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Protein

Alanine dehydrogenase

Gene

ald

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 reversible reductive amination of pyruvate to L-alanine. However, since the physiological environment of M.tuberculosis has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-alanine. May play a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer.1 Publication

Miscellaneous

L-alanine dehydrogenase activity increases when the M.tuberculosis is shifted from aerobic to anaerobic growth conditions.1 Publication

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

<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

Inhibited by CuSO4 and ZnCl2.1 Publication

<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=98.2 µM for NADH (at pH 7.4 and at 37 degrees Celsius)1 Publication
  2. KM=0.31 mM for NAD (at pH 10.2 and at 37 degrees Celsius)1 Publication
  3. KM=0.76 mM for pyruvate (at pH 7.4 and at 25 degrees Celsius)1 Publication
  4. KM=1.45 mM for pyruvate (at pH 7.4 and at 37 degrees Celsius)1 Publication
  5. KM=13.8 mM for L-alanine (at pH 10.2 and at 37 degrees Celsius)1 Publication
  6. KM=15.6 mM for L-alanine (at pH 10.2 and at 25 degrees Celsius)1 Publication
  7. KM=35.4 mM for ammonium (at pH 7.4 and at 37 degrees Celsius)1 Publication
  1. Vmax=31.8 µmol/min/mg enzyme for reductive amination1 Publication
  2. Vmax=23.7 µmol/min/mg enzyme for oxidative deamination1 Publication

pH dependencei

Optimum pH is between 10 and 11 for the oxidative deamination and between 7 and 7.5 for the reductive amination.1 Publication

Temperature dependencei

Relatively stable, it loses only 25% of its total activity after 4 hours at 60 degrees Celsius. The enzyme is much more active at temperatures above 37 degrees Celsius, particularly in the reductive amination. The velocity almost doubles at temperatures between 60-65 degrees Celsius compared with 37 degrees Celsius. Above 65 degrees Celsius there is a sharp decrease in activity, due to thermal inactivation of the enzyme.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: L-alanine degradation via dehydrogenase pathway

This protein is involved in step 1 of the subpathway that synthesizes NH(3) and pyruvate from L-alanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Alanine dehydrogenase (LH57_15190), Alanine dehydrogenase (ald)
This subpathway is part of the pathway L-alanine degradation via dehydrogenase pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes NH(3) and pyruvate from L-alanine, the pathway L-alanine degradation via dehydrogenase pathway and in Amino-acid degradation.

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 sitei15Substrate1 Publication1
Binding sitei75Substrate1 Publication1
<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 sitei96Proton donor/acceptor1 Publication1
Binding sitei134NAD2 Publications1
Binding sitei198NAD2 Publications1
Binding sitei203NAD2 Publications1
Binding sitei220NAD2 Publications1
Active sitei270Proton donor/acceptor1 Publication1
Binding sitei279NAD2 Publications1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi323MagnesiumCombined sources1 Publication1
Metal bindingi327Magnesium; via tele nitrogenCombined 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 bindingi178 – 179NAD2 Publications2
Nucleotide bindingi239 – 240NAD2 Publications2
Nucleotide bindingi267 – 270NAD2 Publications4
Nucleotide bindingi298 – 301NAD2 Publications4

<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 functionOxidoreductase
LigandMagnesium, Metal-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00527;UER00585

<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:
Alanine dehydrogenase (EC:1.4.1.12 Publications)
Alternative name(s):
40 kDa antigen
TB43
<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:ald
Ordered Locus Names:Rv2780
ORF Names:MTV002.45
<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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...
TubercuListi
Rv2780

<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

Secreted

<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>Mutagenesisi96H → A: Completely inactive mutant. 1 Publication1
Mutagenesisi270D → A: Completely inactive mutant. 1 Publication1
Mutagenesisi270D → N: Completely inactive mutant. The bifurcated hydrogen bond between D-270 and the ribose of NAD is replaced by a single hydrogen bond. 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 ‘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_00001989941 – 371Alanine dehydrogenaseAdd BLAST371

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P9WQB1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Upon nutrient starvation.1 Publication

<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

Homohexamer. Trimer of dimers.2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv2780

<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

1371
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
P9WQB1

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

More...
SMRi
P9WQB1

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

<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 AlaDH/PNT family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DCF Bacteria
COG0686 LUCA

KEGG Orthology (KO)

More...
KOi
K00259

Identification of Orthologs from Complete Genome Data

More...
OMAi
CFETSKA

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WQB1

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05305 L-AlaDH, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008141 Ala_DH
IPR008143 Ala_DH/PNT_CS2
IPR008142 AlaDH/PNT_CS1
IPR007886 AlaDH/PNT_N
IPR007698 AlaDH/PNT_NAD(H)-bd
IPR036291 NAD(P)-bd_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR42795 PTHR42795, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01262 AlaDh_PNT_C, 1 hit
PF05222 AlaDh_PNT_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000183 Alanine_dh, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01002 AlaDh_PNT_C, 1 hit
SM01003 AlaDh_PNT_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00518 alaDH, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00836 ALADH_PNT_1, 1 hit
PS00837 ALADH_PNT_2, 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.

