandi269 – 2768Combined sources
Helixi280 – 2823Combined sources
Beta strandi288 – 2969Combined sources
Beta strandi299 – 3046Combined sources
Helixi310 – 32718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AJ1X-ray1.87A/B/C/D2-332[»]
4AJ2X-ray1.75A/B/C/D2-332[»]
4AJ4X-ray1.90A/B/C/D1-332[»]
4AJEX-ray2.35A/B/C/D2-332[»]
4AJHX-ray1.93A/B/C/D2-332[»]
4AJIX-ray1.93A/B/C/D2-332[»]
4AJJX-ray1.75A/B/C/D2-332[»]
4AJKX-ray2.03A/B/C/D2-332[»]
4AJLX-ray1.77A/B/C/D2-332[»]
4AJNX-ray2.10A/B/C/D2-332[»]
4AJOX-ray1.96A/B/C/D2-332[»]
4AL4X-ray1.78A/B/C/D2-332[»]
5ES3X-ray2.29A/B/C/D/E/F/G/H2-332[»]
ProteinModelPortaliP04642.
SMRiP04642. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. LDH family.Curated

Phylogenomic databases

eggNOGiKOG1495. Eukaryota.
COG0039. LUCA.
GeneTreeiENSGT00550000074541.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP04642.
KOiK00016.
OMAiAGDYEDC.
OrthoDBiEOG7X0VH3.
PhylomeDBiP04642.
TreeFamiTF314963.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. 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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04642-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALKDQLIV NLLKEEQVPQ NKITVVGVGA VGMACAISIL MKDLADELAL
60 70 80 90 100
VDVIEDKLKG EMMDLQHGSL FLKTPKIVSS KDYSVTANSK LVIITAGARQ
110 120 130 140 150
QEGESRLNLV QRNVNIFKFI IPNVVKYSPQ CKLLIVSNPV DILTYVAWKI
160 170 180 190 200
SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV
210 220 230 240 250
WSGVNVAGVS LKSLNPQLGT DADKEQWKDV HKQVVDSAYE VIKLKGYTSW
260 270 280 290 300
AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI
310 320 330
SDVVKVTLTP DEEARLKKSA DTLWGIQKEL QF
Length:332
Mass (Da):36,451
Last modified:August 13, 1987 - v1
Checksum:i5E432659D032A4D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1918SCHGWVLG → ADLGEVV AA sequence (PubMed:2991914).Curated
Sequence conflicti324 – 3241W → G in AAA41508 (Ref. 5) Curated
Sequence conflicti326 – 3261I → T in AAA41508 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01964 mRNA. Translation: CAA26000.1.
BC084698 mRNA. Translation: AAH84698.1.
M54926 mRNA. Translation: AAA41508.1.
PIRiA23083.
RefSeqiNP_058721.1. NM_017025.1.
UniGeneiRn.107896.

Genome annotation databases

EnsembliENSRNOT00000017468; ENSRNOP00000017468; ENSRNOG00000013009.
GeneIDi24533.
KEGGirno:24533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01964 mRNA. Translation: CAA26000.1.
BC084698 mRNA. Translation: AAH84698.1.
M54926 mRNA. Translation: AAA41508.1.
PIRiA23083.
RefSeqiNP_058721.1. NM_017025.1.
UniGeneiRn.107896.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AJ1X-ray1.87A/B/C/D2-332[»]
4AJ2X-ray1.75A/B/C/D2-332[»]
4AJ4X-ray1.90A/B/C/D1-332[»]
4AJEX-ray2.35A/B/C/D2-332[»]
4AJHX-ray1.93A/B/C/D2-332[»]
4AJIX-ray1.93A/B/C/D2-332[»]
4AJJX-ray1.75A/B/C/D2-332[»]
4AJKX-ray2.03A/B/C/D2-332[»]
4AJLX-ray1.77A/B/C/D2-332[»]
4AJNX-ray2.10A/B/C/D2-332[»]
4AJOX-ray1.96A/B/C/D2-332[»]
4AL4X-ray1.78A/B/C/D2-332[»]
5ES3X-ray2.29A/B/C/D/E/F/G/H2-332[»]
ProteinModelPortaliP04642.
SMRiP04642. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246686. 3 interactions.
IntActiP04642. 5 interactions.
MINTiMINT-4568905.
STRINGi10116.ENSRNOP00000017468.

Chemistry

BindingDBiP04642.
ChEMBLiCHEMBL2176824.

PTM databases

iPTMnetiP04642.
PhosphoSiteiP04642.

Proteomic databases

PaxDbiP04642.
PRIDEiP04642.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017468; ENSRNOP00000017468; ENSRNOG00000013009.
GeneIDi24533.
KEGGirno:24533.

Organism-specific databases

CTDi3939.
RGDi2996. Ldha.

Phylogenomic databases

eggNOGiKOG1495. Eukaryota.
COG0039. LUCA.
GeneTreeiENSGT00550000074541.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP04642.
KOiK00016.
OMAiAGDYEDC.
OrthoDBiEOG7X0VH3.
PhylomeDBiP04642.
TreeFamiTF314963.

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
BioCyciMetaCyc:MONOMER-11604.
ReactomeiR-RNO-70268. Pyruvate metabolism.

Miscellaneous databases

NextBioi603598.
PROiP04642.

Gene expression databases

ExpressionAtlasiP04642. baseline.
GenevisibleiP04642. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. 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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Epidermal growth factor or serum stimulation of rat fibroblasts induces an elevation in mRNA levels for lactate dehydrogenase and other glycolytic enzymes."
    Matrisian L.M., Rautmann G., Magun B.E., Breathnach R.
    Nucleic Acids Res. 13:711-726(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. Bienvenut W.V., von Kriegsheim A.F., Kolch W.
    Submitted (JUN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14; 43-57; 91-99; 107-112; 119-126; 233-243; 306-315 AND 319-328, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fibroblast and Pheochromocytoma.
  4. "Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5."
    Williams K.R., Reddigari S., Patel G.L.
    Proc. Natl. Acad. Sci. U.S.A. 82:5260-5264(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 82-99; 127-132; 156-157; 170-190; 234-245; 306-315 AND 319-328.
  5. "Characterization of the folding structure of 3'-end of lactate dehydrogenase A-mRNA isolated from hormone stimulated rat C-6 glioma cell culture."
    Bae S.C., Lee S.K.
    J. Microbiol. 25:94-102(1987)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 274-332.
    Tissue: Liver.
  6. Lubec G., Chen W.-Q.
    Submitted (SEP-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 319-328, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; TYR-239; THR-309 AND THR-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLDHA_RAT
AccessioniPrimary (citable) accession number: P04642
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 11, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.