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P19858 (LDHA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

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

General annotation (Comments)

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Post-translational modification

ISGylated By similarity.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionL-lactate dehydrogenase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 332331L-lactate dehydrogenase A chain
PRO_0000168410

Regions

Nucleotide binding29 – 5729NAD By similarity

Sites

Active site1931Proton acceptor By similarity
Binding site1061Substrate By similarity
Binding site1381NAD or substrate By similarity
Binding site1691Substrate By similarity
Binding site2481Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue51N6-acetyllysine By similarity
Modified residue141N6-acetyllysine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue811N6-acetyllysine By similarity
Modified residue1181N6-acetyllysine By similarity
Modified residue1261N6-acetyllysine By similarity
Modified residue2391Phosphotyrosine By similarity
Modified residue2781N6-acetyllysine By similarity
Modified residue3181N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P19858 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DAC59F02BBA7D16C

FASTA33236,598
        10         20         30         40         50         60 
MATLKDQLIQ NLLKEEHVPQ NKITIVGVGA VGMACAISIL MKDLADEVAL VDVMEDKLKG 

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

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

       190        200        210        220        230        240 
HPLSCHGWIL GEHGDSSVPV WSGVNVAGVS LKNLHPELGT DADKEQWKAV HKQVVDSAYE 

       250        260        270        280        290        300 
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI 

       310        320        330 
SDVVKVTLTH EEEACLKKSA DTLWGIQKEL QF 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of bovine lactate dehydrogenase-A isozyme and its synthesis in Escherichia coli."
Ishiguro N., Osame S., Kagiya R., Ichijo S., Shinagawa M.
Gene 91:281-285(1990) [PubMed: 2210387] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90141 mRNA. Translation: BAA14169.1.
D90142 mRNA. Translation: BAA14170.1.
D90143 mRNA. Translation: BAA14171.1.
BC146210 mRNA. Translation: AAI46211.1.
IPIIPI00906445.
PIRJQ2222.
RefSeqNP_776524.1. NM_174099.2.
UniGeneBt.3809.

3D structure databases

ProteinModelPortalP19858.
SMRP19858. Positions 2-332.
ModBaseSearch...

Protein-protein interaction databases

STRINGP19858.

Proteomic databases

PRIDEP19858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000011447; ENSBTAP00000011447; ENSBTAG00000008683.
ENSBTAT00000056276; ENSBTAP00000047729; ENSBTAG00000008683.
GeneID281274.
KEGGbta:281274.

Organism-specific databases

CTD3939.

Phylogenomic databases

eggNOGmaNOG08436.
GeneTreeENSGT00550000074541.
HOVERGENHBG000462.
InParanoidP19858.
OrthoDBEOG4RR6HR.
PhylomeDBP19858.

Family and domain databases

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]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00016.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLDHA_BOVIN
AccessionPrimary (citable) accession number: P19858
Secondary accession number(s): A6H7E0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families