CHMO_SPIOL
ID CHMO_SPIOL Reviewed; 439 AA.
AC O04121;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Choline monooxygenase, chloroplastic;
DE EC=1.14.15.7;
DE Flags: Precursor;
GN Name=CMO;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-84; 200-225; 253-288;
RP 317-361; 367-379; 408-415 AND 419-438, AND MASS SPECTROMETRY.
RC STRAIN=cv. Savoy hybrid 612; TISSUE=Leaf;
RX PubMed=9096415; DOI=10.1073/pnas.94.7.3454;
RA Rathinasabapathi B., Burnet M., Russell B.L., Gage D.A., Liao P.-C.,
RA Nye G.J., Scott P., Golbeck J.H., Hanson A.D.;
RT "Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first
RT step of glycine betaine synthesis in plants: prosthetic group
RT characterization and cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3454-3458(1997).
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 -!- SUBUNIT: Homotrimer or homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- TISSUE SPECIFICITY: Expressed in leaves.
CC -!- INDUCTION: By salt stress.
CC -!- MASS SPECTROMETRY: Mass=42864; Mass_error=22; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9096415};
CC -!- SIMILARITY: Belongs to the choline monooxygenase family. {ECO:0000305}.
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DR EMBL; U85780; AAB52509.1; -; mRNA.
DR PIR; T09214; T09214.
DR AlphaFoldDB; O04121; -.
DR SMR; O04121; -.
DR PRIDE; O04121; -.
DR KEGG; ag:AAB52509; -.
DR BioCyc; MetaCyc:MON-3203; -.
DR BRENDA; 1.14.15.7; 5812.
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 1: Evidence at protein level;
KW 2Fe-2S; Chloroplast; Direct protein sequencing; Iron; Iron-sulfur;
KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Plastid;
KW Stress response; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:9096415"
FT CHAIN 61..439
FT /note="Choline monooxygenase, chloroplastic"
FT /id="PRO_0000020928"
FT DOMAIN 120..227
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 24..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 164
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 181
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 184
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 292
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
SQ SEQUENCE 439 AA; 49214 MW; 3A99FF5B14BC8FDA CRC64;
MMAASASATT MLLKYPTTVC GIPNPSSNNN NDPSNNIVSI PQNTTNPTLK SRTPNKITTN
AVAAPSFPSL TTTTPSSIQS LVHEFDPQIP PEDAHTPPSS WYTEPAFYSH ELERIFYKGW
QVAGISDQIK EPNQYFTGSL GNVEYLVSRD GEGKVHAFHN VCTHRASILA CGSGKKSCFV
CPYHGWVYGM DGSLAKASKA KPEQNLDPKE LGLVPLKVAV WGPFVLISLD RSLEEGGDVG
TEWLGTSAED VKAHAFDPSL QFIHRSEFPM ESNWKIFSDN YLDSSYHVPY AHKYYATELN
FDTYDTQMIE NVTIQRVEGS SNKPDGFDRV GIQAFYAFAY PNFAVERYGP WMTTMHIHPL
GPRKCKLVVD YYIENSMLDD KDYIEKGIAI NDNVQREDVV LCESVQRGLE TPAYRSGRYV
MPIEKGIHHF HCWLQQTLK
