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Reviewed, UniProtKB/Swiss-Prot P69083 (LDHA_GILMI)

Last modified June 16, 2009. Version 31. 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
OrganismGillichthys mirabilis (Long-jawed mudsucker)
Taxonomic identifier8222 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaAcanthopterygiiPercomorphaPerciformesGobioideiGobiidaeGobionellinaeGillichthys

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 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 – 332331L-lactate dehydrogenase A chain
PRO_0000168439

Regions

Nucleotide binding29 – 5729NAD By similarity

Sites

Active site1931Proton acceptor By similarity
Binding site991NAD By similarity
Binding site1061Substrate By similarity
Binding site1381NAD or substrate By similarity
Binding site1691Substrate By similarity
Binding site2481Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P69083-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 74507E0676453905

FASTA33236,235
        10         20         30         40         50         60 
MSTKEKLISH VSKEEAVGSR NKVTVVGVGM VGMASAISIL LKDLCDELAL VDVMEDKLKG 

        70         80         90        100        110        120 
EVMDLQHGSL FLKTHKIVAD KDYSVTANSR VVVVTAGARQ QEGESRLNLV QRNVNIFKFI 

       130        140        150        160        170        180 
IPNIVKYSPN CILMVVSNPV DILTYVAWKL SGFPRHRVIG SGTNLDSARF RHIMGEKLHL 

       190        200        210        220        230        240 
HPSSCHGWIV GEHGDSSVPV WSGVNVAGVS LQTLNPKMGA EGDSENWKAV HKMVVDGAYE 

       250        260        270        280        290        300 
VIKLKGYTSW AIGMSVADLV ESIVKNLHKV HPVSTLVKGM HGVKDEVFLS VPCVLGNSGL 

       310        320        330 
TDVIHMTLKA DEEKQLVKSA ETLWGVQKEL TL 

« Hide

References

[1]"Amino acid sequence differences cannot fully explain interspecific variation in thermal sensitivities of gobiid fish A4-lactate dehydrogenases (A4-LDHs)."
Fields P., Somero G.
J. Exp. Biol. 200:1839-1850(1997) [PubMed: 9319749] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.

Cross-references

Sequence databases

AF079460 mRNA. Translation: AAC28855.1.

3D structure databases

HSSPHSSP built from PDB template 1I0Z based on UniProtKB P07195.
SMRP69083. Positions 2-332.
ModBaseSearch...

Phylogenomic databases

HOVERGENP69083.

Enzyme and pathway databases

BRENDA1.1.1.27. 276765.

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_GILMI
AccessionPrimary (citable) accession number: P69083
Secondary accession number(s): O93620
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 31 of the entry and version 2 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