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Entry version 96 (26 Feb 2020)
Sequence version 2 (01 Apr 2015)
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Protein

Decaprenylphosphoryl-beta-D-ribose oxidase

Gene

dprE1

Organism
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
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

Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans (PubMed:22188377). DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX) (PubMed:22188377). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex (By similarity). Can also use farnesyl-phosphoryl-beta-D-ribofuranose (FPR) as substrate in vitro (PubMed:22188377, PubMed:22956199). Appears to be essential for the growth of M.smegmatis (PubMed:21346818).By similarity3 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 <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

Is inhibited by 8-nitro-benzothiazinones (BTZs) such as BTZ043; BTZs are a new class of antimycobacterial agents that block formation of both cell-wall lipoarabinomannan and arabinogalactan via inhibition of decaprenyl-phospho-arabinose (DPA) synthesis (PubMed:19299584, PubMed:22188377). BTZs are suicide inhibitors that act via covalent modification of DprE1; the essential nitro group of these compounds is reduced by DprE1 to a nitroso group, which then specifically reacts with Cys-386 of DprE1 to form an irreversible semimercaptal adduct (PubMed:22188377, PubMed:22956199). Other compounds with diverse scaffolds (dinitrobenzamides and nitrobenzoquinoxalines) also act as covalent DprE1 inhibitors (PubMed:22956199).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

kcat is 12.7 min(-1) for epimerase activity with FPR as substrate (at pH 8.5 and 25 degrees Celsius).1 Publication
  1. KM=0.11 mM for FPR (at pH 8.5 and 25 degrees Celsius)1 Publication

    <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: cell wall polysaccharide biosynthesis

    This protein is involved in the pathway cell wall polysaccharide biosynthesis, which is part of Cell wall biogenesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway cell wall polysaccharide biosynthesis and in Cell wall biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei116FAD; via amide nitrogenCombined sources1 Publication1
    Binding sitei183FAD; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
    Binding sitei414FADCombined sources1 Publication1

    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 bindingi52 – 62FADCombined sources1 PublicationAdd BLAST11
    Nucleotide bindingi121 – 124FADCombined sources1 Publication4
    Nucleotide bindingi128 – 131FADCombined sources1 Publication4

    <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 resistance, Cell wall biogenesis/degradation
    LigandFAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-17534
    MSME246196:G1H7P-6349-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.98.3 3512

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

    More...
    UniPathwayi
    UPA00963

    <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:
    Decaprenylphosphoryl-beta-D-ribose oxidaseCurated (EC:1.1.98.31 Publication)
    Alternative name(s):
    Decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase1 Publication
    Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE11 Publication
    Short name:
    Decaprenyl-phosphoribose 2'-epimerase subunit 11 Publication
    Decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase1 Publication
    Decaprenylphosphoryl-beta-D-ribose 2-epimerase flavoprotein subunitCurated
    FAD-dependent decaprenylphosphoryl-beta-D-ribofuranose 2-oxidase1 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:dprE11 Publication
    Ordered Locus Names:MSMEG_6382, MSMEI_6214
    ORF Names:LJ00_31545
    <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>OrganismiMycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
    <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 identifieri246196 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
    <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
    • UP000006158 <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
    • UP000000757 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Periplasm

    <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

    Disruption of this gene is only possible in the presence of a plasmid-encoded copy of the gene. Curing of this 'rescue' plasmid from the bacterial population results in a cessation of growth, demonstrating gene essentiality.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>Mutagenesisi335Q → A: 10-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi386C → G: 14-fold decrease in catalytic efficiency. Reduces BTZs to inert metabolites while avoiding covalent inactivation. 2 Publications1
    Mutagenesisi417K → A: Loss of catalytic activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3797019

    <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_00004324711 – 460Decaprenylphosphoryl-beta-D-ribose oxidaseAdd BLAST460

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    A0R607

    <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

    Monomer (PubMed:22956199).

    Interacts with DprE2 to form an epimerase complex (By similarity).

    By similarity1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    246196.MSMEI_6214

    <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

    1460
    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
    A0R607

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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%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>Domaini19 – 193FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST175

    <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 DprE1 family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105IQ5 Bacteria
    COG0277 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_032465_0_0_11

    KEGG Orthology (KO)

    More...
    KOi
    K16653

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.43.10, 1 hit
    3.30.465.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR007173 ALO
    IPR016166 FAD-bd_PCMH
    IPR036318 FAD-bd_PCMH-like_sf
    IPR016167 FAD-bd_PCMH_sub1
    IPR016169 FAD-bd_PCMH_sub2
    IPR006094 Oxid_FAD_bind_N

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF04030 ALO, 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

    <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.

