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Reviewed, UniProtKB/Swiss-Prot A0A1F3 (LDHA_BOSMU)

Last modified October 13, 2009. Version 18. 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

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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
OrganismBos mutus grunniens (Wild yak) (Bos grunniens)
Taxonomic identifier30521 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Cytoplasm By similarity.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 332331L-lactate dehydrogenase A chain
PRO_0000263071

Regions

Nucleotide binding29 – 5729NAD By similarity

Sites

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

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue51N6-acetyllysine By similarity
Modified residue141N6-acetyllysine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue811N6-acetyllysine By similarity
Modified residue1181N6-acetyllysine By similarity
Modified residue1261N6-acetyllysine By similarity
Modified residue2391Phosphotyrosine By similarity
Modified residue2781N6-acetyllysine By similarity
Modified residue3181N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
A0A1F3-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0D854570222CC3F5

FASTA33236,686
        10         20         30         40         50         60 
MATLKDQLIQ NLLKEEHVPQ NKITIVGVGA VGMACAISIL MKDLADEVAL VDVMEDKLKG 

        70         80         90        100        110        120 
EMMDLQHGSL FLRTPKIVSG KDYNVTANSR LVIITAGARQ QEGESRLNLV QRNVNIFKFI 

       130        140        150        160        170        180 
IPNIVKYSPN CKLLVVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV 

       190        200        210        220        230        240 
HPLSCHGWIL GEHGDSSVPV WSGVNVAGVS LKNLHPELGT DADKEQWKAV HKQVVDSAYE 

       250        260        270        280        290        300 
VIKLKGYTSW AIGLSVVDLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI 

       310        320        330 
SDVVKVTLTH EEEAYLKKSA DTLWGIQKEL QF

« Hide

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References

[1]"Cloning and homology modeling of yak lactate dehydrogenase A."
Zheng Y., He Q.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.

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Cross-references

Sequence databases

DQ991437 mRNA. Translation: ABJ90429.1.

3D structure databases

SMRA0A1F3. Positions 2-332.
ModBaseSearch...

Phylogenomic databases

HOVERGENA0A1F3.

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...

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Entry information

Entry nameLDHA_BOSMU
AccessionPrimary (citable) accession number: A0A1F3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 18 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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