P9WQB1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRVGIPTETK NNEFRVAITP AGVAELTRRG HEVLIQAGAG EGSAITDADF
60 70 80 90 100
KAAGAQLVGT ADQVWADADL LLKVKEPIAA EYGRLRHGQI LFTFLHLAAS
110 120 130 140 150
RACTDALLDS GTTSIAYETV QTADGALPLL APMSEVAGRL AAQVGAYHLM
160 170 180 190 200
RTQGGRGVLM GGVPGVEPAD VVVIGAGTAG YNAARIANGM GATVTVLDIN
210 220 230 240 250
IDKLRQLDAE FCGRIHTRYS SAYELEGAVK RADLVIGAVL VPGAKAPKLV
260 270 280 290 300
SNSLVAHMKP GAVLVDIAID QGGCFEGSRP TTYDHPTFAV HDTLFYCVAN
310 320 330 340 350
MPASVPKTST YALTNATMPY VLELADHGWR AACRSNPALA KGLSTHEGAL
360 370
LSERVATDLG VPFTEPASVL A
Length:371
Mass (Da):38,713
Last modified:April 16, 2014 - v1
<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:i9DF7540524DC116A
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 conflicti13E → EFQ in CAA44791 (PubMed:1587598).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
X63069 Genomic DNA Translation: CAA44791.1
U92472 Genomic DNA Translation: AAC38804.1
AL123456 Genomic DNA Translation: CCP45579.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C70883 A43830

NCBI Reference Sequences

More...
RefSeqi
NP_217296.1, NC_000962.3
WP_003899477.1, NZ_NVQJ01000020.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP45579; CCP45579; Rv2780

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
888493

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2780

<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
X63069 Genomic DNA Translation: CAA44791.1
U92472 Genomic DNA Translation: AAC38804.1
AL123456 Genomic DNA Translation: CCP45579.1
PIRiC70883 A43830
RefSeqiNP_217296.1, NC_000962.3
WP_003899477.1, NZ_NVQJ01000020.1

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
2VHVX-ray2.80A/B1-371[»]
2VHWX-ray2.00A/B/C/D/E/F1-371[»]
2VHXX-ray2.00A/B/C/D/E/F1-371[»]
2VHYX-ray2.30A/B1-371[»]
2VHZX-ray2.04A/B1-371[»]
2VOEX-ray2.60A/B/C/D/E/F1-371[»]
2VOJX-ray2.60A/C/E1-371[»]
ProteinModelPortaliP9WQB1
SMRiP9WQB1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2780

Proteomic databases

PaxDbiP9WQB1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45579; CCP45579; Rv2780
GeneIDi888493
KEGGimtu:Rv2780

Organism-specific databases

TubercuListiRv2780

Phylogenomic databases

eggNOGiENOG4105DCF Bacteria
COG0686 LUCA
KOiK00259
OMAiCFETSKA
PhylomeDBiP9WQB1

Enzyme and pathway databases

UniPathwayi
UPA00527;UER00585

Family and domain databases

CDDicd05305 L-AlaDH, 1 hit
InterProiView protein in InterPro
IPR008141 Ala_DH
IPR008143 Ala_DH/PNT_CS2
IPR008142 AlaDH/PNT_CS1
IPR007886 AlaDH/PNT_N
IPR007698 AlaDH/PNT_NAD(H)-bd
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR42795 PTHR42795, 1 hit
PfamiView protein in Pfam
PF01262 AlaDh_PNT_C, 1 hit
PF05222 AlaDh_PNT_N, 1 hit
PIRSFiPIRSF000183 Alanine_dh, 1 hit
SMARTiView protein in SMART
SM01002 AlaDh_PNT_C, 1 hit
SM01003 AlaDh_PNT_N, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00518 alaDH, 1 hit
PROSITEiView protein in PROSITE
PS00836 ALADH_PNT_1, 1 hit
PS00837 ALADH_PNT_2, 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 nameiDHA_MYCTU
<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: P9WQB1
Secondary accession number(s): L0TC82, O33322, P30234
<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: April 16, 2014
Last sequence update: April 16, 2014
Last modified: December 5, 2018
This is version 29 of the entry and version 1 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, Complete proteome, Direct protein sequencing, Reference proteome

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
  4. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
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