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Reviewed, UniProtKB/Swiss-Prot Q9W7M6 (LDHA_AMBME)

Last modified June 16, 2009. Version 50. 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
OrganismAmbystoma mexicanum (Axolotl)
Taxonomic identifier8296 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaCaudataSalamandroideaAmbystomatidaeAmbystoma

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Chain1 – 333333L-lactate dehydrogenase A chain
PRO_0000168456

Regions

Nucleotide binding30 – 5829NAD By similarity

Sites

Active site1941Proton acceptor By similarity
Binding site1001NAD By similarity
Binding site1071Substrate By similarity
Binding site1391NAD or substrate By similarity
Binding site1701Substrate By similarity
Binding site2491Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9W7M6-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: EF97E41E545492C7

FASTA33336,631
        10         20         30         40         50         60 
MSCMKEQLII NILKDEHAPA QNKITVVGVG AVGMACAMSI LMKDLADELA LVDVIEDKLK 

        70         80         90        100        110        120 
GEMMDLQHGS LFLRTPKIVS GKDYSVTANS KLVIVTAGAR QQEGESRLNL VQRNVNIFKF 

       130        140        150        160        170        180 
IIPNVVKYSP DATLLVVSNP VDVLTYVAWK ISGFPKHRVI GSGCNLDSAR FRYLMGEKLG 

       190        200        210        220        230        240 
VHAQSCHGWV VGEHGDSSVP VWSGVNVAGV SLQTLNPELG TDADKENWKE VHKQVVESAY 

       250        260        270        280        290        300 
EVIKLKGYTS WAIGLSVADL AETIMKNLRR VHPVSTKVKG LYGVHEDVFL SVPCVLGNQG 

       310        320        330 
ITDVVKMTLK PEEEDRLRKS SDTLWGIQKE LHF 

« Hide

References

[1]"Molecular evolution of vertebrate lactate dehydrogenase isozymes by gene duplication."
Tsoi S.C.-M., Li J.Y., Mannen H., Li S.S.-L.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AF070998 mRNA. Translation: AAD40735.1.

3D structure databases

HSSPHSSP built from PDB template 1I10 based on UniProtKB P00338.
SMRQ9W7M6. Positions 2-333.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9W7M6.

Enzyme and pathway databases

BRENDA1.1.1.27. 1113.

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_AMBME
AccessionPrimary (citable) accession number: Q9W7M6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: November 1, 1999
Last modified: June 16, 2009
This is version 50 of the entry and version 1 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