Reviewed, UniProtKB/Swiss-Prot Q9SZR0 (CHMO_ARATH)

Names and origin

Protein names

Recommended name:
    Choline monooxygenase, chloroplastic
    EC=1.14.15.7

Gene names

Ordered Locus Names:	At4g29890
ORF Names:	F27B13.130

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the first step of the osmoprotectant glycine betaine synthesis By similarity.
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.
Subcellular location	Plastid › chloroplast stroma By similarity.
Sequence similarities	Belongs to the choline monooxygenase family. Contains 1 Rieske domain.
Sequence caution	The sequence CAB43664.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79747.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular aromatic compound metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction 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 electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 47	47	Chloroplast Potential
	Chain	48 – 422	375	Choline monooxygenase, chloroplastic		PRO_0000020925
Regions
	Domain	96 – 203	108	Rieske
Sites
	Metal binding	138	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	140	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	157	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	160	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	269	1	Iron Potential
	Metal binding	274	1	Iron Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9SZR0-1 [UniParc]. Last modified April 3, 2002. Version 2. Checksum: 33F84FF69D762A77	FASTA	422	47,724
	10 20 30 40 50 60 MMTTLTATVP EFLPPSLKST RGYFNSHSEF GVSISKFSRR RFHNPTRVFA VSDISKLVTE 70 80 90 100 110 120 FDPKIPLERA STPPSSWYTD PQFYSFELDR VFYGGWQAVG YSDQIKESRD FFTGRLGDVD 130 140 150 160 170 180 FVVCRDENGK IHAFHNVCSH HASILASGNG RKSCFVCLYH GWTYSLSGSL VKATRMSGIQ 190 200 210 220 230 240 NFSLSEMGLK PLRVAVWGPF VLLKVTAATS RKGEVETDEL VASEWLGTSV GRLSQGGVDS 250 260 270 280 290 300 PLSYICRREY TIDCNWKVFC DNYLDGGYHV PYAHKGLMSG LDLETYSTTI FEKVSIQECG 310 320 330 340 350 360 GGSKVGEDGF DRLGSEALYA FVYPNFMINR YGPWMDTNLV LPLGPRKCKV VFDYFLDPSL 370 380 390 400 410 420 KDDEAFIKRS LEESDRVQME DVMLCESVQR GLESQAYDKG RYALVEKPMH HFHCLLHHNL KL

References

[1]

"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.

[2]

"Arabidopsis ORF clones." Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL050352 Genomic DNA. Translation: CAB43664.1. Sequence problems. AL161575 Genomic DNA. Translation: CAB79747.1. Sequence problems. BT028917 mRNA. Translation: ABI49464.1.
IPI	IPI00541045.
RefSeq	NP_194718.2.
UniGene	At.31882
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9SZR0.
Genome annotation databases
GeneID	829111.
GenomeReviews	Gene locus AT4G29890 in contig CT486007_GR.
KEGG	ath:AT4G29890.
NMPDR	fig|3702.1.peg.20963.
Organism-specific databases
TAIR	At4g29890.
Phylogenomic databases
OMA	Q9SZR0. NVCPHRA.
Enzyme and pathway databases
BRENDA	1.14.15.7. 302.
Gene expression databases
ArrayExpress	Q9SZR0.
GermOnline	AT4G29890. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR017941. Rieske_2Fe-2S. IPR001663. Rng_hydr_dOase-A. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
PANTHER	PTHR21266:SF2. Rng_hydr_dOase-A. 1 hit.
Pfam	PF00355. Rieske. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHMO_ARATH

Accession

Primary (citable) accession number: Q9SZR0
Secondary accession number(s): Q0IGK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2002
Last sequence update:	April 3, 2002
Last modified:	June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)