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P13491 (LDHA_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase A chain

Short name=LDH-A
EC=1.1.1.27
Alternative name(s):
LDH muscle subunit
Short name=LDH-M
Gene names
Name:LDHA
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-lactate + NAD+ = pyruvate + NADH. HAMAP-Rule MF_00488

Pathway

Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP-Rule MF_00488

Subunit structure

Homotetramer. Ref.2

Subcellular location

Cytoplasm HAMAP-Rule MF_00488.

Post-translational modification

ISGylated By similarity. HAMAP-Rule MF_00488

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-lactate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 332331L-lactate dehydrogenase A chain HAMAP-Rule MF_00488
PRO_0000168418

Regions

Nucleotide binding29 – 5729NAD HAMAP-Rule MF_00488

Sites

Active site1931Proton acceptor Ref.2
Binding site991NAD
Binding site1061Substrate
Binding site1381NAD or substrate
Binding site1691Substrate
Binding site2481Substrate

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue51N6-acetyllysine; alternate By similarity
Modified residue51N6-succinyllysine; alternate By similarity
Modified residue141N6-acetyllysine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue811N6-acetyllysine By similarity
Modified residue1181N6-acetyllysine; alternate By similarity
Modified residue1181N6-succinyllysine; alternate By similarity
Modified residue1261N6-acetyllysine By similarity
Modified residue2241N6-acetyllysine By similarity
Modified residue2321N6-acetyllysine By similarity
Modified residue2391Phosphotyrosine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue3181N6-acetyllysine; alternate By similarity
Modified residue3181N6-succinyllysine; alternate By similarity

Secondary structure

..................................................... 332
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13491 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 84E86C2E7D018EF7

FASTA33236,565
        10         20         30         40         50         60 
MAALKDQLIH NLLKEEHVPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVMEDKLKG 

        70         80         90        100        110        120 
EMMDLQHGSL FLRTPKIVSG KDYSVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI 

       130        140        150        160        170        180 
IPNVVKYSPH CKLLVVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV 

       190        200        210        220        230        240 
HALSCHGWIL GEHGDSSVPV WSGMNVAGVS LKTLHPELGT DADKEQWKQV HKQVVDSAYE 

       250        260        270        280        290        300 
VIKLKGYTTW AIGLSVADLA ESIMKNLRRV HPISTMLKGL YGIKEDVFLS VPCVLGQNGI 

       310        320        330 
SDVVKVTLTS EEEAHLKKSA DTLWGIQKEL QF 

« Hide

References

[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(1989) [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(2009) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22585 mRNA. Translation: AAA31382.1.
PIRA32957.
RefSeqNP_001075746.1. NM_001082277.1.
UniGeneOcu.1108.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP13491.
SMRP13491. Positions 2-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP13491. 1 interaction.
STRING9986.ENSOCUP00000021667.

Proteomic databases

PRIDEP13491.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009107.

Organism-specific databases

CTD3939.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213793.
HOVERGENHBG000462.

Enzyme and pathway databases

SABIO-RKP13491.
UniPathwayUPA00554; UER00611.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00488. Lactate_dehydrog.
InterProIPR001557. 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]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13491.

Entry information

Entry nameLDHA_RABIT
AccessionPrimary (citable) accession number: P13491
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways