ID A0A1V6Q1S8_9EURO Unreviewed; 406 AA.
AC A0A1V6Q1S8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN ORFNames=PENANT_c018G08666 {ECO:0000313|EMBL:OQD83194.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD83194.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD83194.1}.
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DR EMBL; MDYN01000018; OQD83194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6Q1S8; -.
DR STRING; 416450.A0A1V6Q1S8; -.
DR OrthoDB; 297304at2759; -.
DR UniPathway; UPA00529; UER00430.
DR Proteomes; UP000191672; 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 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; 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; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 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:UP000191672}.
FT DOMAIN 42..140
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 406 AA; 47401 MW; B1F8C6E44C45F4DF CRC64;
MWNFWSSPAK QPPSPPKGLP ASWYRSEAMY QLERRAVFSK RWILLTHSSR LKKAGDYLSF
TVANFSFFLI QDRDGNINSF HNICRHRAFP VIRERSGTTS ILSCKYHGWS YGLKGNLSKA
PRFDNETVPD FDKSQHSLFP VHVHVDRAGF VWVNLQAGDT DVKWEKEYDT IDEQPRMQDF
DFAGEFKFDH YWEMELDANW KGVIENYNEC YHCATSHPLI NGVSDLPRYR VEPKAAYMEH
HIYNKDAADS QFRRAITYFN PTTSVTVTDK FFYIQRMIPV SATKSKIENE VYRHRDATDE
EFENINAFYR QVLGEDKELC VGTQQNLDGG VFTSGELHPS KEKGPIHFQN SVRQMVMEHR
QKEEKEGCEI WPALPITPWI SKSDEEETFC SKLDAVRCTT RPELAW
//
