ID   CHMO_BETVU              Reviewed;         446 AA.
AC   O22553;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Choline monooxygenase, chloroplastic;
DE            EC=1.14.15.7;
DE   Flags: Precursor;
GN   Name=CMO;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Great Western D-2; TISSUE=Leaf;
RX   PubMed=9489025; DOI=10.1104/pp.116.2.859;
RA   Russell B.L., Rathinasabapathi B., Hanson A.D.;
RT   "Osmotic stress induces expression of choline monooxygenase in sugar beet
RT   and amaranth.";
RL   Plant Physiol. 116:859-865(1998).
CC   -!- FUNCTION: Catalyzes the first step of the osmoprotectant glycine
CC       betaine synthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC         betaine aldehyde hydrate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:17769, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15870, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738; EC=1.14.15.7;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC       Note=Binds 1 [2Fe-2S] cluster.;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC       Note=Binds 1 Fe cation. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (monooxygenase route):
CC       step 1/1.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC   -!- INDUCTION: By salt and drought stress.
CC   -!- SIMILARITY: Belongs to the choline monooxygenase family. {ECO:0000305}.
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DR   EMBL; AF023132; AAB80954.1; -; mRNA.
DR   PIR; T14542; T14542.
DR   AlphaFoldDB; O22553; -.
DR   SMR; O22553; -.
DR   EnsemblPlants; KMT07791; KMT07791; BVRB_6g146100.
DR   Gramene; KMT07791; KMT07791; BVRB_6g146100.
DR   BRENDA; 1.14.15.7; 836.
DR   UniPathway; UPA00529; UER00430.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0019133; F:choline monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   PANTHER; PTHR43756; PTHR43756; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Chloroplast; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Plastid; Stress response; Transit peptide.
FT   TRANSIT         1..65
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           66..446
FT                   /note="Choline monooxygenase, chloroplastic"
FT                   /id="PRO_0000020927"
FT   DOMAIN          127..234
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         169
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         171
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         188
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         191
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         294
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         299
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   446 AA;  50219 MW;  5D8518485D020402 CRC64;
     MAASATTMLL KYPTLCAMPN SSSSSNNNDL PTSIPLNNNN NLLSNKNKIL QTPNINTSTN
     KIITKAVASP VFPTLKTTSN TPSSIRSLVH EFDPEIPPED ALTPPSTWYT EPAFYSHELE
     RIFYKGWQVA GYSEQVKEKN QYFTGSLGNV EYLVSRDGQG ELHAFHNVCT HRASILACGS
     GKKSCFVCPY HGWVYGLDGS LAKASKATET QNLDPKELGL APLKVAEWGP FILISLDRSL
     DANADVGTEW IGKSAEDVKA HAFDPNLKFT HRSEFPMECN WKVFCDNYLD SSYHVPYAHK
     YYAAELDFDT YNTEMIEKCV IQRVGSSSNK PDGFDRLGTE AFYAFIYPNF AVERYGTWMT
     TMHVVPMGQR KCKLVVDYYL EKAMLDDKAY IDKGIAINDN VQKEDKVLCE SVQRGLETPA
     YRSGRYVMPI EKGIHHFHCW LHETLQ