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Entry version 71 (02 Jun 2021)
Sequence version 1 (19 Sep 2006)
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Protein

Aclacinomycin-N/aclacinomycin-A oxidase

Gene

aknOx

Organism
Streptomyces galilaeus
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 modification of the terminal sugar residues in the last two steps in the biosynthesis of polyketide antibiotics of the aclacinomycin group. In the first reaction, it catalyzes the oxidation of the hydroxyl group at carbon C4 of the L-rhodinose terminal sugar moiety of aclacinomycin N (AclN) to a keto group, modifying the sugar to cinerulose A and generating aclacinomycin A (AclA). In the second reaction, it catalyzes the elimination of two hydrogen atoms from cinerulose A, leading to a double bond between carbon atoms C2 and C3 and the generation of the L-aculose terminal sugar moiety of aclacinomycin Y (AclY). It can also use aclacinomycin analogs, epsilon-pyrromycinone glycosides, rhodirubins (A, B, C and E) and all triglycosides containing L-cinerulose, L-rhodinose or 2-deoxy-L-fucose as terminal sugar.

3 Publications

Miscellaneous

AknOx uses two distinct sets of catalytic residues in the two reactions. Tyr-493 is responsible for proton abstraction from the C-4 hydroxyl group in the first reaction, the oxidation of rhodinose to cinerulose A. Tyr-421 is responsible for the proton abstraction from C3 of cinerulose A in the second reaction, for formation L-aculose.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

FAD2 PublicationsNote: Binds 1 FAD per subunit in a bicovalent manner.1 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 ascorbic acid and iron ion.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

Kcat is 0.17 sec(-1) for oxidase activity with AclA.1 Publication
  1. KM=8.5 µM for AclA1 Publication

    pH dependencei

    Optimum pH is 5.5.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei421Proton acceptor1 Publication1
    <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 sitei451Aclacinomycin1 Publication1
    Binding sitei492FAD1 Publication1
    Active sitei493Proton acceptor1 Publication1

    <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 processAntibiotic biosynthesis
    LigandFAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-18204

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.3.45, 13206
    1.3.3.14, 13206

    <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:
    Aclacinomycin-N/aclacinomycin-A oxidase1 Publication (EC:1.1.3.451 Publication, EC:1.3.3.141 Publication)
    Short name:
    AknOx1 Publication
    Alternative name(s):
    Aclacinomycin oxidoreductase1 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:aknOx1 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>OrganismiStreptomyces galilaeus
    <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 identifieri33899 [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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    <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

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene accumulate various aclacinomycin analogs.1 Publication

    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>Mutagenesisi187Y → F: Loss of oxidase activity. Loss of oxidase activity; when associated with F-493. 1 Publication1
    Mutagenesisi314H → A: The oxidase activity is similar to the wild-type. 1 Publication1
    Mutagenesisi417E → A or Q: The oxidase activity is slightly decreased. 1 Publication1
    Mutagenesisi419S → A: The oxidase activity is slightly decreased. 1 Publication1
    Mutagenesisi421Y → F: The oxidase activity for the first reaction is similar to the wild-type. Loss of oxidase activity; when associated with F-493. 1 Publication1
    Mutagenesisi493Y → F: Loss of oxidase activity. Loss of oxidase activity; when associated with F-187 and F-421. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 43Tat-type signalPROSITE-ProRule annotation1 PublicationAdd BLAST43
    <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_000043067244 – 545Aclacinomycin-N/aclacinomycin-A oxidaseAdd BLAST502

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki113 ↔ 1736-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)1 Publication

    <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

    Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.PROSITE-ProRule annotation1 Publication
    The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.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; dimer of dimers.

    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

    Secondary structure

    1545
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    Q0PCD7

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q0PCD7

    <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%5Fand%5Fdomains%5Fsection">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>Domaini76 – 256FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST181

    <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

    Keywords - Domaini

    Signal

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR012951, BBE
    IPR016166, FAD-bd_PCMH
    IPR036318, FAD-bd_PCMH-like_sf
    IPR006094, Oxid_FAD_bind_N
    IPR006311, TAT_signal

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08031, BBE, 1 hit
    PF01565, FAD_binding_4, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56176, SSF56176, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51387, FAD_PCMH, 1 hit
    PS51318, TAT, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    Q0PCD7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MFVLNEFTRR GFLGTAAAVG GTTVVTTALG GAPAAQAAVP EAADGGACGA
    60 70 80 90 100
    RTALVKVDRV DRRYQDLVTR GFNGRFRGRP DVVYVVHTAD QVVDAVNQAM
    110 120 130 140 150
    AAGQRIAVRS GGHCFEGFVD DPAVRAVIDM SQMRQVFYDS GKRAFAVEPG
    160 170 180 190 200
    ATLGETYRAL YLDWGVTIPA GVCPQVGVGG HVLGGGYGPL SRRDGVVADH
    210 220 230 240 250
    LYAVEVVVVD ASGRARKVVA TSAADDPNRE LWWAHTGGGG GNFGIVTRYW
    260 270 280 290 300
    FRTPGATGTD PSQLLPKAPT STLRHIVTWD WSALTEEAFT RIIDNHGAWH
    310 320 330 340 350
    QSNSAAGTPY ASMHSVFYLN SRAAGQILLD IQIDGGLDGA EALLNDFVAA
    360 370 380 390 400
    VNEGTGVEPA VQRSTEPWLR ATLANKFDTG GFDRTKSKGA YLRKPWTAAQ
    410 420 430 440 450
    AATLYRHLSA DSQVWGEVSL YSYGGKVNSV PETATATAQR DSIIKVWMSA
    460 470 480 490 500
    TWMDPAHDDA NLAWIREIYR EIFATTGGVP VPDDRTEGTF INYPDVDLVD
    510 520 530 540
    ERWNTSGVPW YTLYYKGNYP RLQKVKARWD PRDVFRHALS VRPPG
    Length:545
    Mass (Da):59,014
    Last modified:September 19, 2006 - 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:iA51AE3C6E6229EFF
    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
    AF257324 Genomic DNA Translation: ABI15166.1

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:ABI15166

    <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
    AF257324 Genomic DNA Translation: ABI15166.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2IPIX-ray1.65A/B/C/D44-545[»]
    SMRiQ0PCD7
    ModBaseiSearch...
    PDBe-KBiSearch...

    Genome annotation databases

    KEGGiag:ABI15166

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18204
    BRENDAi1.1.3.45, 13206
    1.3.3.14, 13206

    Miscellaneous databases

    EvolutionaryTraceiQ0PCD7

    Family and domain databases

    InterProiView protein in InterPro
    IPR012951, BBE
    IPR016166, FAD-bd_PCMH
    IPR036318, FAD-bd_PCMH-like_sf
    IPR006094, Oxid_FAD_bind_N
    IPR006311, TAT_signal
    PfamiView protein in Pfam
    PF08031, BBE, 1 hit
    PF01565, FAD_binding_4, 1 hit
    SUPFAMiSSF56176, SSF56176, 1 hit
    PROSITEiView protein in PROSITE
    PS51387, FAD_PCMH, 1 hit
    PS51318, TAT, 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 nameiAKNOX_STRGJ
    <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: Q0PCD7
    <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 29, 2014
    Last sequence update: September 19, 2006
    Last modified: June 2, 2021
    This is version 71 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

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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