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Entry version 84 (23 Feb 2022)
Sequence version 1 (01 Dec 2001)
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Protein

L-arabinitol 4-dehydrogenase

Gene

lad1

Organism
Hypocrea jecorina (Trichoderma reesei)
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. Can partially compensate for xylitol dehydrogenase in xdh1 mutants. Also oxidizes galactitol to L-xylo-3-hexulose as an alternative to the standard Leloir pathway for D-galactose metabolism. NADP cannot act as a cosubstrate.

4 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=18 mM for L-arabinitol (at pH 7)3 Publications
  2. KM=200 mM for xylitol (at pH 7)3 Publications
  3. KM=4.5 mM for L-arabinitol (at pH 8.6)3 Publications
  4. KM=25 mM for D-talitol (at pH 8.6)3 Publications
  5. KM=60 mM for galactitol (at pH 8.6)3 Publications
  6. KM=46 mM for D-sorbitol (at pH 8.6)3 Publications
  7. KM=11.3 mM for D-allitol (at pH 8.6)3 Publications
  8. KM=37 mM for L-mannitol (at pH 8.6)3 Publications
  9. KM=191 mM for L-iditol (at pH 8.6)3 Publications
  10. KM=580 mM for D-arabino-3-hexulose (at pH 8.6)3 Publications
  11. KM=81 mM for L-xylo-3-hexulose (at pH 8.6)3 Publications
  12. KM=96 mM for D-fructose (at pH 8.6)3 Publications
  13. KM=81 mM for D-psicose (at pH 8.6)3 Publications
  14. KM=19 mM for L-sorbitol (at pH 8.6)3 Publications
  15. KM=28 mM for L-tagatose (at pH 8.6)3 Publications
  16. KM=115 mM for D-sorbose (at pH 8.6)3 Publications
  17. KM=180 µM for NAD (at pH 7)3 Publications
  1. Vmax=27 nmol/sec/mg enzyme with L-arabinitol as substrate (at pH 9 and 10)3 Publications
  2. Vmax=10 nmol/sec/mg enzyme with L-arabinitol as substrate (at pH 7)3 Publications
  3. Vmax=6 nmol/sec/mg enzyme with xylitol as substrate (at pH 7)3 Publications
  4. Vmax=0.213 nmol/sec/mg enzyme with L-arabinitol as substrate (at pH 8.6)3 Publications
  5. Vmax=0.146 nmol/sec/mg enzyme with D-talitol as substrate (at pH 8.6)3 Publications
  6. Vmax=0.012 nmol/sec/mg enzyme with galactitol as substrate (at pH 8.6)3 Publications
  7. Vmax=0.034 nmol/sec/mg enzyme with D-sorbitol as substrate (at pH 8.6)3 Publications
  8. Vmax=0.008 nmol/sec/mg enzyme with D-allitol as substrate (at pH 8.6)3 Publications
  9. Vmax=0.027 nmol/sec/mg enzyme with L-mannitol as substrate (at pH 8.6)3 Publications
  10. Vmax=0.021 nmol/sec/mg enzyme with L-iditol as substrate (at pH 8.6)3 Publications
  11. Vmax=0.969 nmol/sec/mg enzyme with D-arabino-3-hexulose as substrate (at pH 8.6)3 Publications
  12. Vmax=0.197 nmol/sec/mg enzyme with L-xylo-3-hexulose as substrate (at pH 8.6)3 Publications
  13. Vmax=0.008 nmol/sec/mg enzyme with D-fructose as substrate (at pH 8.6)3 Publications
  14. Vmax=0.011 nmol/sec/mg enzyme with D-psicose as substrate (at pH 8.6)3 Publications
  15. Vmax=0.001 nmol/sec/mg enzyme with L-sorbitol as substrate (at pH 8.6)3 Publications
  16. Vmax=0.003 nmol/sec/mg enzyme with L-tagatose as substrate (at pH 8.6)3 Publications
  17. Vmax=0.001 nmol/sec/mg enzyme with D-sorbose as substrate (at pH 8.6)3 Publications

pH dependencei

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

Temperature dependencei

Optimum temperature is 55-65 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). 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 bindingi66Zinc; catalyticBy similarity1
Metal bindingi91Zinc; catalyticBy similarity1
Metal bindingi92Zinc; catalyticBy similarity1
Metal bindingi121Zinc; structuralBy similarity1
Metal bindingi124Zinc; structuralBy similarity1
Metal bindingi127Zinc; structuralBy similarity1
Metal bindingi135Zinc; structuralBy similarity1
Metal bindingi176Zinc; 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 sitei224NADBy similarity1
Binding sitei229NADBy similarity1
Binding sitei296NAD; 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 bindingi203 – 204NADBy similarity2
Nucleotide bindingi320 – 322NADBy 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

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
Biological processArabinose catabolism, Carbohydrate metabolism, Galactose metabolism, Xylose metabolism
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.12, 6451

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q96V44

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:lad1
<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>OrganismiHypocrea jecorina (Trichoderma reesei)
<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 identifieri51453 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:TrQ_003398

<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>Mutagenesisi224 – 225DI → SR: Alters cofactor specificity from NAD to NADP; when associated with T-362. 1 Publication2
Mutagenesisi362A → T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225. 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_00004184031 – 377L-arabinitol 4-dehydrogenaseAdd BLAST377

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

<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

Only expressed when grown on L-arabinose.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

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

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SMRi
Q96V44

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

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

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OMAi
RYNGCER

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
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

<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.

Q96V44-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSPSAVDDAP KATGAAISVK PNIGVFTNPK HDLWISEAEP SADAVKSGAD
60 70 80 90 100
LKPGEVTIAV RSTGICGSDV HFWHAGCIGP MIVEGDHILG HESAGEVIAV
110 120 130 140 150
HPTVSSLQIG DRVAIEPNII CNACEPCLTG RYNGCEKVEF LSTPPVPGLL
160 170 180 190 200
RRYVNHPAVW CHKIGNMSWE NGALLEPLSV ALAGMQRAKV QLGDPVLVCG
210 220 230 240 250
AGPIGLVSML CAAAAGACPL VITDISESRL AFAKEICPRV TTHRIEIGKS
260 270 280 290 300
AEETAKSIVS SFGGVEPAVT LECTGVESSI AAAIWASKFG GKVFVIGVGK
310 320 330 340 350
NEISIPFMRA SVREVDIQLQ YRYSNTWPRA IRLIESGVID LSKFVTHRFP
360 370
LEDAVKAFET SADPKSGAIK VMIQSLD
Length:377
Mass (Da):39,886
Last modified:December 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:i5015D4A61D948D1D
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
AF355628 mRNA Translation: AAL08944.1
AY225444 Genomic DNA Translation: AAP57209.1

<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
AF355628 mRNA Translation: AAL08944.1
AY225444 Genomic DNA Translation: AAP57209.1

3D structure databases

SMRiQ96V44
ModBaseiSearch...

Organism-specific databases

VEuPathDBiFungiDB:TrQ_003398

Phylogenomic databases

OMAiRYNGCER

Enzyme and pathway databases

UniPathwayiUPA00146;UER00575
BRENDAi1.1.1.12, 6451
SABIO-RKiQ96V44

Family and domain databases

CDDicd05285, sorbitol_DH, 1 hit
InterProiView protein in InterPro
IPR013149, ADH_C
IPR013154, ADH_N
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

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_HYPJE
<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: Q96V44
<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: December 1, 2001
Last modified: February 23, 2022
This is version 84 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

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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