Reviewed, UniProtKB/Swiss-Prot Q93XE1 (CHMO_AMATR)

Names and origin

Protein names

Recommended name:
    Choline monooxygenase, chloroplastic
    EC=1.14.15.7

Gene names

Name:

CMO

Organism

Amaranthus tricolor (Joseph's coat)

Taxonomic identifier

29722 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Amaranthus

Protein attributes

Sequence length	442 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.
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.
Induction	By salt, drought and heat stress.
Sequence similarities	Belongs to the choline monooxygenase family. Contains 1 Rieske domain.

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
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 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 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 – 58	58	Chloroplast By similarity
	Chain	59 – 442	384	Choline monooxygenase, chloroplastic		PRO_0000020924
Regions
	Domain	123 – 229	107	Rieske
Sites
	Metal binding	165	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	167	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	184	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	187	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	290	1	Iron Potential
	Metal binding	295	1	Iron Potential

Sequences

	Sequence		Length	Mass (Da)
	Q93XE1-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: C7520F16EAA67A0E	FASTA	442	49,845
	10 20 30 40 50 60 MASSASMLIN YPTTFCGVRN SSNPNNDQFS DQINIPSSLN NNINISKITS KTNKIIPKAV 70 80 90 100 110 120 ASPVIPSSIN SNNITTTTPN IKRIIHEFDP KVPAEDGFTP PSTWYTDPSL YSHELDRIFS 130 140 150 160 170 180 KGWQVAGYSD QIKEPNQYFT GSLGNVEYLV CRDGQGKVHA FHNVCTHRAS ILACGTGKKS 190 200 210 220 230 240 CFVCPYHGWV FGLDGSLMKA TKTENQVFDP KELGLVTLKV AIWGPFVLIS LDRSGSEGTE 250 260 270 280 290 300 DVGKEWIGSC AEEVKKHAFD PSLQFINRSE FPMESNWKVF CDNYLDSAYH VPYAHKYYAA 310 320 330 340 350 360 ELDFDTYKTD LLEKVVIQRV ASSSNKPNGF DRLGSEAFYA FIYPNFAVER YGPWMTTMHI 370 380 390 400 410 420 GPLGPRKCKL VVDYYLENAM MNDKPYIEKS IMINDNVQKE DVVLCESVQR GLETPAYRSG 430 440 RYVMPIEKGI HHFHCWLHQT LN

References

[1]	"Isolation of a choline monooxygenase cDNA clone from Amaranthus tricolor and its expressions under stress conditions." Meng Y.L., Wang Y.M., Zhang B., Nii N. Cell Res. 11:187-193(2001) [PubMed: 11642403] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF290974 mRNA. Translation: AAK82768.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.15.7. 257490.
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_AMATR

Accession

Primary (citable) accession number: Q93XE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2002
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)