ID A0A2N1CUE2_9ALTE Unreviewed; 556 AA.
AC A0A2N1CUE2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN Name=betA {ECO:0000313|EMBL:PKG92928.1};
GN ORFNames=CXF95_28550 {ECO:0000313|EMBL:PKG92928.1};
OS Paraglaciecola sp. MB-3u-78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=2058332 {ECO:0000313|EMBL:PKG92928.1, ECO:0000313|Proteomes:UP000233828};
RN [1] {ECO:0000313|EMBL:PKG92928.1, ECO:0000313|Proteomes:UP000233828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB-3u-78 {ECO:0000313|EMBL:PKG92928.1,
RC ECO:0000313|Proteomes:UP000233828};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) 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}.
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:PKG92928.1}.
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DR EMBL; PJCF01000087; PKG92928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1CUE2; -.
DR OrthoDB; 9785276at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000233828; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000233828}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 256..270
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 93..96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 556 AA; 60657 MW; CEEFB22C0D9C605C CRC64;
MTKTTYDYII VGAGSAGCVL ANRLSQDPSN SVLLLETGGS DKSIFIKMPT ALSIPMNSDK
YAWQFHTESE PYLDNRKMHC PRGKVLGGSS SINGMVYVRG HAKDFDQWQQ HGAKGWDYQS
CLPYFQKAEK FYLGKDSYRG DKGPLGVNNG NEMANPLYKV FIKAGQQAGY AATDDYNAGQ
QEGFGPMHMT VKDGVRSSAS REYLDPVKSR SNLTIVTGAL AEKVLLEGKK AVGVEYSVNG
SKVTVKASKE VVLSAGSIGS PHLLQLSGIG DSDTLKAAGV EVKHHLPGVG QNLQDHLEFY
FQYKCKQPIT LNGKLGLISK GLIGARWLFS RSGLGATNHF ESCAFIRSKP GIEWPDIQYH
FLPAAMRYDG KSAFAGHGFQ VHVGHNKPKS RGAVTIKSAD PTVAPKIQFN YLQHQDDIEG
FRACVRLTRE IIEQSAFDEY RDDEIQPGKA IQTDEQIDAF VRQTVESAYH PSCSCKMGED
DMAVVDSNTQ VRGISGLRVV DSSIFPTIPN GNLNAPTIMV AEKAADLILG KPPLSKSQAS
VAVANDWQTV QRSSTI
//
