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Protein

L-lactate dehydrogenase

Gene

ldh

Organism
Lactobacillus casei
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the conversion of lactate to pyruvate.UniRule annotation1 Publication3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically activated by fructose 1,6-bisphosphate (FBP) alone under acidic conditions, while it requires additional activation factors such as divalent cations (Mn2+) under neutral conditions (PubMed:14601, PubMed:7766183). Under acidic conditions, Mn2+ is an inhibitor in the absence of fructose 1,6-bisphosphate (FBP) (PubMed:14601, PubMed:7766183). In case of L.casei, L-LDH binds four fructose 1,6-bisphosphate (FBP) molecules per tetramer, while usual allosteric L-LDH binds only two fructose 1,6-bisphosphate (FBP) molecules per tetramer (PubMed:14601, PubMed:7766183).1 Publication2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.45 mM for pyruvate (at pH 4.8)1 Publication
  2. KM=0.71 mM for pyruvate (at pH 5.5)1 Publication
  3. KM=3 mM for pyruvate (at pH 6.2)1 Publication
  4. KM=12 mM for pyruvate (at pH 7)1 Publication
  1. Vmax=2500 µmol/min/mg enzyme with pyruvate as substrate (at pH 6.2)1 Publication
  2. Vmax=2400 µmol/min/mg enzyme with pyruvate as substrate (at pH 7)1 Publication
  3. Vmax=2000 µmol/min/mg enzyme with pyruvate as substrate (at pH 5.5)1 Publication
  4. Vmax=1900 µmol/min/mg enzyme with pyruvate as substrate (at pH 4.8)1 Publication

Temperature dependencei

Thermostable up to 50 degrees Celsius. Thermostabilized in the presence of both fructose 1,6-bisphosphate (FBP) and Mn2+ ions.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh), L-lactate dehydrogenase (ldh)
This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei20NAD; via amide nitrogenUniRule annotation1
Binding sitei41NADUniRule annotation1
Binding sitei46NADUniRule annotation1
Binding sitei71NADUniRule annotation1
Binding sitei88SubstrateUniRule annotation1
Binding sitei94SubstrateUniRule annotationCombined sources1 Publication1
Binding sitei107NADUniRule annotation1
Binding sitei149NADUniRule annotation1
Binding sitei159Allosteric activatorUniRule annotationCombined sources1 Publication1
Binding sitei174Allosteric activatorUniRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei181Proton acceptorUniRule annotationCombined sources2 Publications1
Binding sitei235SubstrateUniRule annotationCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi85 – 86NADUniRule annotation2
Nucleotide bindingi124 – 126NADUniRule annotation3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Oxidoreductase
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-8681

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00343

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00554;UER00611

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
L-lactate dehydrogenase1 PublicationUniRule annotation (EC:1.1.1.27UniRule annotation1 Publication2 Publications)
Short name:
L-LDH1 PublicationUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ldh1 PublicationUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiLactobacillus casei
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1582 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi171R → Q: Exhibits no significant catalytic activity toward pyruvate up to 50 mM at pH 5.0 in the absence of fructose 1,6-bisphosphate (FBP). In the presence of 5 mM fructose 1,6-bisphosphate (FBP), it exhibits marked catalytic activity. 1 Publication1
Mutagenesisi174H → D: Shows a lower thermoresistance than the wild-type, even in the absence of fructose 1,6-bisphosphate (FBP). Not thermostabilized in the presence of fructose 1,6-bisphosphate (FBP), Mn(2+) or both. Under acidic conditions, the mutant does not show a positive allosteric regulation by fructose 1,6-bisphosphate (FBP), which even inhibits the stimulative effects of the alternative activation factors. In addition, Mn(2+) ions also show greatly reduced inhibitory effects on the mutant enzyme. Under neutral conditions, the reaction of the mutant is slightly enhanced by fructose 1,6-bisphosphate (FBP), but not further stimulates by additional Mn(2+) ions, unlike the case of the wild-type. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001683472 – 326L-lactate dehydrogenaseAdd BLAST325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei226PhosphotyrosineUniRule annotation1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P00343

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.UniRule annotation1 Publication1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00343

