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Entry version 86 (11 Dec 2019)
Sequence version 1 (01 Oct 2003)
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Protein

Choline oxidase

Gene

codA

Organism
Arthrobacter globiformis
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 two-step oxidative conversion of choline to glycine-betaine with betaine aldehyde as an intermediate. Glycine-betaine accumulates to high levels in the cytoplasm of cells to prevent dehydration and plasmolysis in adverse hyperosmotic environments. Accepts either choline or the reaction intermediate betaine-aldehyde as substrate.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

FAD1 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 13.4 sec(-1) with choline as substrate and 11.6 sec(-1) with betaine aldehyde as substrate.
  1. KM=0.6 mM for choline1 Publication
  2. KM=2.3 mM for betaine aldehyde1 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: betaine biosynthesis via choline pathway

    This protein is involved in step 1 of the subpathway that synthesizes betaine from choline.
    Proteins known to be involved in this subpathway in this organism are:
    1. Choline oxidase (codA)
    This subpathway is part of the pathway betaine biosynthesis via choline 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 betaine from choline, the pathway betaine biosynthesis via choline pathway and in Amine and polyamine biosynthesis.

    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 sitei44FAD1
    Binding sitei71FAD1
    Binding sitei232FAD; via amide nitrogen and carbonyl oxygen1
    Binding sitei465FAD1
    <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 sitei466Proton acceptorBy similarity1
    Binding sitei500FAD; via amide nitrogen1

    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 bindingi23 – 24FAD2
    Nucleotide bindingi90 – 92FAD3
    Nucleotide bindingi96 – 103FAD8
    Nucleotide bindingi510 – 512FAD3

    <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 processStress response
    LigandFAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-8608

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.3.17 444

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q7X2H8

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

    More...
    UniPathwayi
    UPA00529;UER00384

    <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:
    Choline oxidase (EC:1.1.3.17)
    <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:codA
    <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>OrganismiArthrobacter globiformis
    <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 identifieri1665 [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 lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter

    <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%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>Mutagenesisi101S → A: Increased efficiencies in the oxidative half-reactions and decreased efficiencies in the reductive half-reactions. 1
    Mutagenesisi312E → A: Abolishes enzymatic activity. 1
    Mutagenesisi312E → D: Reduces catalytic efficiency 230-fold. 1
    Mutagenesisi312E → Q: Reduces affinity for choline 500-fold. 1
    Mutagenesisi464V → A: Results in a 2-fold decrease in the limiting rate constant for flavin reduction. Has no effect on substrate binding. 1

    <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_00004188991 – 546Choline oxidaseAdd BLAST546

    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 residuei99Tele-8alpha-FAD histidine1

    <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

    Homodimer.

    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

    1546
    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
    Q7X2H8

    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
    Q7X2H8

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the GMC oxidoreductase family.Curated

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K17755

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.50.50.60, 1 hit
    4.10.450.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036188 FAD/NAD-bd_sf
    IPR027424 Glucose_Oxidase_domain_2
    IPR012132 GMC_OxRdtase
    IPR000172 GMC_OxRdtase_N
    IPR007867 GMC_OxRtase_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF05199 GMC_oxred_C, 1 hit
    PF00732 GMC_oxred_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000137 Alcohol_oxidase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51905 SSF51905, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00624 GMC_OXRED_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%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.

    Q7X2H8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MHIDNIENLS DREFDYIVVG GGSAGAAVAA RLSEDPAVSV ALVEAGPDDR
    60 70 80 90 100
    GVPEVLQLDR WMELLESGYD WDYPIEPQEN GNSFMRHARA KVMGGCSSHN
    110 120 130 140 150
    SCIAFWAPRE DLDEWEAKYG ATGWNAEAAW PLYKRLETNE DAGPDAPHHG
    160 170 180 190 200
    DSGPVHLMNV PPKDPTGVAL LDACEQAGIP RAKFNTGTTV VNGANFFQIN
    210 220 230 240 250
    RRADGTRSSS SVSYIHPIVE QENFTLLTGL RARQLVFDAD RRCTGVDIVD
    260 270 280 290 300
    SAFGHTHRLT ARNEVVLSTG AIDTPKLLML SGIGPAAHLA EHGIEVLVDS
    310 320 330 340 350
    PGVGEHLQDH PEGVVQFEAK QPMVAESTQW WEIGIFTPTE DGLDRPDLMM
    360 370 380 390 400
    HYGSVPFDMN TLRHGYPTTE NGFSLTPNVT HARSRGTVRL RSRDFRDKPM
    410 420 430 440 450
    VDPRYFTDPE GHDMRVMVAG IRKAREIAAQ PAMAEWTGRE LSPGVEAQTD
    460 470 480 490 500
    EELQDYIRKT HNTVYHPVGT VRMGAVEDEM SPLDPELRVK GVTGLRVADA
    510 520 530 540
    SVMPEHVTVN PNITVMMIGE RCADLIRSAR AGETTTADAE LSAALA
    Length:546
    Mass (Da):59,830
    Last modified:October 1, 2003 - 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:i457B2EFCEDCC06AF
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti255H → R in CAA59321 (PubMed:8555454).Curated1
    Sequence conflicti255H → R in AAS99880 (PubMed:19186067).Curated1

    <p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 60618.3 Da. Determined by MALDI. Mass of the protein with one linked FAD moiety.1 Publication

    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
    X84895 Genomic DNA Translation: CAA59321.2
    AY304485 Genomic DNA Translation: AAP68832.1
    AY589052 Genomic DNA Translation: AAS99880.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S62689 S52489

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:AAP68832

    <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
    X84895 Genomic DNA Translation: CAA59321.2
    AY304485 Genomic DNA Translation: AAP68832.1
    AY589052 Genomic DNA Translation: AAS99880.1
    PIRiS62689 S52489

    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
    2JBVX-ray1.86A/B1-546[»]
    3LJPX-ray2.20A/B1-546[»]
    3NNEX-ray2.47A/B/C/D/E/F/G/H1-546[»]
    4MJWX-ray1.95A/B1-546[»]
    SMRiQ7X2H8
    ModBaseiSearch...
    PDBe-KBiSearch...

    Genome annotation databases

    KEGGiag:AAP68832

    Phylogenomic databases

    KOiK17755

    Enzyme and pathway databases

    UniPathwayiUPA00529;UER00384
    BioCyciMetaCyc:MONOMER-8608
    BRENDAi1.1.3.17 444
    SABIO-RKiQ7X2H8

    Miscellaneous databases

    EvolutionaryTraceiQ7X2H8

    Family and domain databases

    Gene3Di3.50.50.60, 1 hit
    4.10.450.10, 1 hit
    InterProiView protein in InterPro
    IPR036188 FAD/NAD-bd_sf
    IPR027424 Glucose_Oxidase_domain_2
    IPR012132 GMC_OxRdtase
    IPR000172 GMC_OxRdtase_N
    IPR007867 GMC_OxRtase_C
    PfamiView protein in Pfam
    PF05199 GMC_oxred_C, 1 hit
    PF00732 GMC_oxred_N, 1 hit
    PIRSFiPIRSF000137 Alcohol_oxidase, 1 hit
    SUPFAMiSSF51905 SSF51905, 1 hit
    PROSITEiView protein in PROSITE
    PS00624 GMC_OXRED_2, 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 nameiCHOX_ARTGO
    <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: Q7X2H8
    Secondary accession number(s): Q59117, Q6PPA2
    <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: September 5, 2012
    Last sequence update: October 1, 2003
    Last modified: December 11, 2019
    This is version 86 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

    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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