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P00341 (LDHA_SQUAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase A chain
Short name=LDH-A
EC=1.1.1.27
Alternative name(s):
LDH-M
Gene names
Name:ldha
OrganismSqualus acanthias (Spiny dogfish)
Taxonomic identifier7797 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalimorphii › Squaliformes › Squalidae › Squalus

Protein attributes

Sequence length333 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.

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 333332L-lactate dehydrogenase A chain
PRO_0000168455

Regions

Nucleotide binding30 – 5829NAD

Sites

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

Amino acid modifications

Modified residue21N-acetylalanine

Experimental info

Sequence conflict1241D → N AA sequence Ref.2
Sequence conflict1841S → C AA sequence Ref.2
Sequence conflict198 – 2003SVP → VPS AA sequence Ref.2
Sequence conflict206 – 2116NVAGVS → WNA AA sequence Ref.2
Sequence conflict2221D → N AA sequence Ref.2
Sequence conflict226 – 2272EN → QD AA sequence Ref.2
Sequence conflict286 – 2872ND → DN AA sequence Ref.2
Sequence conflict297 – 2982DN → ND AA sequence Ref.2

Secondary structure

1 ........................................................ 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00341 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 20C3B5F84B6C0117

FASTA33336,695
        10         20         30         40         50         60 
MATLKDKLIG HLATSQEPRS YNKITVVGVG AVGMACAISI LMKDLADEVA LVDVMEDKLK 

        70         80         90        100        110        120 
GEMMDLQHGS LFLHTAKIVS GKDYSVSAGS KLVVITAGAR QQEGESRLNL VQRNVNIFKF 

       130        140        150        160        170        180 
IIPDIVKHSP DCIILVVSNP VDVLTYVAWK LSGLPMHRII GSGCNLDSAR FRYLMGERLG 

       190        200        210        220        230        240 
VHSSSCHGWV IGEHGDSSVP VWSGMNVAGV SLKELHPELG TDKDKENWKK LHKDVVDSAY 

       250        260        270        280        290        300 
EVIKLKGYTS WAIGLSVADL AETIMKNLCR VHPVSTMVKD FYGIKNDVFL SLPCVLDNHG 

       310        320        330 
ISNIVKMKLK PDEEQQLQKS ATTLWDIQKD LKF

« Hide

References

[1]"The cDNA sequence of the lactate dehydrogenase-A of the spiny dogfish (Squalus acanthias): corrections to the amino acid sequence and an analysis of the phylogeny of vertebrate lactate dehydrogenases."
Stock D.W., Powers D.A.
Mol. Mar. Biol. Biotechnol. 4:284-294(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"Amino acid sequence of dogfish muscle lactate dehydrogenase."
Taylor S.S.
J. Biol. Chem. 252:1799-1806(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-333.
[3]"Atomic co-ordinates for dogfish M4 apo-lactate dehydrogenase."
Adams M.J., Ford G.C., Liljas A., Rossmann M.G.
Biochem. Biophys. Res. Commun. 53:46-51(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY.
[4]"Structural adaptations of lactate dehydrogenase isozymes."
Eventoff W., Rossmann M.G., Taylor S.S., Torff H.-J., Meyer H., Keil W., Kiltz H.-H.
Proc. Natl. Acad. Sci. U.S.A. 74:2677-2681(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"Refined crystal structure of dogfish M4 apo-lactate dehydrogenase."
Abad-Zapatero C., Griffith J.P., Sussman J.L., Rossmann M.G.
J. Mol. Biol. 198:445-467(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U38893 mRNA. Translation: AAA91038.1.
PIRDEDFLM. A00350.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LDMX-ray2.10A2-333[»]
3LDHX-ray3.00A4-333[»]
6LDHX-ray2.00A2-333[»]
8LDHX-ray2.80A2-333[»]
ProteinModelPortalP00341.
SMRP00341. Positions 2-333.
ModBaseSearch...

Proteomic databases

PRIDEP00341.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000462.

Enzyme and pathway databases

SABIO-RKP00341.
UniPathwayUPA00554; UER00611.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
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.
PTHR11540:SF3. PTHR11540:SF3. 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. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00341.

Entry information

Entry nameLDHA_SQUAC
AccessionPrimary (citable) accession number: P00341
Secondary accession number(s): Q92114
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 106 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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