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
//