    A0R607-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSTTEFPTTT KRLMGWGRTA PTVASVLSTS DPEVIVRAVT RAAEEGGRGV
    60 70 80 90 100
    IARGLGRSYG DNAQNGGGLV IDMPALNRIH SIDSGTRLVD VDAGVSLDQL
    110 120 130 140 150
    MKAALPHGLW VPVLPGTRQV TVGGAIGCDI HGKNHHSAGS FGNHVRSMEL
    160 170 180 190 200
    LTANGEVRHL TPAGPDSDLF WATVGGNGLT GIILRATIEM TPTETAYFIA
    210 220 230 240 250
    DGDVTGSLDE TIAFHSDGSE ANYTYSSAWF DAISKPPKLG RAAISRGSLA
    260 270 280 290 300
    KLDQLPSKLQ KDPLKFDAPQ LLTLPDIFPN GLANKFTFMP IGELWYRKSG
    310 320 330 340 350
    TYRNKVQNLT QFYHPLDMFG EWNRAYGSAG FLQYQFVVPT EAVEEFKSII
    360 370 380 390 400
    VDIQRSGHYS FLNVFKLFGP GNQAPLSFPI PGWNVCVDFP IKAGLHEFVT
    410 420 430 440 450
    ELDRRVLEFG GRLYTAKDSR TTAETFHAMY PRIDEWIRIR RSVDPDGVFA
    460
    SDMARRLQLL
    Length:460
    Mass (Da):50,377
    Last modified:April 1, 2015 - 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:i2F19107D18638FC0
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence ABK72795 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti386C → G in strain: MN47; BTZ043-resistant. 1 Publication1
    Natural varianti386C → S in strain: MN84; BTZ043-resistant. 1 Publication1

    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
    CP000480 Genomic DNA Translation: ABK72795.1 Different initiation.
    CP001663 Genomic DNA Translation: AFP42640.1
    CP009494 Genomic DNA Translation: AIU11363.1

    NCBI Reference Sequences

    More...
    RefSeqi
    YP_890595.1, NC_008596.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ABK72795; ABK72795; MSMEG_6382
    AFP42640; AFP42640; MSMEI_6214
    AIU11363; AIU11363; LJ00_31545

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    4532115

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    msb:LJ00_31545
    msg:MSMEI_6214
    msm:MSMEG_6382

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|246196.19.peg.6209

    <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
    CP000480 Genomic DNA Translation: ABK72795.1 Different initiation.
    CP001663 Genomic DNA Translation: AFP42640.1
    CP009494 Genomic DNA Translation: AIU11363.1
    RefSeqiYP_890595.1, NC_008596.1

    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
    4AUTX-ray2.10A1-460[»]
    4F4QX-ray2.62A1-460[»]
    4G3TX-ray2.35A58-460[»]
    4G3UX-ray2.69A/B58-460[»]
    SMRiA0R607
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi246196.MSMEI_6214

    Chemistry databases

    ChEMBLiCHEMBL3797019

    Proteomic databases

    PRIDEiA0R607

    Genome annotation databases

    EnsemblBacteriaiABK72795; ABK72795; MSMEG_6382
    AFP42640; AFP42640; MSMEI_6214
    AIU11363; AIU11363; LJ00_31545
    GeneIDi4532115
    KEGGimsb:LJ00_31545
    msg:MSMEI_6214
    msm:MSMEG_6382
    PATRICifig|246196.19.peg.6209

    Phylogenomic databases

    eggNOGiENOG4105IQ5 Bacteria
    COG0277 LUCA
    HOGENOMiCLU_032465_0_0_11
    KOiK16653

    Enzyme and pathway databases

    UniPathwayiUPA00963
    BioCyciMetaCyc:MONOMER-17534
    MSME246196:G1H7P-6349-MONOMER
    BRENDAi1.1.98.3 3512

    Family and domain databases

    Gene3Di3.30.43.10, 1 hit
    3.30.465.10, 1 hit
    InterProiView protein in InterPro
    IPR007173 ALO
    IPR016166 FAD-bd_PCMH
    IPR036318 FAD-bd_PCMH-like_sf
    IPR016167 FAD-bd_PCMH_sub1
    IPR016169 FAD-bd_PCMH_sub2
    IPR006094 Oxid_FAD_bind_N
    PfamiView protein in Pfam
    PF04030 ALO, 1 hit
    PF01565 FAD_binding_4, 1 hit
    SUPFAMiSSF56176 SSF56176, 1 hit
    PROSITEiView protein in PROSITE
    PS51387 FAD_PCMH, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiDPRE1_MYCS2
    <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: A0R607
    Secondary accession number(s): I7FMU1
    <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: April 1, 2015
    Last sequence update: April 1, 2015
    Last modified: February 26, 2020
    This is version 96 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

    3D-structure, Reference proteome

    Documents

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