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Database: UniProt
Entry: W2RM89_9EURO
LinkDB: W2RM89_9EURO
Original site: W2RM89_9EURO 
ID   W2RM89_9EURO            Unreviewed;       403 AA.
AC   W2RM89;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE            EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN   ORFNames=HMPREF1541_07805 {ECO:0000313|EMBL:ETN36818.1};
OS   Cyphellophora europaea CBS 101466.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX   NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN36818.1, ECO:0000313|Proteomes:UP000030752};
RN   [1] {ECO:0000313|EMBL:ETN36818.1, ECO:0000313|Proteomes:UP000030752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN36818.1,
RC   ECO:0000313|Proteomes:UP000030752};
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 Phialophora europaea CBS 101466.";
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}.
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DR   EMBL; KB822724; ETN36818.1; -; Genomic_DNA.
DR   RefSeq; XP_008720350.1; XM_008722128.1.
DR   AlphaFoldDB; W2RM89; -.
DR   STRING; 1220924.W2RM89; -.
DR   GeneID; 19975144; -.
DR   VEuPathDB; FungiDB:HMPREF1541_07805; -.
DR   eggNOG; ENOG502QQJW; Eukaryota.
DR   HOGENOM; CLU_026244_1_2_1; -.
DR   InParanoid; W2RM89; -.
DR   OrthoDB; 297304at2759; -.
DR   UniPathway; UPA00529; UER00430.
DR   Proteomes; UP000030752; 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; 2.
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:UP000030752}.
FT   DOMAIN          169..344
FT                   /note="Aromatic-ring-hydroxylating dioxygenase alpha
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00848"
SQ   SEQUENCE   403 AA;  46519 MW;  FD7FDD4676AB17C0 CRC64;
     MASLLNYFGF GATKPQAAAE PDQGPVKTAV KALPANWYTS QPLYDLERRA IFSRKWLMIT
     HQVRIKQVGE YLRYEAANFV FILYRDASGN VKGIHNTSGL SGQPIVQEQK GTLDLSAAES
     FTFPIHIRVD QKGFIWVNLD GAETPEIPWE EDFDGVDTQP RFEGFNFNDE YEFDHEWEMT
     GDYNWKILAD NYNECYHCAS THPDLKEMAD LETYSVTTQD GYILHNVRGR PGSEGEQRYK
     VHPTYYYPST SMNVSPHFFF MQRFVPHGPV KSTMRYEVYR HKDAPESEFQ FIAQMYRRVM
     SEDKALCEAS QQNLNRGVFT NGEMHPRLEQ GPLFFQAKCR DLVKEHRQRE MMVKREIWPT
     QLSWTPRRTV VQSAKLEIPS VPAYYYSNSS GIEQGSAIAS VAA
//
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