ID   CHMO_AMATR              Reviewed;         442 AA.
AC   Q93XE1;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Choline monooxygenase, chloroplastic;
DE            EC=1.14.15.7;
DE   Flags: Precursor;
GN   Name=CMO;
OS   Amaranthus tricolor (Joseph's coat) (Amaranthus gangeticus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Amaranthus.
OX   NCBI_TaxID=29722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=11642403; DOI=10.1038/sj.cr.7290085;
RA   Meng Y.L., Wang Y.M., Zhang B., Nii N.;
RT   "Isolation of a choline monooxygenase cDNA clone from Amaranthus tricolor
RT   and its expressions under stress conditions.";
RL   Cell Res. 11:187-193(2001).
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   -!- INDUCTION: By salt, drought and heat stress.
CC   -!- SIMILARITY: Belongs to the choline monooxygenase family. {ECO:0000305}.
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DR   EMBL; AF290974; AAK82768.1; -; mRNA.
DR   AlphaFoldDB; Q93XE1; -.
DR   SMR; Q93XE1; -.
DR   BRENDA; 1.14.15.7; 284.
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..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           59..442
FT                   /note="Choline monooxygenase, chloroplastic"
FT                   /id="PRO_0000020924"
FT   DOMAIN          123..229
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         165
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         167
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         184
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         187
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         290
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         295
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   442 AA;  49845 MW;  C7520F16EAA67A0E CRC64;
     MASSASMLIN YPTTFCGVRN SSNPNNDQFS DQINIPSSLN NNINISKITS KTNKIIPKAV
     ASPVIPSSIN SNNITTTTPN IKRIIHEFDP KVPAEDGFTP PSTWYTDPSL YSHELDRIFS
     KGWQVAGYSD QIKEPNQYFT GSLGNVEYLV CRDGQGKVHA FHNVCTHRAS ILACGTGKKS
     CFVCPYHGWV FGLDGSLMKA TKTENQVFDP KELGLVTLKV AIWGPFVLIS LDRSGSEGTE
     DVGKEWIGSC AEEVKKHAFD PSLQFINRSE FPMESNWKVF CDNYLDSAYH VPYAHKYYAA
     ELDFDTYKTD LLEKVVIQRV ASSSNKPNGF DRLGSEAFYA FIYPNFAVER YGPWMTTMHI
     GPLGPRKCKL VVDYYLENAM MNDKPYIEKS IMINDNVQKE DVVLCESVQR GLETPAYRSG
     RYVMPIEKGI HHFHCWLHQT LN