ID W9HM64_FUSOX Unreviewed; 396 AA.
AC W9HM64;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN ORFNames=FOYG_15566 {ECO:0000313|EMBL:EWY81291.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY81291.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY81291.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) 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}.
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DR EMBL; JH717849; EWY81291.1; -; Genomic_DNA.
DR AlphaFoldDB; W9HM64; -.
DR HOGENOM; CLU_026244_1_2_1; -.
DR OrthoDB; 297304at2759; -.
DR UniPathway; UPA00529; UER00430.
DR Proteomes; UP000030753; 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:UP000030753}.
FT DOMAIN 171..346
FT /note="Aromatic-ring-hydroxylating dioxygenase alpha
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00848"
SQ SEQUENCE 396 AA; 45731 MW; 380BEA5DDF31B105 CRC64;
MAQSFLKRYF GLGGSSTPAA SPVTEKSAVR ALPASWYTSV EMYELEKRAI FSKKWLLTTH
KARVPNAGDW LKYEMANFEF VIARDEDGNI NAFHNITRFG TFPIVAPEQG DHGDANTGFD
QKQNGLLPIH VKVDARGFIW INMDGAKTPE VAWEDDFDNL DTHERFSYYN FDDYNFDHVW
QMEGDYNWKI LADNYNECYH CKVAHPDIPT IADLNSYWVE TQKSYIQHFG AQRQDQIDRG
FRIAVTYYLP NASTNISPHF FMIQRFVPLS PSRSIMRYEF FRNKNSSDED FNLITELYKR
VMSEDKYLCA NAQKNVNAGV FINGEMHPEM EQGPLFFQQS IREQLQNHHK KEQEVGHEIW
PAQQEAPQTT INTKATSSAN YSSGIDIRPA HKAIVV
//
