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Entry: M2ZJX3_PSEFD
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Original site: M2ZJX3_PSEFD 
ID   M2ZJX3_PSEFD            Unreviewed;       411 AA.
AC   M2ZJX3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE            EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN   ORFNames=MYCFIDRAFT_34621 {ECO:0000313|EMBL:EME79409.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME79409.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME79409.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME79409.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446562; EME79409.1; -; Genomic_DNA.
DR   RefSeq; XP_007929641.1; XM_007931450.1.
DR   AlphaFoldDB; M2ZJX3; -.
DR   GeneID; 19339003; -.
DR   KEGG; pfj:MYCFIDRAFT_34621; -.
DR   eggNOG; ENOG502QQJW; Eukaryota.
DR   HOGENOM; CLU_026244_1_2_1; -.
DR   OrthoDB; 297304at2759; -.
DR   UniPathway; UPA00529; UER00430.
DR   Proteomes; UP000016932; Unassembled WGS sequence.
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   CDD; cd00680; RHO_alpha_C; 1.
DR   CDD; cd03469; Rieske_RO_Alpha_N; 1.
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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932}.
FT   DOMAIN          52..159
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   411 AA;  47566 MW;  14714B69DFE84838 CRC64;
     MASLMNFFGR GKATTEEPKK NGTVRALPAA WYTSQEMYEL ERRAIFQRRW LFITHKSRLQ
     QPGDFLRYKI AGYDFVLVVD RNNQINAFHN VCRHRAYKVV EEESGRKNIL ACRYHGWSYG
     LNGKLAKAPD YQQIEGFNKD DNSLLPIHTH VDDNGFVWIN MDAGEKPEIS FEQDVGEQNV
     KQSRFEKFNF DNYELDHVYE LNGDYNWKIA SDNFNECYHC KTTHPDVPTF LTIDSHNCEG
     DNGHLQHDQA PTKEQIEKGF DCNSTYYFPH ASMTVSPHFL MIQKFLPGGP SKSVMHYEIY
     RNKSSSDEDF HAIADTYSRV MGEDKVLCER AQSNLNAGVF VNGELHHRWE KGPLYFQQQC
     REAITEHFNK EKAAGRELNP AMQKLKEGES NSDLEICASL ACNARKEVLA W
//
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