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Protein

L-lactate dehydrogenase A chain

Gene

LDHA

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991NAD
Binding sitei106 – 1061Substrate
Binding sitei138 – 1381NAD or substrate
Binding sitei169 – 1691Substrate
Active sitei193 – 1931Proton acceptor1 Publication
Binding sitei248 – 2481Substrate

Regions

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

GO - Molecular functioni

  1. L-lactate dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP13491.
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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 332331L-lactate dehydrogenase A chainPRO_0000168418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
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 residuei224 – 2241N6-acetyllysineBy similarity
Modified residuei232 – 2321N6-acetyllysineBy similarity
Modified residuei239 – 2391PhosphotyrosineBy similarity
Modified residuei243 – 2431N6-acetyllysineBy similarity
Modified residuei310 – 3101PhosphoserineBy similarity
Modified residuei318 – 3181N6-acetyllysine; alternateBy similarity
Modified residuei318 – 3181N6-succinyllysine; alternateBy similarity

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP13491.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP13491. 1 interaction.
STRINGi9986.ENSOCUP00000021667.

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 – 6612Combined sources
Helixi67 – 715Combined sources
Beta strandi76 – 794Combined sources
Helixi83 – 864Combined sources
Beta strandi90 – 945Combined sources
Helixi109 – 12719Combined 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 – 1946Combined sources
Helixi201 – 2033Combined sources
Helixi211 – 2144Combined sources
Turni216 – 2194Combined sources
Helixi228 – 24518Combined sources
Helixi250 – 26415Combined sources
Beta strandi269 – 2768Combined 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
3H3FX-ray2.38A/B/C/D/E/F/G/H2-332[»]
4I8XX-ray2.23A/B/C/D/E/F/G/H2-332[»]
4I9HX-ray2.17A/B/C/D/E/F/G/H2-332[»]
4I9NX-ray2.35A/B/C/D/E/F/G/H2-332[»]
4I9UX-ray2.50A/B/C/D/E/F/G/H2-332[»]
ProteinModelPortaliP13491.
SMRiP13491. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13491.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP13491.
KOiK00016.

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.
SUPFAMiSSF56327. 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.

P13491-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALKDQLIH NLLKEEHVPQ NKITVVGVGA VGMACAISIL MKDLADELAL
60 70 80 90 100
VDVMEDKLKG EMMDLQHGSL FLRTPKIVSG KDYSVTANSK LVIITAGARQ
110 120 130 140 150
QEGESRLNLV QRNVNIFKFI IPNVVKYSPH CKLLVVSNPV DILTYVAWKI
160 170 180 190 200
SGFPKNRVIG SGCNLDSARF RYLMGERLGV HALSCHGWIL GEHGDSSVPV
210 220 230 240 250
WSGMNVAGVS LKTLHPELGT DADKEQWKQV HKQVVDSAYE VIKLKGYTTW
260 270 280 290 300
AIGLSVADLA ESIMKNLRRV HPISTMLKGL YGIKEDVFLS VPCVLGQNGI
310 320 330
SDVVKVTLTS EEEAHLKKSA DTLWGIQKEL QF
Length:332
Mass (Da):36,565
Last modified:January 23, 2007 - v3
Checksum:i84E86C2E7D018EF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22585 mRNA. Translation: AAA31382.1.
PIRiA32957.
RefSeqiNP_001075746.1. NM_001082277.1.
UniGeneiOcu.1108.

Genome annotation databases

GeneIDi100009107.
KEGGiocu:100009107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22585 mRNA. Translation: AAA31382.1.
PIRiA32957.
RefSeqiNP_001075746.1. NM_001082277.1.
UniGeneiOcu.1108.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H3FX-ray2.38A/B/C/D/E/F/G/H2-332[»]
4I8XX-ray2.23A/B/C/D/E/F/G/H2-332[»]
4I9HX-ray2.17A/B/C/D/E/F/G/H2-332[»]
4I9NX-ray2.35A/B/C/D/E/F/G/H2-332[»]
4I9UX-ray2.50A/B/C/D/E/F/G/H2-332[»]
ProteinModelPortaliP13491.
SMRiP13491. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP13491. 1 interaction.
STRINGi9986.ENSOCUP00000021667.

Proteomic databases

PRIDEiP13491.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009107.
KEGGiocu:100009107.

Organism-specific databases

CTDi3939.

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP13491.
KOiK00016.

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
SABIO-RKP13491.

Miscellaneous databases

EvolutionaryTraceiP13491.

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.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of rabbit lactate dehydrogenase-M and lactate dehydrogenase-H cDNAs. Control of lactate dehydrogenase expression in rabbit muscle."
    Sass C., Briand M., Benslimane S., Renaud M., Briand Y.
    J. Biol. Chem. 264:4076-4081(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Modeling of isotope effects on binding oxamate to lactic dehydrogenase."
    Swiderek K., Panczakiewicz A., Bujacz A., Bujacz G., Paneth P.
    J. Phys. Chem. B 113:12782-12789(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-332 IN COMPLEX WITH NADH AMD INHIBITOR, SUBUNIT, ACTIVE SITE, SUBSTRATE-BINDING SITES, NAD-BINDING SITES.

Entry informationi

Entry nameiLDHA_RABIT
AccessioniPrimary (citable) accession number: P13491
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

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 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.