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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)DescriptionActionsGraphical viewLength
Binding sitei99NADBy similarity1
Binding sitei106SubstrateBy similarity1
Binding sitei138NAD or substrateBy similarity1
Binding sitei169SubstrateBy similarity1
Active sitei193Proton acceptorBy similarity1
Binding sitei248SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 57NADBy similarityAdd BLAST29

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 animal 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
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 databases

ChEMBLiCHEMBL2176824.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001684192 – 332L-lactate dehydrogenase A chainAdd BLAST331

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei5N6-acetyllysine; alternateBy similarity1
Modified residuei5N6-succinyllysine; alternateBy similarity1
Modified residuei14N6-acetyllysineBy similarity1
Modified residuei57N6-acetyllysineBy similarity1
Modified residuei81N6-acetyllysineBy similarity1
Modified residuei118N6-acetyllysine; alternateBy similarity1
Modified residuei118N6-succinyllysine; alternateBy similarity1
Modified residuei126N6-acetyllysineBy similarity1
Modified residuei213PhosphoserineCombined sources1
Modified residuei224N6-acetyllysineBy similarity1
Modified residuei232N6-acetyllysineBy similarity1
Modified residuei239PhosphotyrosineCombined sources1
Modified residuei243N6-acetyllysineBy similarity1
Modified residuei309PhosphothreonineCombined sources1
Modified residuei318N6-acetyllysine; alternateBy similarity1
Modified residuei318N6-succinyllysine; alternateBy similarity1
Modified residuei322PhosphothreonineCombined sources1

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP04642.
PRIDEiP04642.

PTM databases

iPTMnetiP04642.
PhosphoSitePlusiP04642.

Expressioni

Gene expression databases

BgeeiENSRNOG00000013009.
ExpressionAtlasiP04642. differential.
GenevisibleiP04642. RN.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

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

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP04642.

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 8Combined sources5
Beta strandi9 – 11Combined sources3
Beta strandi20 – 26Combined sources7
Helixi30 – 41Combined sources12
Beta strandi46 – 51Combined sources6
Helixi55 – 67Combined sources13
Helixi68 – 71Combined sources4
Beta strandi76 – 79Combined sources4
Helixi83 – 86Combined sources4
Beta strandi89 – 94Combined sources6
Helixi106 – 109Combined sources4
Helixi110 – 127Combined sources18
Beta strandi132 – 135Combined sources4
Beta strandi137 – 139Combined sources3
Helixi140 – 151Combined sources12
Helixi155 – 157Combined sources3
Beta strandi158 – 160Combined sources3
Helixi164 – 178Combined sources15
Helixi182 – 184Combined sources3
Beta strandi189 – 191Combined sources3
Helixi201 – 203Combined sources3
Helixi211 – 214Combined sources4
Turni216 – 219Combined sources4
Helixi228 – 245Combined sources18
Helixi250 – 264Combined sources15
Beta strandi269 – 276Combined sources8
Helixi280 – 282Combined sources3
Beta strandi288 – 296Combined sources9
Beta strandi299 – 304Combined sources6
Helixi310 – 327Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OMAiNNEHRVL.
OrthoDBiEOG091G0HME.
PhylomeDBiP04642.
TreeFamiTF314963.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti184 – 191SCHGWVLG → ADLGEVV AA sequence (PubMed:2991914).Curated8
Sequence conflicti324W → G in AAA41508 (Ref. 5) Curated1
Sequence conflicti326I → T in AAA41508 (Ref. 5) Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP04642.
ChEMBLiCHEMBL2176824.

PTM databases

iPTMnetiP04642.
PhosphoSitePlusiP04642.

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.
OMAiNNEHRVL.
OrthoDBiEOG091G0HME.
PhylomeDBiP04642.
TreeFamiTF314963.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP04642.

Gene expression databases

BgeeiENSRNOG00000013009.
ExpressionAtlasiP04642. differential.
GenevisibleiP04642. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog. 1 hit.
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...

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: November 30, 2016
This is version 158 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.