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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)DescriptionActionsGraphical viewLength
    Binding sitei44FAD1
    Binding sitei71FAD1
    Binding sitei232FAD; via amide nitrogen and carbonyl oxygen1
    Binding sitei465FAD1
    Active sitei466Proton acceptorBy similarity1
    Binding sitei500FAD; via amide nitrogen1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi23 – 24FAD2
    Nucleotide bindingi90 – 92FAD3
    Nucleotide bindingi96 – 103FAD8
    Nucleotide bindingi510 – 512FAD3

    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)DescriptionActionsGraphical viewLength
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004188991 – 546Choline oxidaseAdd BLAST546

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei99Tele-8alpha-FAD histidine1

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1546
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 4Combined sources3
    Helixi6 – 8Combined sources3
    Beta strandi13 – 19Combined sources7
    Helixi23 – 32Combined sources10
    Beta strandi40 – 43Combined sources4
    Helixi53 – 56Combined sources4
    Helixi58 – 64Combined sources7
    Beta strandi73 – 75Combined sources3
    Beta strandi79 – 81Combined sources3
    Helixi95 – 98Combined sources4
    Helixi109 – 117Combined sources9
    Helixi126 – 136Combined sources11
    Beta strandi137 – 139Combined sources3
    Beta strandi154 – 159Combined sources6
    Helixi165 – 176Combined sources12
    Beta strandi184 – 188Combined sources5
    Beta strandi191 – 196Combined sources6
    Beta strandi198 – 201Combined sources4
    Beta strandi205 – 207Combined sources3
    Helixi210 – 214Combined sources5
    Helixi216 – 218Combined sources3
    Beta strandi224 – 227Combined sources4
    Beta strandi231 – 237Combined sources7
    Beta strandi241 – 251Combined sources11
    Beta strandi256 – 267Combined sources12
    Helixi270 – 280Combined sources11
    Helixi286 – 291Combined sources6
    Beta strandi297 – 299Combined sources3
    Turni301 – 304Combined sources4
    Beta strandi306 – 308Combined sources3
    Beta strandi315 – 321Combined sources7
    Beta strandi328 – 330Combined sources3
    Beta strandi333 – 337Combined sources5
    Beta strandi339 – 342Combined sources4
    Beta strandi347 – 355Combined sources9
    Turni359 – 361Combined sources3
    Helixi362 – 364Combined sources3
    Beta strandi370 – 379Combined sources10
    Beta strandi386 – 389Combined sources4
    Beta strandi391 – 393Combined sources3
    Beta strandi400 – 402Combined sources3
    Helixi412 – 428Combined sources17
    Helixi431 – 433Combined sources3
    Turni434 – 436Combined sources3
    Beta strandi437 – 443Combined sources7
    Helixi450 – 460Combined sources11
    Beta strandi487 – 489Combined sources3
    Beta strandi492 – 497Combined sources6
    Helixi500 – 502Combined sources3
    Helixi512 – 525Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliQ7X2H8.
    SMRiQ7X2H8.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti255H → R in CAA59321 (PubMed:8555454).Curated1
    Sequence conflicti255H → R in AAS99880 (PubMed:19186067).Curated1

    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
    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[»]
    ProteinModelPortaliQ7X2H8.
    SMRiQ7X2H8.
    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: November 2, 2016
    This is version 73 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.