CHOX_ARTGO
ID CHOX_ARTGO Reviewed; 546 AA.
AC Q7X2H8; Q59117; Q6PPA2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Choline oxidase;
DE EC=1.1.3.17;
GN Name=codA;
OS Arthrobacter globiformis.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8555454; DOI=10.1007/bf00014964;
RA Deshnium P., Los D.A., Hayashi H., Mustardy L., Murata N.;
RT "Transformation of Synechococcus with a gene for choline oxidase enhances
RT tolerance to salt stress.";
RL Plant Mol. Biol. 29:897-907(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, MASS SPECTROMETRY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 8010 / DSM 20124 / BCRC 10598 / JCM 1332 / KCTC 9101 / NBRC
RC 12137 / NCIMB 8907 / NRRL B-2979 / 168;
RX PubMed=14678796; DOI=10.1016/j.abb.2003.10.003;
RA Fan F., Ghanem M., Gadda G.;
RT "Cloning, sequence analysis, and purification of choline oxidase from
RT Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress
RT tolerance.";
RL Arch. Biochem. Biophys. 421:149-158(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MTCC 944;
RX PubMed=19186067; DOI=10.1016/j.plaphy.2009.01.001;
RA Sharmila P., Phanindra M.L., Anwar F., Singh K., Gupta S.,
RA Pardha Saradhi P.;
RT "Targeting prokaryotic choline oxidase into chloroplasts enhance the
RT potential of photosynthetic machinery of plants to withstand oxidative
RT damage.";
RL Plant Physiol. Biochem. 47:391-396(2009).
RN [4]
RP FUNCTION, AND COFACTOR.
RX PubMed=12795615; DOI=10.1021/bi0274266;
RA Rand T., Halkier T., Hansen O.C.;
RT "Structural characterization and mapping of the covalently linked FAD
RT cofactor in choline oxidase from Arthrobacter globiformis.";
RL Biochemistry 42:7188-7194(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RC STRAIN=ATCC 8010 / DSM 20124 / BCRC 10598 / JCM 1332 / KCTC 9101 / NBRC
RC 12137 / NCIMB 8907 / NRRL B-2979 / 168;
RX PubMed=18072756; DOI=10.1021/bi7017943;
RA Quaye O., Lountos G.T., Fan F., Orville A.M., Gadda G.;
RT "Role of Glu312 in binding and positioning of the substrate for the hydride
RT transfer reaction in choline oxidase.";
RL Biochemistry 47:243-256(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF MUTANT ALA-101.
RX PubMed=20561507; DOI=10.1016/j.abb.2010.06.014;
RA Finnegan S., Yuan H., Wang Y.F., Orville A.M., Weber I.T., Gadda G.;
RT "Structural and kinetic studies on the Ser101Ala variant of choline
RT oxidase: catalysis by compromise.";
RL Arch. Biochem. Biophys. 501:207-213(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT ALA-464.
RX PubMed=20184377; DOI=10.1021/bi902048c;
RA Finnegan S., Agniswamy J., Weber I.T., Gadda G.;
RT "Role of valine 464 in the flavin oxidation reaction catalyzed by choline
RT oxidase.";
RL Biochemistry 49:2952-2961(2010).
CC -!- FUNCTION: Catalyzes the two-step oxidative conversion of choline to
CC glycine-betaine with betaine aldehyde as an intermediate. Glycine-
CC betaine accumulates to high levels in the cytoplasm of cells to prevent
CC dehydration and plasmolysis in adverse hyperosmotic environments.
CC Accepts either choline or the reaction intermediate betaine-aldehyde as
CC substrate. {ECO:0000269|PubMed:12795615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choline + H2O + 2 O2 = glycine betaine + H(+) + 2 H2O2;
CC Xref=Rhea:RHEA:11536, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17750; EC=1.1.3.17;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12795615};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for choline {ECO:0000269|PubMed:14678796};
CC KM=2.3 mM for betaine aldehyde {ECO:0000269|PubMed:14678796};
CC Note=kcat is 13.4 sec(-1) with choline as substrate and 11.6 sec(-1)
CC with betaine aldehyde as substrate.;
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from choline: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14678796}.