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P00343

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00343

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni126 – 129Substrate bindingUniRule annotationCombined sources1 Publication4
Regioni154 – 157Substrate bindingUniRule annotationCombined sources1 Publication4
Regioni171 – 174Allosteric activator bindingCombined sources1 Publication4

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the LDH/MDH superfamily. LDH family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C80 Bacteria
COG0039 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.110.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00488 Lactate_dehydrog, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001557 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
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02866 Ldh_1_C, 1 hit
PF00056 Ldh_1_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000102 Lac_mal_DH, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00086 LLDHDRGNASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit
SSF56327 SSF56327, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01771 L-LDH-NAD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00064 L_LDH, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P00343-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASITDKDHQ KVILVGDGAV GSSYAYAMVL QGIAQEIGIV DIFKDKTKGD
60 70 80 90 100
AIDLSNALPF TSPKKIYSAE YSDAKDADLV VITAGAPQKP GETRLDLVNK
110 120 130 140 150
NLKILKSIVD PIVDSGFNGI FLVAANPVDI LTYATWKLSG FPKNRVVGSG
160 170 180 190 200
TSLDTARFRQ SIAEMVNVDA RSVHAYIMGE HGDTEFPVWS HANIGGVTIA
210 220 230 240 250
EWVKAHPEIK EDKLVKMFED VRDAAYEIIK LKGATFYGIA TALARISKAI
260 270 280 290 300
LNDENAVLPL SVYMDGQYGL NDIYIGTPAV INRNGIQNIL EIPLTDHEEE
310 320
SMQKSASQLK KVLTDAFAKN DIETRQ
Length:326
Mass (Da):35,531
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i934905641592AF8A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti26Y → F AA sequence (PubMed:6411465).Curated1
Sequence conflicti52I → T AA sequence (PubMed:6411465).Curated1
Sequence conflicti88 – 89QK → KQ AA sequence (PubMed:6411465).Curated2
Sequence conflicti119G → L AA sequence (PubMed:6411465).Curated1
Sequence conflicti270L → I AA sequence (PubMed:6411465).Curated1
Sequence conflicti273I → L AA sequence (PubMed:6411465).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D12591 Genomic DNA Translation: BAA02133.1
M76708 Genomic DNA Translation: AAA25245.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A43944 DELBLA

NCBI Reference Sequences

More...
RefSeqi
WP_003567646.1, NZ_MWVD01000024.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
31583240

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12591 Genomic DNA Translation: BAA02133.1
M76708 Genomic DNA Translation: AAA25245.2
PIRiA43944 DELBLA
RefSeqiWP_003567646.1, NZ_MWVD01000024.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LLCX-ray3.00A2-326[»]
2ZQYX-ray2.60A/B/C/D1-326[»]
2ZQZX-ray2.50A/B/C/D/E/F1-326[»]
3VKUX-ray1.96A/B/C/D/E/F1-326[»]
3VKVX-ray2.70A/B/C/D/E/F1-326[»]
3VPFX-ray2.79A/B/C/D/E/F1-326[»]
ProteinModelPortaliP00343
SMRiP00343
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP00343

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi31583240

Phylogenomic databases

eggNOGiENOG4105C80 Bacteria
COG0039 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00554;UER00611

BioCyciMetaCyc:MONOMER-8681
SABIO-RKiP00343

Miscellaneous databases

EvolutionaryTraceiP00343

Family and domain databases

Gene3Di3.90.110.10, 1 hit
HAMAPiMF_00488 Lactate_dehydrog, 1 hit
InterProiView protein in InterPro
IPR001557 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
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF02866 Ldh_1_C, 1 hit
PF00056 Ldh_1_N, 1 hit
PIRSFiPIRSF000102 Lac_mal_DH, 1 hit
PRINTSiPR00086 LLDHDRGNASE
SUPFAMiSSF51735 SSF51735, 1 hit
SSF56327 SSF56327, 1 hit
TIGRFAMsiTIGR01771 L-LDH-NAD, 1 hit
PROSITEiView protein in PROSITE
PS00064 L_LDH, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLDH_LACCA
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00343
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 142 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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