ID A0A1S9DW80_ASPOZ Unreviewed; 372 AA.
AC A0A1S9DW80;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN ORFNames=OAory_01010820 {ECO:0000313|EMBL:OOO13333.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO13333.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO13333.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO13333.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) 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:OOO13333.1}.
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DR EMBL; MKZY01000002; OOO13333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DW80; -.
DR VEuPathDB; FungiDB:AO090005000367; -.
DR eggNOG; ENOG502QQJW; Eukaryota.
DR OMA; NIMVEWY; -.
DR UniPathway; UPA00529; UER00430.
DR Proteomes; UP000190312; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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 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; 1.
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 Dioxygenase {ECO:0000313|EMBL:OOO13333.1};
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:UP000190312}.
FT DOMAIN 137..312
FT /note="Aromatic-ring-hydroxylating dioxygenase alpha
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00848"
FT REGION 318..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 43110 MW; 8289D1DECAE0A032 CRC64;
MSFLRNFFGT SATAAKDDQN TPIRALPASW YTSQAMYQLE RRSIFSRKWL LTTHKARVPN
PGDWVQYDAA GYEFVVMKDH QGNVKACHSS DLAPVHTHID RNGFVWVNLD ASATPEVAWK
DDFEGVDEQP RFQHYNFDEY NFDHTWDMEG DFNWKILADN YNECYHCQVA HPDIPTIADL
NSYYVKTKDG HIQHYGAQRQ DQIDKGFRIA TTYFWPNASF NISPHFFFMQ RFTPMSPTKS
VMRYEVYRHK DASDEEFNLI SDMYKRIMSE DKYLCIHTQK NLNAGVFVNG QLHPEMEKGP
LHFQKTVREV VTEHNKKEDA AGHEIWPAQR SAPQDSTVSQ DTFSFPTPVD SYTEKDDLKD
SLNANLATAI AV
//