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Database: UniProt
Entry: A0A100IC10_ASPNG
LinkDB: A0A100IC10_ASPNG
Original site: A0A100IC10_ASPNG 
ID   A0A100IC10_ASPNG        Unreviewed;      1072 AA.
AC   A0A100IC10;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE            EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN   ORFNames=ABL_02694 {ECO:0000313|EMBL:GAQ38505.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ38505.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ38505.1}.
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DR   EMBL; BCMY01000003; GAQ38505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IC10; -.
DR   PaxDb; 5061-CADANGAP00004593; -.
DR   VEuPathDB; FungiDB:An04g09790; -.
DR   VEuPathDB; FungiDB:An04g09810; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1222968; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_130535; -.
DR   VEuPathDB; FungiDB:ATCC64974_86550; -.
DR   VEuPathDB; FungiDB:ATCC64974_86560; -.
DR   VEuPathDB; FungiDB:M747DRAFT_140870; -.
DR   VEuPathDB; FungiDB:M747DRAFT_313653; -.
DR   OMA; WRKKTRC; -.
DR   UniPathway; UPA00529; UER00430.
DR   Proteomes; UP000068243; 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:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   CDD; cd12148; fungal_TF_MHR; 1.
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   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43756:SF5; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   Pfam; PF04082; Fungal_trans; 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.
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   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          49..136
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          467..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1072 AA;  121031 MW;  8457EE4C0221B7D0 CRC64;
     MASALWNYLG LRETPTAPTN EAVRALPASW YTSQEMFELE RRAIFSRKWL LTTHKLRLPN
     TGDWLQYEVS GFNFVLVRDK EGNINAFHNV CRHRAFPLVT EEKGSARIFA CKYHGWSYGL
     NGKLAKAPGY QDLDGFDKSK NSLLPIHVHL DANGFIWVNL DAGEQPEISW DDDFKGIDLQ
     SRFADVKWED YTFDHTWEQE GDYNWKILAD NYNECYHCAT THPDIPALAD LATYSVDTKD
     GGIIHDAHSK PDQIAAGLRI ASTYYFPNAS MTVSPHFFFM QRFVPLSPTR SVMKYEVYRN
     KNSSDEDFEL INTMYKRIMS EDKYLCDLTQ KNLNAGVFVN GELHPKMEKG PLYFQKVVRD
     VVTEHFQREE KEGQEYWPAR QRVPKEAATS AQDMQFCANL GCGAGKECCS NIGAQPPAAV
     AWQSFRGCSR PFLDFAVADA PPQKDRLAEL EEKVNLILNG NILARSTGPE TKLSPPSPRR
     RDSHTPYPVP SGLGEGTTPH SSPSVIARAI NLYVEHCHRQ PVWCFDFDGP GEPGSLPEEL
     ICSLLALTLR YLHEQEQGQH YADDARTLIM LRIANGTVEL ATIESLCLLS YSSFIDGNTH
     LGQFYLGLAS QLCRAAMLDV AVAYSTDDPH MERKKRLFWS LQLLEQSYGR QTGILRTSTE
     IWRPPYFATD GDQDSHKATG PPPPPMPQDS VGCTNPHDTG IWNMSNQFGW VWSNVRGYVS
     DCARSKMKEP WRHESMYSMI LSDLTEVENR TPFCHRYDHV QFYERTGEEL SYELAYWVPW
     LKLQFMYHAI LTVLNHPFLY IMASRQNPNL AIPNSFWRRS SELVVLHATW IVRLIDMVVE
     KEVRLSDPFF AHVAAIAATV QLYYCCAGDP RLKYKSRVDY AKCREFLRTF ATTSRACEGL
     HRILDQMMRI ASGSENVDYE TWLPSKIYLS IPLMWDILQF NVTDRSAGGR ADGRLLHSSL
     AASAVGQGSE EDSTLEVIVT TSPEVTVNTA DGGQAVPLPL YRTPATSKAN AAATSITRDT
     LVAPIDSLMV NTPWLWADSA PLGDMESSLG YANSGPGGGD AEFSSWWNLG NL
//
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