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Database: UniProt
Entry: G2X4G8_VERDV
LinkDB: G2X4G8_VERDV
Original site: G2X4G8_VERDV 
ID   G2X4G8_VERDV            Unreviewed;       421 AA.
AC   G2X4G8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE            EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN   ORFNames=VDAG_05050 {ECO:0000313|EMBL:EGY23612.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY23612.1, ECO:0000313|Proteomes:UP000001611};
RN   [1] {ECO:0000313|Proteomes:UP000001611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC   {ECO:0000313|Proteomes:UP000001611};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS572703; EGY23612.1; -; Genomic_DNA.
DR   RefSeq; XP_009653081.1; XM_009654786.1.
DR   AlphaFoldDB; G2X4G8; -.
DR   STRING; 498257.G2X4G8; -.
DR   EnsemblFungi; EGY23612; EGY23612; VDAG_05050.
DR   GeneID; 20706513; -.
DR   KEGG; vda:VDAG_05050; -.
DR   eggNOG; ENOG502QQJW; Eukaryota.
DR   HOGENOM; CLU_026244_1_2_1; -.
DR   InParanoid; G2X4G8; -.
DR   OMA; NIMVEWY; -.
DR   OrthoDB; 297304at2759; -.
DR   UniPathway; UPA00529; UER00430.
DR   Proteomes; UP000001611; Chromosome 4.
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; 2.
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   Monooxygenase {ECO:0000313|EMBL:EGY23612.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001611}.
FT   DOMAIN          49..136
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   421 AA;  48446 MW;  E2E3A97F6CB54231 CRC64;
     MSLLKRYLGL AGAAPAQDPK APVRALPASW YTSQDMYELE RRAIFSRKWL LTTHKSRLPN
     PGDWVKYDVA GYSFIVVQDR KGKINAFHNV CRHRAFPVVT STHGNSFIFS CKYHGWSYGL
     SGNLAKAPGY QDLEGFDKSQ NGLFPIHVHI DKNGFIWLNL DAGETPEIPW GEDFEGVDEQ
     QRFEHYNFED YVYDHTWEME GEYNWKILAD NYNECYHCPQ AHPDIPSIAD LNSYYVQTKA
     SHIQHFGQPT EEQIAKGFRV AATYFWPNAS MNVSPHFFFI QRFMPSGPTK SVMKYEVFRN
     KNSSDEDFGV INDMYKRIMS EDKYLCLNSQ KNLNAGIFVN GELHPELEKG PLFFQRTVRE
     VMTAHFEKEQ LLGEEIWPAQ QRVPKSAAAS QADTNFCSAV DCCRKTKITE KKQTMAEALA
     F
//
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