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Protein

Choline monooxygenase, chloroplastic

Gene

CMO

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step of the osmoprotectant glycine betaine synthesis.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi162 – 1621Iron-sulfur (2Fe-2S)Curated
Metal bindingi164 – 1641Iron-sulfur (2Fe-2S); via pros nitrogenCurated
Metal bindingi181 – 1811Iron-sulfur (2Fe-2S)Curated
Metal bindingi184 – 1841Iron-sulfur (2Fe-2S); via pros nitrogenCurated
Metal bindingi287 – 2871IronSequence Analysis
Metal bindingi292 – 2921IronSequence Analysis

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. choline monooxygenase activity Source: UniProtKB-EC
  3. iron ion binding Source: InterPro
  4. 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 Source: InterPro

GO - Biological processi

  1. aromatic compound catabolic process Source: InterPro
  2. glycine betaine biosynthetic process from choline Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00529; UER00430.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline monooxygenase, chloroplastic (EC:1.14.15.7)
Gene namesi
Name:CMO
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

  1. chloroplast stroma Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6060Chloroplast1 PublicationAdd
BLAST
Chaini61 – 439379Choline monooxygenase, chloroplasticPRO_0000020928Add
BLAST

Expressioni

Tissue specificityi

Expressed in leaves.

Inductioni

By salt stress.

Interactioni

Subunit structurei

Homotrimer or homodimer.Curated

Structurei

3D structure databases

ProteinModelPortaliO04121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini120 – 227108RieskePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the choline monooxygenase family.Curated
Contains 1 Rieske domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
3.90.380.10. 2 hits.
InterProiIPR017941. Rieske_2Fe-2S.
IPR015879. Ring_hydroxy_dOase_asu_C_dom.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
PfamiPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSiPR00090. RNGDIOXGNASE.
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O04121-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMAASASATT MLLKYPTTVC GIPNPSSNNN NDPSNNIVSI PQNTTNPTLK
60 70 80 90 100
SRTPNKITTN AVAAPSFPSL TTTTPSSIQS LVHEFDPQIP PEDAHTPPSS
110 120 130 140 150
WYTEPAFYSH ELERIFYKGW QVAGISDQIK EPNQYFTGSL GNVEYLVSRD
160 170 180 190 200
GEGKVHAFHN VCTHRASILA CGSGKKSCFV CPYHGWVYGM DGSLAKASKA
210 220 230 240 250
KPEQNLDPKE LGLVPLKVAV WGPFVLISLD RSLEEGGDVG TEWLGTSAED
260 270 280 290 300
VKAHAFDPSL QFIHRSEFPM ESNWKIFSDN YLDSSYHVPY AHKYYATELN
310 320 330 340 350
FDTYDTQMIE NVTIQRVEGS SNKPDGFDRV GIQAFYAFAY PNFAVERYGP
360 370 380 390 400
WMTTMHIHPL GPRKCKLVVD YYIENSMLDD KDYIEKGIAI NDNVQREDVV
410 420 430
LCESVQRGLE TPAYRSGRYV MPIEKGIHHF HCWLQQTLK
Length:439
Mass (Da):49,214
Last modified:July 1, 1997 - v1
Checksum:i3A99FF5B14BC8FDA
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85780 mRNA. Translation: AAB52509.1.
PIRiT09214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85780 mRNA. Translation: AAB52509.1.
PIRiT09214.

3D structure databases

ProteinModelPortaliO04121.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00529; UER00430.

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
3.90.380.10. 2 hits.
InterProiIPR017941. Rieske_2Fe-2S.
IPR015879. Ring_hydroxy_dOase_asu_C_dom.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
PfamiPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSiPR00090. RNGDIOXGNASE.
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCHMO_SPIOL
AccessioniPrimary (citable) accession number: O04121
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: July 1, 1997
Last modified: January 7, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.