ID A0A149VEJ4_9PROT Unreviewed; 545 AA.
AC A0A149VEJ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KXV78574.1};
GN ORFNames=AD928_09510 {ECO:0000313|EMBL:KXU93054.1}, AD954_02225
GN {ECO:0000313|EMBL:KXV78574.1};
OS Acetobacter cerevisiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=178900 {ECO:0000313|EMBL:KXV78574.1, ECO:0000313|Proteomes:UP000075462};
RN [1] {ECO:0000313|Proteomes:UP000075462, ECO:0000313|Proteomes:UP000075473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 1545 {ECO:0000313|EMBL:KXV78574.1,
RC ECO:0000313|Proteomes:UP000075462}, and LMG 1625
RC {ECO:0000313|EMBL:KXU93054.1, ECO:0000313|Proteomes:UP000075473};
RA Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT "Improved classification and identification of acetic acid bacteria using
RT matrix-assisted laser desorption/ionization time-of-flight mass
RT spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT respectively.";
RL Submitted (JUN-2015) 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:KXV78574.1}.
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DR EMBL; LHZA01000150; KXU93054.1; -; Genomic_DNA.
DR EMBL; LIAA01000009; KXV78574.1; -; Genomic_DNA.
DR RefSeq; WP_062250105.1; NZ_LIAA01000009.1.
DR AlphaFoldDB; A0A149VEJ4; -.
DR PATRIC; fig|178900.5.peg.671; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000075462; Unassembled WGS sequence.
DR Proteomes; UP000075473; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000075473}.
FT DOMAIN 10..43
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 240..325
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 414..533
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 545 AA; 60900 MW; D427DE837534A75D CRC64;
MPSEQTLSAD VVIVGSGVAG SSIANELARA GISVIVLEAG PRVDRQHFVE NFRNLENKPS
YQGPFPAVPW ARHPPNQITP NDYLHTSGPN AEAYQQVYLR MMGGTTWHWA GCAWRYLPSD
FELKTRYGQG RDWALKYEDL EPFYYQAEVM MGVCGPDPAK EDLGSPRKQP YPMEALPISY
AAQQFRKLID EKTPWRVVHE PQARNTRPYD SRPTCEGHNN CMPICPIGAM YNGSYSVYHA
EAAGAKFIPN AVVYKIERDS ANKRVTGVQY YDPDKNSHRV TGKYFVIAAH CIETAKLLLV
SADEQSPDGV ANSSGHVGRN MMDHTGVQVT FISGDKALWP GRGPLETNVI DNFRDGDWRN
ERGAYLVHMV DDNQVDFATQ MAISKGYVGR ELEEQIRYLS SHTVRLFSHN EALPDPDNRL
TLSKTNKDIL GIPHPDVYYK LPEYTVKSCE HTRKVFKELI GLMHGTDEEW TPGYFPQDHP
SGSTIMGTDP KDSVVDGHCR THDHENLFIA SSSVFSTVGT GNITLTVAAL ALRVADTLKK
ELLHG
//
