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Reviewed, UniProtKB/Swiss-Prot O93541 (LDHA_CHAGU)

Last modified November 25, 2008. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    L-lactate dehydrogenase A chain
      Short name=LDH-A
    EC=1.1.1.27
Gene names
Name: ldha
OrganismChampsocephalus gunnari (Mackerel icefish)
Taxonomic identifier52237 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Notothenioidei › Channichthyidae › Champsocephalus

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Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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

CytoplasmBy similarity.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

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Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure

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: InterPro

   Molecular functionL-lactate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 331330L-lactate dehydrogenase A chain
PRO_0000168431

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

Secondary structure

1 ......................... 331
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O93541-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 556546DC3A03237E

FASTA33136,156
        10         20         30         40         50         60 
MSTKEKLISH VMKEEPVGSR SKVTVVGVGM VGMASAISIL LKDLCDELAM VDVMEDKLKG 

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

       130        140        150        160        170        180 
PNIVKYSPNC ILMVVSNPVD ILTYVAWKLS GFPRHRVIGS 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 PCVLGNSGLT 

       310        320        330 
DVIHMTLKAE EEKQLQKSAE TLWGVQKELT L

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References

[1]"Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes."
Fields P.A., Somero G.N.
Proc. Natl. Acad. Sci. U.S.A. 95:11476-11481(1998) [PubMed: 9736762] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF079824 mRNA. Translation: AAC63282.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2V65X-ray2.35A/B1-331[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENO93541.

Family and domain databases

InterProIPR001557. L-lactate/malate_DHase.
IPR011304. L-lactate_DHase.
IPR001236. Lactate/malate_DHase.
IPR015955. Lactate_DHase/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd.
[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.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLDHA_CHAGU
AccessionPrimary (citable) accession number: O93541
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 55 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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