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Protein

Choline oxidase

Gene

codA

Organism
Arthrobacter globiformis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

Choline + 2 O2 + H2O = betaine + 2 H2O2.

Cofactori

FAD1 Publication

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

    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441FAD
    Binding sitei71 – 711FAD
    Binding sitei232 – 2321FAD; via amide nitrogen and carbonyl oxygen
    Binding sitei465 – 4651FAD
    Active sitei466 – 4661Proton acceptorBy similarity
    Binding sitei500 – 5001FAD; via amide nitrogen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 242FAD
    Nucleotide bindingi90 – 923FAD
    Nucleotide bindingi96 – 1038FAD
    Nucleotide bindingi510 – 5123FAD

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    FAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-8608.
    BRENDAi1.1.3.17. 444.
    SABIO-RKQ7X2H8.
    UniPathwayiUPA00529; UER00384.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Choline oxidase (EC:1.1.3.17)
    Gene namesi
    Name:codA
    OrganismiArthrobacter globiformis
    Taxonomic identifieri1665 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011S → A: Increased efficiencies in the oxidative half-reactions and decreased efficiencies in the reductive half-reactions.
    Mutagenesisi312 – 3121E → A: Abolishes enzymatic activity.
    Mutagenesisi312 – 3121E → D: Reduces catalytic efficiency 230-fold.
    Mutagenesisi312 – 3121E → Q: Reduces affinity for choline 500-fold.
    Mutagenesisi464 – 4641V → A: Results in a 2-fold decrease in the limiting rate constant for flavin reduction. Has no effect on substrate binding.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 546546Choline oxidasePRO_0000418899Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei99 – 991Tele-8alpha-FAD histidine

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    546
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43Combined sources
    Helixi6 – 83Combined sources
    Beta strandi13 – 197Combined sources
    Helixi23 – 3210Combined sources
    Beta strandi40 – 434Combined sources
    Helixi53 – 564Combined sources
    Helixi58 – 647Combined sources
    Beta strandi73 – 753Combined sources
    Beta strandi79 – 813Combined sources
    Helixi95 – 984Combined sources
    Helixi109 – 1179Combined sources
    Helixi126 – 13611Combined sources
    Beta strandi137 – 1393Combined sources
    Beta strandi154 – 1596Combined sources
    Helixi165 – 17612Combined sources
    Beta strandi184 – 1885Combined sources
    Beta strandi191 – 1966Combined sources
    Beta strandi198 – 2014Combined sources
    Beta strandi205 – 2073Combined sources
    Helixi210 – 2145Combined sources
    Helixi216 – 2183Combined sources
    Beta strandi224 – 2274Combined sources
    Beta strandi231 – 2377Combined sources
    Beta strandi241 – 25111Combined sources
    Beta strandi256 – 26712Combined sources
    Helixi270 – 28011Combined sources
    Helixi286 – 2916Combined sources
    Beta strandi297 – 2993Combined sources
    Turni301 – 3044Combined sources
    Beta strandi306 – 3083Combined sources
    Beta strandi315 – 3217Combined sources
    Beta strandi328 – 3303Combined sources
    Beta strandi333 – 3375Combined sources
    Beta strandi339 – 3424Combined sources
    Beta strandi347 – 3559Combined sources
    Turni359 – 3613Combined sources
    Helixi362 – 3643Combined sources
    Beta strandi370 – 37910Combined sources
    Beta strandi386 – 3894Combined sources
    Beta strandi391 – 3933Combined sources
    Beta strandi400 – 4023Combined sources
    Helixi412 – 42817Combined sources
    Helixi431 – 4333Combined sources
    Turni434 – 4363Combined sources
    Beta strandi437 – 4437Combined sources
    Helixi450 – 46011Combined sources
    Beta strandi487 – 4893Combined sources
    Beta strandi492 – 4976Combined sources
    Helixi500 – 5023Combined sources
    Helixi512 – 52514Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliQ7X2H8.
    SMRiQ7X2H8. Positions 1-526.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7X2H8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GMC oxidoreductase family.Curated

    Phylogenomic databases

    KOiK17755.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR000172. GMC_OxRdtase_N.
    IPR007867. GMC_OxRtase_C.
    [Graphical view]
    PfamiPF05199. GMC_oxred_C. 1 hit.
    PF00732. GMC_oxred_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    PROSITEiPS00624. GMC_OXRED_2. 1 hit.
    [Graphical view]

    Sequencei

    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
    Checksum:i457B2EFCEDCC06AF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti255 – 2551H → R in CAA59321 (PubMed:8555454).Curated
    Sequence conflicti255 – 2551H → R in AAS99880 (PubMed:19186067).Curated

    Mass spectrometryi

    Molecular mass is 60618.3 Da from positions 1 - 546. Determined by MALDI. Mass of the protein with one linked FAD moiety.1 Publication

    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.

    Genome annotation databases

    KEGGiag:AAP68832.

    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:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliQ7X2H8.
    SMRiQ7X2H8. Positions 1-526.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAP68832.

    Phylogenomic databases

    KOiK17755.

    Enzyme and pathway databases

    UniPathwayiUPA00529; UER00384.
    BioCyciMetaCyc:MONOMER-8608.
    BRENDAi1.1.3.17. 444.
    SABIO-RKQ7X2H8.

    Miscellaneous databases

    EvolutionaryTraceiQ7X2H8.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR000172. GMC_OxRdtase_N.
    IPR007867. GMC_OxRtase_C.
    [Graphical view]
    PfamiPF05199. GMC_oxred_C. 1 hit.
    PF00732. GMC_oxred_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    PROSITEiPS00624. GMC_OXRED_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCHOX_ARTGO
    AccessioniPrimary (citable) accession number: Q7X2H8
    Secondary accession number(s): Q59117, Q6PPA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: October 1, 2003
    Last modified: January 20, 2016
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.