ID V2G5M5_9BURK Unreviewed; 585 AA.
AC V2G5M5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:ESH88573.1};
GN ORFNames=B551_0223550 {ECO:0000313|EMBL:ESH88573.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESH88573.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESH88573.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) 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, 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:ESH88573.1}.
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DR EMBL; AMPR02000452; ESH88573.1; -; Genomic_DNA.
DR AlphaFoldDB; V2G5M5; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000053474; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000053474}.
FT DOMAIN 82..105
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 254..268
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 546..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 64508 MW; 7EA02DC002956069 CRC64;
MSQTVDYIVV GAGSAGCVLA NRLSEDGRHA VCLLEAGPPD RYPWIHIPIG YGKTMFHKEV
NWGFHTDPDP NMLNRRIYWP RGRTLGGSSA INGLIYVRGQ REDYDHWAAL GNRGWSWDDC
LPYFRKLENN DLGPGPTRGT DGPLNATSID RRHPLVDAFI EAGESLGLPR KADFNTGDQE
GVGYYQLTTR KGWRCSTAVA YLRPAQSRPN LRIETGAHTT AILFEGRRAV GVRYMQNGRQ
QVLRARREVL LCAGALQSPQ LLQLSGIGPS ALLREFGVPV VHALPGVGEN LQDHLQIRLI
YQVARPITTN DQLRSLFGKA RMGLEWLLWR QGPLAIGINQ GAMFCRVLPQ ESATPDTQFH
FATLSADMAG GQVHPFSGCT YSVCQLRPES RGTVRIRSTD PFTPPSMQPN YLSAELDRRS
AIASVRFARR VARTEPMRTL MQAEFRPGDA VQSDDEILHF CREYGATIFH PSGTAKMGPA
SDPLAVVDER LRVHGVAGLR VVDCSVMPTL VSGNTNVPVV MMAERAADFI REDARAETVS
EIVGAAAAGS ARVEREPEHQ AEGDTGRQAE AGTERQPERR ITEPV
//
