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UniProtKB - P80175 (ADHN_AMYME)

Entry version 74 (23 Feb 2022)
Sequence version 2 (16 Oct 2013)
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Protein

NDMA-dependent alcohol dehydrogenase

Gene
N/A
Organism
Amycolatopsis methanolica
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

Catalytically different from common alcohol dehydrogenases. Effective in oxidizing ethanol, other primary alcohols and benzylalcohol only in the presence of p-nitroso-N,N-dimethylaniline (NDMA) as an electron acceptor. NADH acts as a cofactor here instead as a coenzyme.

1 Publication

<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

NADH1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 trans-4-(N,N-dimethylamino)-cinnamaldehyde through direct binding to the catalytic zinc ion in a substrate-like geometry. Isobutyramide acts as competitive inhibitor with respect to the electron acceptor NDMA. Acetaldehyde, AMP, ADP, ATP, as well as CuSO4, FeSO4, HgCl2, NiCl2, ZnSO4, KCN, and NaN3 are additional inhibitors of the catalytic activity.3 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

KM for benzylalcohol is lower than 0.005 mM.1 Publication
  1. KM=0.082 mM for ethanol1 Publication
  2. KM=0.0039 mM for 1-propanol1 Publication
  3. KM=0.0025 mM for 1-butanol1 Publication
  4. KM=13.4 mM for 2-propanol1 Publication
  5. KM=10.1 mM for 2-butanol1 Publication
  6. KM=6.0 mM for formaldehyde1 Publication
  1. Vmax=5.9 µmol/min/mg enzyme toward ethanol1 Publication
  2. Vmax=6.09 µmol/min/mg enzyme toward 1-propanol1 Publication
  3. Vmax=6.09 µmol/min/mg enzyme toward 1-butanol1 Publication
  4. Vmax=5.94 µmol/min/mg enzyme toward 2-propanol1 Publication
  5. Vmax=5.7 µmol/min/mg enzyme toward 2-butanol1 Publication
  6. Vmax=5.7 µmol/min/mg enzyme toward benzylalcohol1 Publication
  7. Vmax=4.96 µmol/min/mg enzyme toward formaldehyde1 Publication

pH dependencei

Optimum pH is 7.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius.1 Publication

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 bindingi40Zinc 1; catalyticBy similarity1
Metal bindingi61Zinc 1; catalyticBy similarity1
Metal bindingi91Zinc 2By similarity1
Metal bindingi94Zinc 2By similarity1
Metal bindingi97Zinc 2By similarity1
Metal bindingi105Zinc 2By similarity1
Metal bindingi167Zinc 1; catalyticBy similarity1

<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 ...

<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
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.99.36, 314

<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:
NDMA-dependent alcohol dehydrogenase1 Publication (EC:1.1.99.361 Publication)
Short name:
NDMA-ADH1 Publication
Alternative name(s):
Nicotinoprotein alcohol/aldehyde oxidoreductase1 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>OrganismiAmycolatopsis methanolica
<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 identifieri1814 [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 lineageiBacteria › Actinobacteria › Pseudonocardiales › Pseudonocardiaceae › Amycolatopsis

<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_00000644531 – 371NDMA-dependent alcohol dehydrogenaseAdd BLAST371

<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

Homotrimer.

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		P80175

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

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013149, ADH_C
IPR013154, ADH_N
IPR023921, ADH_Zn_actinomycetes
IPR002328, ADH_Zn_CS
IPR011032, GroES-like_sf
IPR036291, NAD(P)-bd_dom_sf
IPR020843, PKS_ER

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00829, PKS_ER, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50129, SSF50129, 2 hits
SSF51735, SSF51735, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR03989, Rxyl_3153, 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.

P80175-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTKAAVLHS AGKPFEIEEL ELDGPREGEV LIKYTAAGLC HSDLHLIDND 
        60         70         80         90        100
LVPRFPIVGG HEGAGVIEDV GPGVTKVKPG DHVVCSFIPN CGTCRYCATG 
       110        120        130        140        150
RSNLCDMGAT ILDGGMPDGS FRFHRGGTDY GAMCMLGTFS ERATISQHSV 
       160        170        180        190        200
VKVDDWLPLE TAVLVGCGVP TGWASANYAG GVRAGDTCVV YGIGGIGINA 
       210        220        230        240        250
VQGAAHAGAA NVIAVDPVAF KREKALELGA THAFASADEA AAKVAELTWG 
       260        270        280        290        300
QMADQALITV GTVVEQVVTD AFNVIGKGGT VVITGLANPE KLTVHLSGGV 
       310        320        330        340        350
MTLFEKTVKG TLFGSANPQY DIVRLLRLYQ AGHVKLDELV TKRYSLEEVN 
       360        370 
EGYQDLRDGK NIRGVIMHSA D
Length:371
Mass (Da):38,992
Last modified:October 16, 2013 - v2
<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:iA3BC614F4A410C23
GO

Sequence databases

Protein sequence database of the Protein Information Resource

More...PIRi		S30335

<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

PIRiS30335

3D structure databases

SMRiP80175
ModBaseiSearch...

Enzyme and pathway databases

BRENDAi1.1.99.36, 314

Family and domain databases

InterProiView protein in InterPro
IPR013149, ADH_C
IPR013154, ADH_N
IPR023921, ADH_Zn_actinomycetes
IPR002328, ADH_Zn_CS
IPR011032, GroES-like_sf
IPR036291, NAD(P)-bd_dom_sf
IPR020843, PKS_ER
PfamiView protein in Pfam
PF08240, ADH_N, 1 hit
PF00107, ADH_zinc_N, 1 hit
SMARTiView protein in SMART
SM00829, PKS_ER, 1 hit
SUPFAMiSSF50129, SSF50129, 2 hits
SSF51735, SSF51735, 1 hit
TIGRFAMsiTIGR03989, Rxyl_3153, 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 nameiADHN_AMYME
<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: P80175
<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: July 1, 1993
Last sequence update: October 16, 2013
Last modified: February 23, 2022
This is version 74 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
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