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Entry version 91 (02 Dec 2020)
Sequence version 1 (01 Jun 2001)
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Protein

Alanine dehydrogenase

Gene

ald

Organism
Bilophila wadsworthia
Status
Reviewed-Annotation score:

Annotation score:4 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

Involved in an anaerobic respiration pathway that converts the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and sulfide. Catalyzes the oxidative deamination of alanine which regenerates pyruvate, the amino group acceptor for the taurine--pyruvate aminotransferase enzyme, and liberates ammonia. Can also catalyze the reverse reaction in vitro. Cannot use NADP(H)+ as a substrate. To a lesser extent, is also able to deaminate L-2-aminobutyrate in vitro, and in the amination reaction the enzyme can utilize oxaloacetate and 2-oxobutyrate in addition to pyruvate.

1 Publication

Miscellaneous

Taurine is an abundant dietary and host-derived molecule whose metabolism to hydrogen sulfide (H2S) by members of the human gut microbiota has many prominent connections to host health and disease. The human gut bacterium and opportunistic pathogen Bilophila wadsworthia produces H2S when respiring sulfite (HSO3-) released from organosulfonate substrates such as taurine and isethionate.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 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=1.6 mM for L-alanine (at pH 10 and 35 degrees Celsius)1 Publication
  2. KM=0.15 mM for NAD+ (at pH 10 and 35 degrees Celsius)1 Publication
  3. KM=1.1 mM for pyruvate (at pH 9 and 35 degrees Celsius)1 Publication
  4. KM=31 mM for ammonia (at pH 9 and 35 degrees Celsius)1 Publication
  5. KM=0.04 mM for NADH (at pH 9 and 35 degrees Celsius)1 Publication
  1. Vmax=17 µmol/sec/mg enzyme for the reductive amination of pyruvate1 Publication
  2. Vmax=1.2 µmol/sec/mg enzyme for the oxidative deamination of alanine1 Publication

pH dependencei

Optimum pH is 9.0 for reductive amination of pyruvate and pH 9.0-11.5 for oxidative deamination of alanine.1 Publication

Temperature dependencei

Optimum temperature is 55-60 degrees Celsius for reductive amination and 50-55 degrees Celsius for oxidative deamination. But at 60 degrees Celsius an inactivation of the enzyme is observed after about 1 minute, while at 65 degrees Celsius the enzyme is inactive after about 10 seconds.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: alkanesulfonate degradation

This protein is involved in the pathway alkanesulfonate degradation, which is part of Organosulfur degradation.1 Publication
View all proteins of this organism that are known to be involved in the pathway alkanesulfonate degradation and in Organosulfur degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei15SubstrateUniRule annotation1
Binding sitei74SubstrateUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei95Proton donor/acceptorUniRule annotation1
Binding sitei133NADUniRule annotation1
Binding sitei197NADUniRule annotation1
Binding sitei202NADUniRule annotation1
Binding sitei219NADUniRule annotation1
Active sitei269Proton donor/acceptorUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi238 – 239NADUniRule annotation2
Nucleotide bindingi266 – 269NADUniRule annotation4
Nucleotide bindingi304 – 307NADUniRule annotation4

<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
LigandNAD, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-12510

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.4.1.1, 856

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

More...
UniPathwayi
UPA00338

<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%5Fand%5Ftaxonomy%5Fsection">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 dehydrogenase1 Publication (EC:1.4.1.11 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ald1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBilophila wadsworthia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri35833 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeBilophila

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004509511 – 377Alanine dehydrogenaseAdd BLAST377

<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

Up-regulated in the presence of taurine.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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer.

1 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

<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

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
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
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q9AIK2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRVGIPTEIK VQEFRVGITP AGVHALKEAG HTVLVQKGAG LGSMITDEEY
60 70 80 90 100
VAAGAQMVAT AKECWDCDMV VKVKEPLAPE YDLFHEGLIL YTYLHLAPEP
110 120 130 140 150
ALTKALLEKK VIGIAYETVQ FDNGFLPLLA PMSEVAGRMA TQVGAQMLTK
160 170 180 190 200
IEGGMGLLMG GTAGVQAAHV VILGAGTVGL SAAKVAMGMG ARVTILDSNL
210 220 230 240 250
FRLRQIDDLF GGRIQTLASN AFNIAAATKD ADLLVGSVLI PGALTPKLVT
260 270 280 290 300
EAMVKTMKPG SAIVDVAIDQ GGCIEPTAKH GATYHDKPTF KYPVNGGEVV
310 320 330 340 350
CYSVGNMPGA VARTSTFTLT NATMPYMVDL ANKGWKKACQ DDKALARGIN
360 370
TYDGKVYFKG VSDALGYELH CTCDILK
Length:377
Mass (Da):39,853
Last modified:June 1, 2001 - 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:iA1545C407984704D
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF269148 Genomic DNA Translation: AAK38118.1

NCBI Reference Sequences

More...
RefSeqi
WP_005028751.1, NZ_CABKPK010000001.1

<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
AF269148 Genomic DNA Translation: AAK38118.1
RefSeqiWP_005028751.1, NZ_CABKPK010000001.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Phylogenomic databases

eggNOGiENOG4105DCF, Bacteria
COG0686, LUCA

Enzyme and pathway databases

UniPathwayiUPA00338
BioCyciMetaCyc:MONOMER-12510
BRENDAi1.4.1.1, 856

Family and domain databases

CDDicd05305, L-AlaDH, 1 hit
InterProiView protein in InterPro
IPR008141, Ala_DH
IPR008143, Ala_DH/PNT_CS2
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
PS00837, ALADH_PNT_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_BILWA
<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: Q9AIK2
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 7, 2020
Last sequence update: June 1, 2001
Last modified: December 2, 2020
This is version 91 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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