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Reviewed, UniProtKB/Swiss-Prot Q9PW61 (LDHA_DISEL)

Last modified February 9, 2010. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-lactate dehydrogenase A chain
      Short name=LDH-A
    EC=1.1.1.27
Gene names
Name: ldha
OrganismDissostichus eleginoides (Patagonian toothfish)
Taxonomic identifier100907 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaAcanthopterygiiPercomorphaPerciformesNotothenioideiNototheniidaeDissostichus

Protein attributes

Sequence length331 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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processanaerobic glycolysis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

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: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 331330L-lactate dehydrogenase A chain
PRO_0000168435

Regions

Nucleotide binding29 – 5729NAD By similarity

Sites

Active site1921Proton acceptor By similarity
Binding site981NAD By similarity
Binding site1051Substrate By similarity
Binding site1371NAD or substrate By similarity
Binding site1681Substrate By similarity
Binding site2471Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PW61-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3AA5EDF03766FE65

FASTA33136,144
        10         20         30         40         50         60 
MSTKEKLISH VMKEEPVGSR NKVTVVGVGM VGMASAISIL LKDLCDELAM VDVMEDKLKG 

        70         80         90        100        110        120 
EVMDLQHGSL FLKTKIVGDK DYSVTANSKV VVVTAGARQQ EGESRLNLVQ RNVNIFKFII 

       130        140        150        160        170        180 
PNIVKYSPNC ILMVVSNPVD ILTYVAWKLS GFPRNRVIGS GTNLDSARFR HLIGEKLHLH 

       190        200        210        220        230        240 
PSSCHAWIVG EHGDSSVPVW SGVNVAGVSL QGLNPQMGTE GDGENWKAIH KEVVDGAYEV 

       250        260        270        280        290        300 
IKLKGYTSWA IGMSVADLVE SIIKNMHKVH PVSTLVQGMH GVKDEVFLSV PSVLGNSGLT 

       310        320        330 
DVIHMTLKAE EEKQLQKSAE TLWGVQKELT L 

« Hide

References

[1]"Cold adaptation in lactate dehydrogenases from Antarctic fish."
Marshall C.J., McInnes S.J., Love C.A.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF170027 mRNA. Translation: AAD48482.1.

3D structure databases

SMRQ9PW61. Positions 2-331.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9PW61.

Enzyme and pathway databases

BRENDA1.1.1.27. 298174.

Family and domain databases

InterProIPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR001236. Lactate/malate_DH.
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.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLDHA_DISEL
AccessionPrimary (citable) accession number: Q9PW61
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 58 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents