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Database: UniProt
Entry: A0A2B7XS35_9EURO
LinkDB: A0A2B7XS35_9EURO
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ID   A0A2B7XS35_9EURO        Unreviewed;       308 AA.
AC   A0A2B7XS35;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE            EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN   ORFNames=AJ79_04666 {ECO:0000313|EMBL:PGH11765.1};
OS   Helicocarpus griseus UAMH5409.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX   NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH11765.1, ECO:0000313|Proteomes:UP000223968};
RN   [1] {ECO:0000313|EMBL:PGH11765.1, ECO:0000313|Proteomes:UP000223968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH11765.1,
RC   ECO:0000313|Proteomes:UP000223968};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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:PGH11765.1}.
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DR   EMBL; PDNB01000068; PGH11765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7XS35; -.
DR   STRING; 1447875.A0A2B7XS35; -.
DR   OrthoDB; 297304at2759; -.
DR   UniPathway; UPA00529; UER00430.
DR   Proteomes; UP000223968; 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; 2.
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:UP000223968}.
FT   DOMAIN          122..173
FT                   /note="Aromatic-ring-hydroxylating dioxygenase alpha
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00848"
FT   DOMAIN          188..289
FT                   /note="Aromatic-ring-hydroxylating dioxygenase alpha
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00848"
SQ   SEQUENCE   308 AA;  35774 MW;  AC0864A7C4ED2DEA CRC64;
     MTELQRTLPA SWYRSLPLYH LERRAVFLKA WYLLGPVTRF HEVGSKVYYE IAQESIYVER
     HSGTSVLPTV GELKVVHGST GLELPCHLTP TGLLFGTISQ DAPDFYEFYP DLEPLLERVD
     FTRLPHRRSI KYEGNFNWKT MVDGYQECLH CQYTHPSFSV YYPPTFYTVY NHLNFSQHVA
     DPKKPDDGLF LYFFPNCTLN VYGGGMSSFR VCPTENPNVT RMEFDYYHLE SGDKFEEYFK
     FVRQVAMEDY ELCEKAQENL QKGVYNEGIL NPVKETGVAY YQNRVFDLVT DQHKLEKLCG
     GSEKGGGR
//
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