CC -!- MASS SPECTROMETRY: Mass=60618.3; Method=MALDI; Note=Mass of the protein
CC with one linked FAD moiety.; Evidence={ECO:0000269|PubMed:14678796};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X84895; CAA59321.2; -; Genomic_DNA.
DR EMBL; AY304485; AAP68832.1; -; Genomic_DNA.
DR EMBL; AY589052; AAS99880.1; -; Genomic_DNA.
DR PIR; S62689; S52489.
DR PDB; 2JBV; X-ray; 1.86 A; A/B=1-546.
DR PDB; 3LJP; X-ray; 2.20 A; A/B=1-546.
DR PDB; 3NNE; X-ray; 2.47 A; A/B/C/D/E/F/G/H=1-546.
DR PDB; 4MJW; X-ray; 1.95 A; A/B=1-546.
DR PDBsum; 2JBV; -.
DR PDBsum; 3LJP; -.
DR PDBsum; 3NNE; -.
DR PDBsum; 4MJW; -.
DR AlphaFoldDB; Q7X2H8; -.
DR SMR; Q7X2H8; -.
DR KEGG; ag:AAP68832; -.
DR BioCyc; MetaCyc:MON-8608; -.
DR BRENDA; 1.1.3.17; 444.
DR SABIO-RK; Q7X2H8; -.
DR UniPathway; UPA00529; UER00384.
DR EvolutionaryTrace; Q7X2H8; -.
DR GO; GO:0033713; F:choline:oxygen 1-oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Stress response.
FT CHAIN 1..546
FT /note="Choline oxidase"
FT /id="PRO_0000418899"
FT ACT_SITE 466
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 23..24
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 90..92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 96..103
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 465
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 500
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 510..512
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT MOD_RES 99
FT /note="Tele-8alpha-FAD histidine"
FT MUTAGEN 101
FT /note="S->A: Increased efficiencies in the oxidative half-
FT reactions and decreased efficiencies in the reductive half-
FT reactions."
FT MUTAGEN 312
FT /note="E->A: Abolishes enzymatic activity."
FT MUTAGEN 312
FT /note="E->D: Reduces catalytic efficiency 230-fold."
FT MUTAGEN 312
FT /note="E->Q: Reduces affinity for choline 500-fold."
FT MUTAGEN 464
FT /note="V->A: Results in a 2-fold decrease in the limiting
FT rate constant for flavin reduction. Has no effect on
FT substrate binding."
FT CONFLICT 255
FT /note="H -> R (in Ref. 1; CAA59321 and 3; AAS99880)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3LJP"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 256..267
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2JBV"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:4MJW"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:2JBV"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 370..379
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 412..428
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:2JBV"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 450..460
FT /evidence="ECO:0007829|PDB:2JBV"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:3NNE"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:2JBV"
FT HELIX 512..525
FT /evidence="ECO:0007829|PDB:2JBV"
SQ SEQUENCE 546 AA; 59830 MW; 457B2EFCEDCC06AF CRC64;
MHIDNIENLS DREFDYIVVG GGSAGAAVAA RLSEDPAVSV ALVEAGPDDR GVPEVLQLDR
WMELLESGYD WDYPIEPQEN GNSFMRHARA KVMGGCSSHN SCIAFWAPRE DLDEWEAKYG
ATGWNAEAAW PLYKRLETNE DAGPDAPHHG DSGPVHLMNV PPKDPTGVAL LDACEQAGIP
RAKFNTGTTV VNGANFFQIN RRADGTRSSS SVSYIHPIVE QENFTLLTGL RARQLVFDAD
RRCTGVDIVD SAFGHTHRLT ARNEVVLSTG AIDTPKLLML SGIGPAAHLA EHGIEVLVDS
PGVGEHLQDH PEGVVQFEAK QPMVAESTQW WEIGIFTPTE DGLDRPDLMM HYGSVPFDMN
TLRHGYPTTE NGFSLTPNVT HARSRGTVRL RSRDFRDKPM VDPRYFTDPE GHDMRVMVAG
IRKAREIAAQ PAMAEWTGRE LSPGVEAQTD EELQDYIRKT HNTVYHPVGT VRMGAVEDEM
SPLDPELRVK GVTGLRVADA SVMPEHVTVN PNITVMMIGE RCADLIRSAR AGETTTADAE
LSAALA
