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Entry version 54 (05 Dec 2018)
Sequence version 1 (01 Oct 2002)
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Protein

NADH-dependent phenylglyoxylate dehydrogenase subunit beta

Gene

padI

Organism
Azoarcus evansii
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

Involved in the anaerobic metabolism of phenylalanine and phenylacetate. Catalyzes the oxidative decarboxylation of phenylglyoxylate to benzoyl-CoA and CO2. It can also react slowly with 2-oxo-3-methylbutanoate and use different electron acceptors such as benzyl viologen, methyl viologen, FAD or FMN, but NAD seems to be the physiological electron acceptor. Also catalyzes an isotope exchange between CO2 and the carboxyl group which proves partial or complete reversibility of the oxidative decarboxylation reaction.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

[4Fe-4S] cluster1 PublicationNote: Binds 3 [4Fe-4S] clusters per heteropentamers.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

Activated by magnesium ions and thiamine diphosphate.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=45 µM for phenylglyoxylate (under anaerobic conditions at 37 degrees Celsius and pH 7.8)1 Publication
  2. KM=55 µM for coenzyme-A (under anaerobic conditions at 37 degrees Celsius and pH 7.8)1 Publication
  3. KM=74 µM for NAD (under anaerobic conditions at 37 degrees Celsius and pH 7.8)1 Publication

    pH dependencei

    Optimum pH is 8 when measured with benzyl viologen. Half-maximal activities are obtained at pH 9 and pH 6.8.1 Publication

    <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
    Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD

    <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:
    NADH-dependent phenylglyoxylate dehydrogenase subunit beta (EC:1.2.1.58)
    Alternative name(s):
    Phenylglyoxylate:NAD oxidoreductase
    Phenylglyoxylate:acceptor oxidoreductase
    <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:padI
    <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>OrganismiAzoarcus evansii
    <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 identifieri59406 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesZoogloeaceaeAzoarcus

    <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_00004185371 – 446NADH-dependent phenylglyoxylate dehydrogenase subunit betaAdd BLAST446

    <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

    Induced anaerobically by phenylalanine, phenylacetate or phenylglyoxylate.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

    Dimer of heteropentamers composed of an alpha (PadG), a beta (PadI), a gamma (PadE), a delta (PadF) and an epsilon (PadH) subunit.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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q8L3A9

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

    More...
    SMRi
    Q8L3A9

    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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini6 – 354Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST30
    Domaini49 – 804Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32
    Domaini82 – 1114Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30
    Domaini109 – 1414Fe-4S ferredoxin-type 4PROSITE-ProRule annotationAdd BLAST33

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K18356

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017896 4Fe4S_Fe-S-bd
    IPR029061 THDP-binding
    IPR011766 TPP_enzyme-bd_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF13247 Fer4_11, 1 hit
    PF12837 Fer4_6, 1 hit
    PF02775 TPP_enzyme_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52518 SSF52518, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51379 4FE4S_FER_2, 4 hits

    <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.

    Q8L3A9-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGRAYSTIAF DPAKCDGCGD CMTACAQAKT GTDDIARSRI QIYGREGAAD
    60 70 80 90 100
    KTFELALCRQ CADPKCVTVC PAGALNKDGT SGVIGWDATK CVDCLLCTVG
    110 120 130 140 150
    CAYAGIALDE ATGHVAKCDT CDGNPACVPA CPHGALKHIT TANIYNEVGD
    160 170 180 190 200
    WEDLFAPGLA GCQGCNTELL MRHTLRRVGP DTVLATPPGC VPGMGSVGFN
    210 220 230 240 250
    GTTGTKVPVF HPLLTNTAAM LAGIKRQYKR VGRDVQALAI AGDGGASDVG
    260 270 280 290 300
    FQSLSGRAER GEQMLFMVVD NEGYMNTGMQ RSSCTPYGAW TSTTPVGETS
    310 320 330 340 350
    RGKTQDAKNL PLIMVNHRCA YVATASTAYM EDLYDKLDKA IAASKNGFAY
    360 370 380 390 400
    LHVYSPCTTA WRFPSNLNME VARKAVETNF VMLWEYTPQD GLHFTKPVDD
    410 420 430 440
    PLPVTDYLKA MGRFRHLTPE QVEHIQKKVV ENQKFVERMT EHAHVG
    Length:446
    Mass (Da):47,981
    Last modified:October 1, 2002 - 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:iEFCEC3C164D92F50
    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
    AJ428571 Genomic DNA Translation: CAD21693.1

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:CAD21693

    <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
    AJ428571 Genomic DNA Translation: CAD21693.1

    3D structure databases

    ProteinModelPortaliQ8L3A9
    SMRiQ8L3A9
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:CAD21693

    Phylogenomic databases

    KOiK18356

    Family and domain databases

    InterProiView protein in InterPro
    IPR017896 4Fe4S_Fe-S-bd
    IPR029061 THDP-binding
    IPR011766 TPP_enzyme-bd_C
    PfamiView protein in Pfam
    PF13247 Fer4_11, 1 hit
    PF12837 Fer4_6, 1 hit
    PF02775 TPP_enzyme_C, 1 hit
    SUPFAMiSSF52518 SSF52518, 1 hit
    PROSITEiView protein in PROSITE
    PS51379 4FE4S_FER_2, 4 hits

    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 nameiPADI_AZOEV
    <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: Q8L3A9
    <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: September 5, 2012
    Last sequence update: October 1, 2002
    Last modified: December 5, 2018
    This is version 54 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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