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Protein

Ornithine decarboxylase

Gene
N/A
Organism
Trypanosoma brucei brucei
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 first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.By similarity

<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

pyridoxal 5'-phosphate3 Publications

<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

Inhibited by antizyme (AZ) in response to polyamine levels. AZ inhibits the assembly of the functional homodimer by binding to ODC monomers and targeting them for ubiquitin-independent proteolytic destruction by the 26S proteasome.By similarity

<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 15 sec(-1) with L-ornithine as substrate.1 Publication
  1. KM=400 µM for L-ornithine1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: putrescine biosynthesis via L-ornithine pathway

    This protein is involved in step 1 of the subpathway that synthesizes putrescine from L-ornithine.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Ornithine decarboxylase
    This subpathway is part of the pathway putrescine biosynthesis via L-ornithine pathway, which is itself part of Amine and polyamine biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from L-ornithine, the pathway putrescine biosynthesis via L-ornithine pathway and in Amine and polyamine biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei195Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates1 Publication1
    <p>This subsection of the ‘Function’ 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 sitei198Pyridoxal phosphate3 Publications1
    Binding sitei235Pyridoxal phosphate; via amino nitrogen3 Publications1
    <p>This subsection of the ‘Function’ 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 sitei358Proton donor; shared with dimeric partner2 Publications1
    Binding sitei359Substrate; shared with dimeric partner2 Publications1
    Binding sitei387Pyridoxal phosphate3 Publications1

    <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

    • ornithine decarboxylase activity Source: GeneDB

    GO - Biological processi

    • polyamine biosynthetic process Source: GeneDB
    • putrescine biosynthetic process from ornithine Source: UniProtKB-UniPathway

    <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 functionDecarboxylase, Lyase
    Biological processPolyamine biosynthesis
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.1.17 6519

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P07805

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

    More...
    UniPathwayi
    UPA00535;UER00288

    <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:
    Ornithine decarboxylase (EC:4.1.1.171 Publication)
    Short name:
    ODC
    <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>OrganismiTrypanosoma brucei brucei
    <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 identifieri5702 [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 lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

    <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_and_biotech_section">'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>Mutagenesisi358C → S or A: Converts the enzyme into a decarboxylation-dependent transaminase, producing gamma-aminobutyaldehyde (gamma-ABA) and pyridoxamine 5-phosphate (PMP) instead of putrescine. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001499031 – 423Ornithine decarboxylaseAdd BLAST423

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei67N6-(pyridoxal phosphate)lysineCombined sources2 Publications1

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P07805

    <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

    Homodimer. Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers.By similarity

    <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

    1423
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Database of protein disorder

    More...
    DisProti
    DP00051

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P07805

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

    More...
    SMRi
    P07805

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P07805

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni272 – 275Pyridoxal phosphate binding3 Publications4
    Regioni329 – 330Substrate binding2 Publications2

    <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

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.40.37.10, 1 hit
    3.20.20.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR009006 Ala_racemase/Decarboxylase_C
    IPR022643 De-COase2_C
    IPR022644 De-COase2_N
    IPR022653 De-COase2_pyr-phos_BS
    IPR000183 Orn/DAP/Arg_de-COase
    IPR002433 Orn_de-COase
    IPR029066 PLP-binding_barrel

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11482 PTHR11482, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02784 Orn_Arg_deC_N, 1 hit
    PF00278 Orn_DAP_Arg_deC, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01179 ODADCRBXLASE
    PR01182 ORNDCRBXLASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50621 SSF50621, 1 hit
    SSF51419 SSF51419, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00878 ODR_DC_2_1, 1 hit
    PS00879 ODR_DC_2_2, 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_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.

    P07805-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MDIVVNDDLS CRFLEGFNTR DALCKKISMN TCDEGDPFFV ADLGDIVRKH
    60 70 80 90 100
    ETWKKCLPRV TPFYAVKCND DWRVLGTLAA LGTGFDCASN TEIQRVRGIG
    110 120 130 140 150
    VPPEKIIYAN PCKQISHIRY ARDSGVDVMT FDCVDELEKV AKTHPKAKMV
    160 170 180 190 200
    LRISTDDSLA RCRLSVKFGA KVEDCRFILE QAKKLNIDVT GVSFHVGSGS
    210 220 230 240 250
    TDASTFAQAI SDSRFVFDMG TELGFNMHIL DIGGGFPGTR DAPLKFEEIA
    260 270 280 290 300
    GVINNALEKH FPPDLKLTIV AEPGRYYVAS AFTLAVNVIA KKVTPGVQTD
    310 320 330 340 350
    VGAHAESNAQ SFMYYVNDGV YGSFNCILYD HAVVRPLPQR EPIPNEKLYP
    360 370 380 390 400
    SSVWGPTCDG LDQIVERYYL PEMQVGEWLL FEDMGAYTVV GTSSFNGFQS
    410 420
    PTIYYVVSGL PDHVVRELKS QKS
    Length:423
    Mass (Da):46,881
    Last modified:May 30, 2000 - 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:i924A5AA6C4CD2C36
    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 AAA30218 differs from that shown. Reason: Erroneous initiation.Curated

    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
    J02771 Genomic DNA Translation: AAA30218.1 Different initiation.
    J02771 Genomic DNA Translation: AAA30219.1

    Genome annotation databases

    GeneDB pathogen genome database from Sanger Institute

    More...
    GeneDBi
    Tb927.11.13730:pep

    <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
    J02771 Genomic DNA Translation: AAA30218.1 Different initiation.
    J02771 Genomic DNA Translation: AAA30219.1

    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
    1F3TX-ray2.00A/B/C/D1-423[»]
    1QU4X-ray2.90A/B/C/D1-423[»]
    1SZRX-ray2.15A/B/C/D1-423[»]
    2TODX-ray2.00A/B/C/D1-423[»]
    DisProtiDP00051
    ProteinModelPortaliP07805
    SMRiP07805
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiP07805

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneDBiTb927.11.13730:pep

    Enzyme and pathway databases

    UniPathwayi
    UPA00535;UER00288

    BRENDAi4.1.1.17 6519
    SABIO-RKiP07805

    Miscellaneous databases

    EvolutionaryTraceiP07805

    Family and domain databases

    Gene3Di2.40.37.10, 1 hit
    3.20.20.10, 1 hit
    InterProiView protein in InterPro
    IPR009006 Ala_racemase/Decarboxylase_C
    IPR022643 De-COase2_C
    IPR022644 De-COase2_N
    IPR022653 De-COase2_pyr-phos_BS
    IPR000183 Orn/DAP/Arg_de-COase
    IPR002433 Orn_de-COase
    IPR029066 PLP-binding_barrel
    PANTHERiPTHR11482 PTHR11482, 1 hit
    PfamiView protein in Pfam
    PF02784 Orn_Arg_deC_N, 1 hit
    PF00278 Orn_DAP_Arg_deC, 1 hit
    PRINTSiPR01179 ODADCRBXLASE
    PR01182 ORNDCRBXLASE
    SUPFAMiSSF50621 SSF50621, 1 hit
    SSF51419 SSF51419, 1 hit
    PROSITEiView protein in PROSITE
    PS00878 ODR_DC_2_1, 1 hit
    PS00879 ODR_DC_2_2, 1 hit

    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 nameiDCOR_TRYBB
    <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: P07805
    <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: August 1, 1988
    Last sequence update: May 30, 2000
    Last modified: December 5, 2018
    This is version 113 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)

    <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

    Documents

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