ID   CHMO_ATRHO              Reviewed;         438 AA.
AC   Q9LKN0;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, 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   Atriplex hortensis (Mountain spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Atripliceae; Atriplex.
OX   NCBI_TaxID=34272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11330176;
RA   Shen Y.G., Du B.X., Zhang J.S., Chen S.Y.;
RT   "Cloning and characterization of CMO gene from Atriplex hortensis.";
RL   Sheng Wu Gong Cheng Xue Bao 17:1-6(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   -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC   -!- INDUCTION: By salt stress.
CC   -!- SIMILARITY: Belongs to the choline monooxygenase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF270651; AAF76895.1; -; mRNA.
DR   AlphaFoldDB; Q9LKN0; -.
DR   SMR; Q9LKN0; -.
DR   BRENDA; 1.14.15.7; 9991.
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..438
FT                   /note="Choline monooxygenase, chloroplastic"
FT                   /id="PRO_0000020926"
FT   DOMAIN          121..228
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         163
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
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         182
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         185
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         288
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         293
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   438 AA;  48771 MW;  C63970A1DD1CADE3 CRC64;
     MAASATTMLL KYPTTVCGIP NSSANNSTDP SNNIVQIPQT TTTNSPLLKF RTPNKPVNAV
     AAPAFPSVTT TTTTTPSSIQ SLVKDFDPLV PAEDALTPPS SWYTEPAFYA HELDRIFYKG
     WQVAGYSDQV KEANQYFTGT LGNVEYLVCR DGEGKVHAFH NVCTHRASIL ACGSGKKSCF
     VCPYHGWVYG MNGSLTKASK ATPEQSLNPD ELGLVPLKVA VWGPFILISL DRSSREVGDV
     GSEWLGSCAE DVKAHAFDPN LQFINRSEFP IESNWKIFSD NYLDSSYHVP YAHKYYATEL
     DFDTYQTDMV GNVTIQRVAG TSNNGFNRLG TQAFYAFAYP NFAVERYGPW MTTMHIVPLG
     PRKCKLVVDY YIEKSKLDDK DYIEKGIAIN DNVQKEDVVL CESVQKGLET PAYRSGRYVM
     PIEKGIHHFH CWLHQVLK