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O32765 (LDH_LACHE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase

Short name=L-LDH
EC=1.1.1.27
Gene names
Name:ldh
Synonyms:ldhL
OrganismLactobacillus helveticus (Lactobacillus suntoryeus)
Taxonomic identifier1587 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-lactate + NAD+ = pyruvate + NADH. HAMAP MF_00488

Enzyme regulation

Fructose-1,6-diphosphate-dependent. HAMAP MF_00488

Pathway

Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP MF_00488

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP MF_00488.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processglycolysis

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

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323L-lactate dehydrogenase HAMAP MF_00488
PRO_0000168348

Regions

Nucleotide binding16 – 4429NAD By similarity

Sites

Active site1791Proton acceptor By similarity
Binding site921Substrate By similarity
Binding site1241NAD or substrate By similarity
Binding site1551Substrate By similarity
Binding site2321Substrate By similarity

Amino acid modifications

Modified residue2231Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
O32765 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 835E52465AA4C35A

FASTA32335,111
        10         20         30         40         50         60 
MAREEKPRKV ILVGDGAVGS TFAFSMVQQG IAEELGIIDI AKEHVEGDAI DLADATPWTS 

        70         80         90        100        110        120 
PKNIYAADYP DCKDADLVVI TAGAPQKPGE TRLDLVNKNL KILSSIVEPV VESGFEGIFL 

       130        140        150        160        170        180 
VVANPVDILT HATWRMSGFP KDRVIGSGTS LDTGRLQKVI GKMENVDPSS VNAYMLGEHG 

       190        200        210        220        230        240 
DTEFPAWSYN NVAGVKVADW VKAHNMPESK LEDIHQEVKD MAYDIINKKG ATFYGIGTAS 

       250        260        270        280        290        300 
AMIAKAILND EHRVLPLSVP MDGEYGLHDL HIGTPAVVGR KGLEQVIEMP LSDKEQELMT 

       310        320 
ASADQLKKVM DKAFKETGVK VRQ 

« Hide

References

[1]"Molecular genetic characterization of the L-lactate dehydrogenase gene (ldhL) of Lactobacillus helveticus and biochemical characterization of the enzyme."
Savijoki K., Palva A.
Appl. Environ. Microbiol. 63:2850-2856(1997) [PubMed: 9212432] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: 53/7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z81318 Genomic DNA. Translation: CAB03618.1.

3D structure databases

ProteinModelPortalO32765.
SMRO32765. Positions 8-316.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00488. Lactate_dehydrog.
[Tree]
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]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11540: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...

Entry information

Entry nameLDH_LACHE
AccessionPrimary (citable) accession number: O32765
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: January 1, 1998
Last modified: December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families