Choline monooxygenase, chloroplastic precursor

Contribute

Send feedback

Read comments (?) or add your own

O04121 (CHMO_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Choline monooxygenase, chloroplastic
EC=1.14.15.7

Gene names

Name:

CMO

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Chenopodioideae › Anserineae › Spinacia

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast 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

Ontologies

Keywords
Biological process	Stress response
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: InterPro glycine betaine biosynthetic process from choline Inferred from electronic annotation. Source: UniProtKB-UniPathway response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW choline monooxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of two atoms of oxygen into one donor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 60

Chloroplast Ref.1

Chain

61 – 439

379

Choline monooxygenase, chloroplastic

PRO_0000020928

Regions

Domain

120 – 227

108

Rieske

Sites

Metal binding

162

Iron-sulfur (2Fe-2S) Probable

Metal binding

164

Iron-sulfur (2Fe-2S); via pros nitrogen Probable

Metal binding

181

Iron-sulfur (2Fe-2S) Probable

Metal binding

184

Iron-sulfur (2Fe-2S); via pros nitrogen Probable

Metal binding

287

Iron Potential

Metal binding

292

Iron Potential

Sequences

Sequence

Length

Mass (Da)

Tools

O04121 [UniParc].

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

FASTA

439

49,214

        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.
PIR	T09214.
3D structure databases
ProteinModelPortal	O04121.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00529; UER00430.
Family and domain databases
Gene3D	2.102.10.10. 1 hit. 3.90.380.10. 2 hits.
InterPro	IPR017941. Rieske_2Fe-2S. IPR015879. Ring_hydroxy_dOase_asu_C_dom. IPR001663. Rng_hydr_dOase-A. [Graphical view]
Pfam	PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
SUPFAM	SSF50022. Rieske_dom. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHMO_SPIOL

Accession

Primary (citable) accession number: O04121

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2002
Last sequence update:	July 1, 1997
Last modified:	May 29, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents