ID   A0A1T1HT98_9PSED        Unreviewed;       551 AA.
AC   A0A1T1HT98;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:OOV92957.1};
GN   ORFNames=MF4836_22940 {ECO:0000313|EMBL:OOV92957.1};
OS   Pseudomonas sp. MF4836.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1960827 {ECO:0000313|EMBL:OOV92957.1, ECO:0000313|Proteomes:UP000190183};
RN   [1] {ECO:0000313|Proteomes:UP000190183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF4836 {ECO:0000313|Proteomes:UP000190183};
RA   Fagerlund A.;
RT   "Genome sequencing of bacteria from food industry.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:OOV92957.1}.
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DR   EMBL; MVOL01000010; OOV92957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1HT98; -.
DR   STRING; 1960827.MF4836_22940; -.
DR   Proteomes; UP000190183; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          15..49
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          247..333
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          421..540
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   551 AA;  60403 MW;  3A46D96FD79CCB9C CRC64;
     MNSPIKKTNG DIEADVVIVG SGVVGAMIAD QLARQGHSVL ILEAGPIIER AQVVENFRNL
     PFDHRLIDKP DYQTIYPQTP YALAPLYFPD NNYISLSGPD SNSFKQYYLR AVGGTTWHWA
     GSNWRHLPVD FVLNSTYGVG RDWPISYDEL EPYYCRAEEE MGISGPHDPA LQSPSQRSRP
     YLFDMIPRGY ADNYVASVVN PHGYHFVPVP QARSVTPWEG RPACCGSNNC QPICPIGAMY
     AGIQHVQKAE RNGALVLAES VAYKIDTDQN NKVTAVHWYD AKRQSHRASG TVFVLACNAI
     ETPRLLLQAA NPANPNGIAN SSDQVGRNMM DHTGFYCSFL ADKPIWGGRG PQQNSSMVGM
     RDSPTRADHS SFSFIFDNRS RVPNATQQAL DMGLVGVELD EEIRRRVAFG IYITVMMEPL
     PDANNRLTLS NTRFDGLGLA CPDIHYDTGD YVRRGAVAAR ERLRHLSGLF NGVEFHTSPF
     NGNNHLMGST IMGDDPKTSV VDGDCRAHDH ANLWLPGGSA MPSGSVVNST LTMVALGLKA
     ADSISSSLAG N
//