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Database: UniProt
Entry: W9WL74_9EURO
LinkDB: W9WL74_9EURO
Original site: W9WL74_9EURO 
ID   W9WL74_9EURO            Unreviewed;       458 AA.
AC   W9WL74;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, 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=A1O5_07824 {ECO:0000313|EMBL:EXJ68892.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ68892.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ68892.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ68892.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) 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:EXJ68892.1}.
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DR   EMBL; AMGX01000012; EXJ68892.1; -; Genomic_DNA.
DR   RefSeq; XP_007746602.1; XM_007748412.1.
DR   AlphaFoldDB; W9WL74; -.
DR   STRING; 1182543.W9WL74; -.
DR   GeneID; 19192529; -.
DR   eggNOG; ENOG502QQJW; Eukaryota.
DR   HOGENOM; CLU_026244_1_2_1; -.
DR   OrthoDB; 2086661at2759; -.
DR   UniPathway; UPA00529; UER00430.
DR   Proteomes; UP000019471; 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; 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.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019471}.
FT   DOMAIN          63..161
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          410..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  51777 MW;  B3D87A76E08B04F9 CRC64;
     MPAPIMIDDG TRSAAADVVH QLHIKGLSEK AISTDVGCSL PHGFYHLPAI YHLERRAIFS
     KRWFLVSHKA RYDNVGDYVQ YEMAGFNFVV VKNKEGDIVG FHNICRHRAF PIVHETSGTA
     KIFSCKYHGW TYGLNGKLTK APRFTPESVP AFDASDIRLF PIHTHVDRNG FVYVNLDARP
     EPEISWEEQF GDLDRQAVLQ NSGVDWDAVE YDFTWVKEGK FNWKIMQDNY NECYHCLTAH
     PDVARTTALD TYYVSPGTPH HYISHFSEPK ASILATSAFD TTRFAGRSAT HVWPGGHFSP
     NPGTGFMHLM RSLPTSPTTT RQEYDVYKLN TPHATPEAHQ RMINFYQKVV DEDFGLCERV
     QTNLERGIFE AGPLHPFHEE GVQAFQAMVL KVLRQQITLE EAAGREIWAA RPPAQRVGNK
     ETNSADAANS DGDGESDGKS ICAKMLDCDQ TRLKVLEW
//
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