ID C3Z2U0_BRAFL Unreviewed; 410 AA.
AC C3Z2U0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN Name=LOC118416715 {ECO:0000313|RefSeq:XP_035677811.1};
GN ORFNames=BRAFLDRAFT_118191 {ECO:0000313|EMBL:EEN53341.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN53341.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN53341.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN53341.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
RN [2] {ECO:0000313|RefSeq:XP_035677811.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035677811.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035677811.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the first step of the osmoprotectant glycine
CC betaine synthesis. {ECO:0000256|ARBA:ARBA00002149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC betaine aldehyde hydrate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:17769, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15870, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738; EC=1.14.15.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001883};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine aldehyde from choline (monooxygenase route):
CC step 1/1. {ECO:0000256|ARBA:ARBA00004866}.
CC -!- SIMILARITY: Belongs to the choline monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010848}.
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DR EMBL; GG666574; EEN53341.1; -; Genomic_DNA.
DR RefSeq; XP_002597329.1; XM_002597283.1.
DR RefSeq; XP_035677811.1; XM_035821918.1.
DR STRING; 7739.C3Z2U0; -.
DR KEGG; bfo:118416715; -.
DR eggNOG; ENOG502QQJW; Eukaryota.
DR InParanoid; C3Z2U0; -.
DR OMA; NIMVEWY; -.
DR OrthoDB; 294884at2759; -.
DR UniPathway; UPA00529; UER00430.
DR Proteomes; UP000001554; Chromosome 5.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0019133; F:choline monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43756:SF5; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000313|RefSeq:XP_035677811.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554}.
FT DOMAIN 81..187
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 410 AA; 46471 MW; A36EEA9ED6C9EAA8 CRC64;
MGRLFKVGCA FVRHRSSVLT PILQVVTKPL STTSTSVTTE VHKFCLETPI DEATTPPASW
YTDGRLHDLE MRTVFRRNWV AVGVANQVAK PGQFFTGVLG TDPFVVVRDQ SDQLRAFHNV
CRHRANIVVR QGEGQAQHFT CCYHGWTYRL DGRLSKALRL RGIKNFSARE NGLKPVAVRT
WGPVVLVQLE GDGREDFEEK TSPLLQHLDT QGFTHGMRHI CRRIYDAKCN WKLLVENAQD
HNSHVEYVHK DLAKIVDLPS TKVQATELYS KMTGQGATEN EQSTEGQRYG QAGYIVANVF
PNLAINRYGP WLDTNLLLPL ATDRTRIVMD YFLEEDFVKN IGDKELAEFV ETSLKDSDQV
QKEDNDICES VQRGLTSSAY DVGRYLPAIE HGPHRFHIFL GTELRKGLKL
//
