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O04121 (CHMO_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Choline monooxygenase, chloroplastic

EC=1.14.15.7
Gene names
Name:CMO
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first step of the osmoprotectant glycine betaine synthesis.

Catalytic activity

Choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin.

Cofactor

Binds 1 2Fe-2S cluster.

Binds 1 iron ion Probable.

Magnesium By similarity.

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (monooxygenase route): step 1/1.

Subunit structure

Homotrimer or homodimer Probable.

Subcellular location

Plastidchloroplast stroma.

Tissue specificity

Expressed in leaves.

Induction

By salt stress.

Sequence similarities

Belongs to the choline monooxygenase family.

Contains 1 Rieske domain.

Mass spectrometry

Molecular mass is 42864±22 Da from positions 61 - 439. Determined by MALDI. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6060Chloroplast Ref.1
Chain61 – 439379Choline monooxygenase, chloroplastic
PRO_0000020928

Regions

Domain120 – 227108Rieske

Sites

Metal binding1621Iron-sulfur (2Fe-2S) Probable
Metal binding1641Iron-sulfur (2Fe-2S); via pros nitrogen Probable
Metal binding1811Iron-sulfur (2Fe-2S) Probable
Metal binding1841Iron-sulfur (2Fe-2S); via pros nitrogen Probable
Metal binding2871Iron Potential
Metal binding2921Iron Potential

Sequences

Sequence LengthMass (Da)Tools
O04121 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 3A99FF5B14BC8FDA

FASTA43949,214
        10         20         30         40         50         60 
MMAASASATT MLLKYPTTVC GIPNPSSNNN NDPSNNIVSI PQNTTNPTLK SRTPNKITTN 

        70         80         90        100        110        120 
AVAAPSFPSL TTTTPSSIQS LVHEFDPQIP PEDAHTPPSS WYTEPAFYSH ELERIFYKGW 

       130        140        150        160        170        180 
QVAGISDQIK EPNQYFTGSL GNVEYLVSRD GEGKVHAFHN VCTHRASILA CGSGKKSCFV 

       190        200        210        220        230        240 
CPYHGWVYGM DGSLAKASKA KPEQNLDPKE LGLVPLKVAV WGPFVLISLD RSLEEGGDVG 

       250        260        270        280        290        300 
TEWLGTSAED VKAHAFDPSL QFIHRSEFPM ESNWKIFSDN YLDSSYHVPY AHKYYATELN 

       310        320        330        340        350        360 
FDTYDTQMIE NVTIQRVEGS SNKPDGFDRV GIQAFYAFAY PNFAVERYGP WMTTMHIHPL 

       370        380        390        400        410        420 
GPRKCKLVVD YYIENSMLDD KDYIEKGIAI NDNVQREDVV LCESVQRGLE TPAYRSGRYV 

       430 
MPIEKGIHHF HCWLQQTLK 

« Hide

References

[1]"Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: prosthetic group characterization and cDNA cloning."
Rathinasabapathi B., Burnet M., Russell B.L., Gage D.A., Liao P.-C., Nye G.J., Scott P., Golbeck J.H., Hanson A.D.
Proc. Natl. Acad. Sci. U.S.A. 94:3454-3458(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-84; 200-225; 253-288; 317-361; 367-379; 408-415 AND 419-438, MASS SPECTROMETRY.
Strain: cv. Savoy hybrid 612.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85780 mRNA. Translation: AAB52509.1.
PIRT09214.

3D structure databases

ProteinModelPortalO04121.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00529; UER00430.

Family and domain databases

Gene3D2.102.10.10. 1 hit.
3.90.380.10. 2 hits.
InterProIPR017941. Rieske_2Fe-2S.
IPR015879. Ring_hydroxy_dOase_asu_C_dom.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
PfamPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSPR00090. RNGDIOXGNASE.
SUPFAMSSF50022. SSF50022. 1 hit.
PROSITEPS51296. RIESKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHMO_SPIOL
AccessionPrimary (citable) accession number: O04121
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: July 1, 1997
Last modified: February 19, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways