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Database: UniProt
Entry: E1ZKG6_CHLVA
LinkDB: E1ZKG6_CHLVA
Original site: E1ZKG6_CHLVA 
ID   E1ZKG6_CHLVA            Unreviewed;       953 AA.
AC   E1ZKG6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE            EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN   ORFNames=CHLNCDRAFT_136500 {ECO:0000313|EMBL:EFN53689.1};
OS   Chlorella variabilis (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN   [1] {ECO:0000313|EMBL:EFN53689.1, ECO:0000313|Proteomes:UP000008141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC64A {ECO:0000313|EMBL:EFN53689.1,
RC   ECO:0000313|Proteomes:UP000008141};
RX   PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA   Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA   Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA   Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT   "The Chlorella variabilis NC64A genome reveals adaptation to
RT   photosymbiosis, coevolution with viruses, and cryptic sex.";
RL   Plant Cell 22:2943-2955(2010).
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; GL433850; EFN53689.1; -; Genomic_DNA.
DR   RefSeq; XP_005845791.1; XM_005845729.1.
DR   AlphaFoldDB; E1ZKG6; -.
DR   STRING; 554065.E1ZKG6; -.
DR   GeneID; 17353235; -.
DR   KEGG; cvr:CHLNCDRAFT_136500; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   InParanoid; E1ZKG6; -.
DR   OrthoDB; 297304at2759; -.
DR   UniPathway; UPA00529; UER00430.
DR   Proteomes; UP000008141; 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   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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; PF01593; Amino_oxidase; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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:UP000008141}.
FT   DOMAIN          588..695
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          36..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..736
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   953 AA;  102614 MW;  3171AB66783CB18A CRC64;
     MREMDTSSVD VEGAGVAAPE AAVAAPEAAA SLAEVAPLAA GSDPPALLPE EAEAVAEPRD
     ELPGYLEDLT DQQHRELRDR RNEERSKAGH TGFTPSTEAS DGSWGDVEWS PDQQQQPAQC
     RTPQQQQVPP RARRATWRQS WTRTHTVELA GKAGNIKVDL GASWIHGLTG NPLVALAGQA
     GVALAKQPTD YENSVLYLPD GREASDAQWL KWEATFSEFE EYVSELQARD DPLGRDPGLG
     AAARQFIQGK RLTGLDRQAF LFEVNTFVEQ EYAASVANLS LFFNYDSGLG DGDKLVTGGY
     QNLVKWLARG IDVRLGHKVI AIDSSRPDRI AVAVAGRGTF TARRVVVAVP LGVMQAGSIR
     FKPSGLPAAN RRALGMLGSG MLNKVVLVFD RVFWDADVEA INRIAPAGNG AFQETLNLFP
     VTGQPVLVAF NAANYARHLE KKSAKQVKDE FLAVLRSLYD DVPEPRSYKV TAWGRDEFSL
     GSYSYTKAPV AGEEGFIRAH RDTAKPMAGN RIFFAGEHTS VNEPATVHGA YWSGQQAARD
     VIANELPPLE PWPHAGEPIS RAATPPSSWY AQPGVLEREE SAVFQRSWLA VAHANRVAAP
     GAYTAGSLLS LEWLACRDEQ GGLHAFHNVC RHHAAILAQG AGTASCFQCP YHGWTYGLDG
     RLQRATRLKG IEDFRAADHG LVPLQVEEWG GFVWVRQRHF YGGSSRPAAA SASSGGGSKA
     IRQQEQQQQQ QQAGQEEGVA AWLGPGGSAA ALAAGIADSL VLVASREYEI ACNWKVFIDN
     YLDGGYHVSV AHPELASGLD LATYRSTLCE RLSIQSCQPA AAAAAAEAGE AHAGTSGGSA
     GEQGMWRRQR IAGGRPPAYG PWLDANYVVP LAANRCKVLF DYFLDPSLAG DAGFIEESLA
     ASHRVQLEDV ALCESVQRGL ASAAYDTGRY APGVEGPMFH FHQLLHADLA AEC
//
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