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
//