ID   A0A093EXN3_TYTAL        Unreviewed;       595 AA.
AC   A0A093EXN3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=N341_09617 {ECO:0000313|EMBL:KFV46751.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV46751.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV46751.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV46751.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC         ChEBI:CHEBI:17499; EC=1.1.99.1;
CC         Evidence={ECO:0000256|RuleBase:RU003969};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC       route): step 1/1. {ECO:0000256|RuleBase:RU003969}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; KK377741; KFV46751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093EXN3; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000054190; Unassembled WGS sequence.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR011533; BetA.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   NCBIfam; TIGR01810; betA; 1.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054190}.
FT   DOMAIN          126..149
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          298..312
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         128
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         136..139
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         263
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   595 AA;  66724 MW;  8D8D5D120369AF12 CRC64;
     MHKVKGTLFK AHTLKNILGI NKQQFKISHT SSQLSSEKTN SYNYVIVGAG SAGCVLANRL
     TEDPRSTVLL LEAGPKDTLL GSKRLMWKIH MPAALTYNLC DEKFNWYYHT TSQKYMDNRI
     MYWPRGRVWG GSSSLNAMVY IRGHAEDYNR WSREGATGWD YEHCLPYFKK AQTHELGPDQ
     YRGGNGPLYV SRGKTNHPLH HAFLEATQQA GYPFTDDMNG YQQEGFGWMD MTVHQGQRWS
     TASAYLRPAI SRPNLSVAEK TLVTKILFQG TKSIGVEYVK NGQRKKAFAN NEVILSGGAI
     NSPQLLMLSG IGNADDLKKL GIPVVCHLPG VGQNLQDHLE VYVQQKCTKP ITLYNAQKPV
     NMVKIGLEWL WKFTGEGATA HLESGGFIRS EPGVPHPDIQ FHFLPSQVID HGRIPSTMEA
     YQVHVGPMRS TSVGWLKLKS TDPKDHPIIE PNYMSTERDI WEFRQCVKLT REIFAQKAFE
     KFRGPEIQPG NHVQSDKEID AFIRQKADSA YHPSCTCKMG QLSDSTAVVD PQTKVIGVEH
     LRVVDASIMP SVVSGNLNAP TIMIAEKAAD LIKGLPSLQE KNVPVYKPKT LETQR
//