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Database: UniProt
Entry: A0A1M4UQF3_9GAMM
LinkDB: A0A1M4UQF3_9GAMM
Original site: A0A1M4UQF3_9GAMM 
ID   A0A1M4UQF3_9GAMM        Unreviewed;       542 AA.
AC   A0A1M4UQF3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SHE58877.1};
GN   ORFNames=SAMN02745148_00723 {ECO:0000313|EMBL:SHE58877.1};
OS   Halomonas ilicicola DSM 19980.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1121942 {ECO:0000313|EMBL:SHE58877.1, ECO:0000313|Proteomes:UP000184346};
RN   [1] {ECO:0000313|EMBL:SHE58877.1, ECO:0000313|Proteomes:UP000184346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19980 {ECO:0000313|EMBL:SHE58877.1,
RC   ECO:0000313|Proteomes:UP000184346};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; FQUJ01000003; SHE58877.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M4UQF3; -.
DR   STRING; 1121942.SAMN02745148_00723; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000184346; 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; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000184346}.
FT   DOMAIN          88..111
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          260..274
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         90
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   542 AA;  59785 MW;  7226CAA6E8BD97BD CRC64;
     MSMSAPRPSE YDYIIIGAGS AGCVLANRLS EDPGVEVLLL EAGGRDWNPW IHVPVGYFKT
     MHNPATDWCY LTEPDPGIAN RQLQWPRGKV LGGSSSLNGL LYIRGQKQDY DDWAGDGNTG
     WDYASVLPYF KKSECQSRGA DDYHGVDGPL HVSDLRLRRE IAERFIDAAK AIGIPGNSDV
     NGQDQEGVGY FQQTAFKGFR CSTAKAFLRP ARKRRNLTVM TRAQCKQLLL DGKHVHGVVF
     EHQKQEKTAR ARREVILSSG AIGSPQILQC SGIGEPEHLK SVGVECRHTL PGVGENLQDH
     LQVRLVFKTS CSTLNDEVRH PLKQFMVGTQ YVLTRTGPLT LAASQVYVFT QSREGLDRPD
     IQFHMQPLSA DKPAEGVHPF SAFTSSVCQL RPHSRGRVRI TSANPLDYPA IHPNYLSAEE
     DQRVVVDAIK VARRIAEAKP LEEVITEEYV PGEKFQTDEE LLDAARQYSQ TIYHPTSTCK
     MGSDSDPMAV VDARLRVHGL SGLRVVDASI MPSIVSGNTN APTIMIAEKA ADMIKEDHGG
     PS
//
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