ID A0A0N0V6D9_FUSLA Unreviewed; 398 AA.
AC A0A0N0V6D9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN ORFNames=FLAG1_07350 {ECO:0000313|EMBL:KPA39774.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA39774.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA39774.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA39774.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPA39774.1}.
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DR EMBL; JXCE01000171; KPA39774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0V6D9; -.
DR OrthoDB; 297304at2759; -.
DR UniPathway; UPA00529; UER00430.
DR Proteomes; UP000037904; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR CDD; cd00680; RHO_alpha_C; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
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; PF00848; Ring_hydroxyl_A; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00022714};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022714};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000037904}.
FT DOMAIN 173..348
FT /note="Aromatic-ring-hydroxylating dioxygenase alpha
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00848"
SQ SEQUENCE 398 AA; 45844 MW; D4C987B9D637F693 CRC64;
MAQSFLKRCF GLGGTSAAPT TCSTTPEKSA VRALPASWYT SVEMYELEKR AIFSKKWLLT
THQARLRNAG DWLKYEIANF ELVIAKDEDG NINAFHNITR FGAFPIVAPE QGDHGDASTG
FDQKQNGLLP IHVKVDARGF IWINMDGAKV PEVAWEDDFD NLDTHERFSY YNFEDYNFDH
VWEMEGDYNW KILADNYNEC YHCKVAHPDI PTIADLNSYW VETQKQYIQH FGAQRQDQID
RGFRIAVTYY LPNASTNISP HFFMIQRFVP HSPTRSTMRY EFFRNKNSSD DDFTLITELY
KRVMSEDKYL CANAQKNVNA GVFINGEMHP EMEQGPLFFQ QNVRAALQEH HKKEQEAGKE
IWPAQQEVPT TTINTKINGQ TNYSSGIDLR PAKKAIVV
//
