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UniProtKB - A2QAC0 (LAD_ASPNC)

Entry version 73 (23 Feb 2022)
Sequence version 1 (23 Sep 2008)
Previous versions | rss
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Protein

L-arabinitol 4-dehydrogenase

Gene

ladA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 NAD-dependent oxidation of L-arabinitol to L-xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. Not active with NADP as cosubstrate.

2 Publications

<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 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

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.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=89 mM for L-arabinitol (at pH 9.6)3 Publications
  2. KM=5 mM for L-xylulose (at pH 9.6)3 Publications
  3. KM=50 µM for NAD (at pH 9.6)3 Publications
  4. KM=8 µM for NADH (at pH 9.6)3 Publications
  1. Vmax=96 µmol/min/mg enzyme for the forward reaction3 Publications
  2. Vmax=805 µmol/min/mg enzyme for the reverse reaction3 Publications

pH dependencei

Optimum pH is 9.4. Active from pH 7 to pH 11.3 Publications

Temperature dependencei

Optimum temperature is 40-50 degrees Celsius.3 Publications

<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: L-arabinose degradation via L-arabinitol

This protein is involved in step 2 of the subpathway that synthesizes D-xylulose 5-phosphate from L-arabinose (fungal route).1 Publication This subpathway is part of the pathway L-arabinose degradation via L-arabinitol, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from L-arabinose (fungal route), the pathway L-arabinose degradation via L-arabinitol and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi55Zinc; catalyticBy similarity1
Metal bindingi80Zinc; catalyticBy similarity1
Metal bindingi81Zinc; catalyticBy similarity1
Metal bindingi110Zinc; structuralBy similarity1
Metal bindingi113Zinc; structuralBy similarity1
Metal bindingi116Zinc; structuralBy similarity1
Metal bindingi124Zinc; structuralBy similarity1
Metal bindingi165Zinc; catalyticBy similarity1
<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 sitei213NADBy similarity1
Binding sitei218NADBy similarity1
Binding sitei293NAD; via carbonyl oxygenBy similarity1

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 bindingi192 – 193NADBy similarity2
Nucleotide bindingi317 – 319NADBy similarity3

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
Biological processArabinose catabolism, Carbohydrate metabolism
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.12, 518

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

More...UniPathwayi		UPA00146;UER00575

<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:
L-arabinitol 4-dehydrogenase (EC:1.1.1.12)
Short name:
LAD
<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:ladA
ORF Names:An01g10920
<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>OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
<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 identifieri425011 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Circumdati ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000006706 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 2R

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:An01g10920

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi70M → F: Abolishes enzyme activity. 1 Publication1
Mutagenesisi213 – 214DI → SR: Alters cofactor specificity from NAD to NADP; when associated with T-359. 1 Publication2
Mutagenesisi318Y → F: Increases affinity for D-sorbitol. 1 Publication1
Mutagenesisi359A → T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004184041 – 386L-arabinitol 4-dehydrogenaseAdd BLAST386

Proteomic databases

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

More...PaxDbi		A2QAC0

<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

Homotetramer.

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

3D structure databases

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

More...SMRi		A2QAC0

Database of comparative protein structure models

More...ModBasei		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 zinc-containing alcohol dehydrogenase family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_026673_11_5_1

Family and domain databases

Conserved Domains Database

More...CDDi		cd05285, sorbitol_DH, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013149, ADH_C
IPR013154, ADH_N
IPR002328, ADH_Zn_CS
IPR011032, GroES-like_sf
IPR036291, NAD(P)-bd_dom_sf
IPR045306, SDH-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08240, ADH_N, 1 hit
PF00107, ADH_zinc_N, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00059, ADH_ZINC, 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.

A2QAC0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATATVLEKA NIGVFTNTKH DLWVADAKPT LEEVKNGQGL QPGEVTIEVR 
        60         70         80         90        100
STGICGSDVH FWHAGCIGPM IVTGDHILGH ESAGQVVAVA PDVTSLKPGD 
       110        120        130        140        150
RVAVEPNIIC NACEPCLTGR YNGCENVQFL STPPVDGLLR RYVNHPAIWC 
       160        170        180        190        200
HKIGDMSYED GALLEPLSVS LAGIERSGLR LGDPCLVTGA GPIGLITLLS 
       210        220        230        240        250
ARAAGASPIV ITDIDEGRLE FAKSLVPDVR TYKVQIGLSA EQNAEGIINV 
       260        270        280        290        300
FNDGQGSGPG ALRPRIAMEC TGVESSVASA IWSVKFGGKV FVIGVGKNEM 
       310        320        330        340        350
TVPFMRLSTW EIDLQYQYRY CNTWPRAIRL VRNGVIDLKK LVTHRFLLED 
       360        370        380 
AIKAFETAAN PKTGAIKVQI MSSEDDVKAA SAGQKI
Length:386
Mass (Da):41,345
Last modified:September 23, 2008 - 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:iCCC018D7E5CF75C6
GO

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
AJ854040 Genomic DNA Translation: CAH69383.1
AM269980 Genomic DNA Translation: CAK37272.1

NCBI Reference Sequences

More...RefSeqi		XP_001389509.1, XM_001389472.2

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		CAK37272; CAK37272; An01g10920

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4977395

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ang:ANI_1_1474014

<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
AJ854040 Genomic DNA Translation: CAH69383.1
AM269980 Genomic DNA Translation: CAK37272.1
RefSeqiXP_001389509.1, XM_001389472.2

3D structure databases

SMRiA2QAC0
ModBaseiSearch...

Proteomic databases

PaxDbiA2QAC0

Genome annotation databases

EnsemblFungiiCAK37272; CAK37272; An01g10920
GeneIDi4977395
KEGGiang:ANI_1_1474014

Organism-specific databases

VEuPathDBiFungiDB:An01g10920

Phylogenomic databases

HOGENOMiCLU_026673_11_5_1

Enzyme and pathway databases

UniPathwayiUPA00146;UER00575
BRENDAi1.1.1.12, 518

Family and domain databases

CDDicd05285, sorbitol_DH, 1 hit
InterProiView protein in InterPro
IPR013149, ADH_C
IPR013154, ADH_N
IPR002328, ADH_Zn_CS
IPR011032, GroES-like_sf
IPR036291, NAD(P)-bd_dom_sf
IPR045306, SDH-like
PfamiView protein in Pfam
PF08240, ADH_N, 1 hit
PF00107, ADH_zinc_N, 1 hit
SUPFAMiSSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00059, ADH_ZINC, 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 nameiLAD_ASPNC
<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: A2QAC0
Secondary accession number(s): Q5GN52
<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: September 5, 2012
Last sequence update: September 23, 2008
Last modified: February 23, 2022
This is version 73 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 programFungal 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

Reference proteome

Documents

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