ID E1VIP9_9GAMM Unreviewed; 586 AA.
AC E1VIP9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:CBL44691.1};
GN ORFNames=HDN1F_11080 {ECO:0000313|EMBL:CBL44691.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL44691.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL44691.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
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}.
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DR EMBL; FP929140; CBL44691.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VIP9; -.
DR STRING; 83406.HDN1F_11080; -.
DR KEGG; gpb:HDN1F_11080; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_6; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000002677; Chromosome.
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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000002677}.
FT DOMAIN 244..258
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 547..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..579
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95..98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 586 AA; 64511 MW; 25491D70B23E340D CRC64;
MQAVEEFDFI VIGGGSAGCI AAARIADANL GSVLLVEAGD AAEENPETLL ASGFAQAFAN
ENTLIDRLSI QQPRCAKRTL YMGSGTGMGG SGAVNGMVYT RGDRRDYAQW PEGWRWENVA
PSFDALEHTL GVSTRNPNEF TNTCLDAALQ SGFERKDELN DGELCGHIGY QLMNYHGGDR
RHAYSAFIKG FPRENLTVLT RTRLERIEFD ENMTAIAVHV RQRSAMQEIV RRIGLRKEII
LCAGALETPK LLMLSGVGPS NQLRHFGIEP RAEVPAVGRN LQDHPNVCIF YRGNSETQSF
YPQVYGFERM NPALALADQQ ADTCFVFYSA ASSLAPSMQR MLPALMLPAS QYGNRRWHRW
IRNTVTLAFR LPFLQRFVNK VYGIVVILGK PSSRGEVTLA SADPAHAPRI NPGYFLNSDD
LDTLTNGVIK AQQIAGQPAL TRWGNQGLSL AARSTDREKI KQWIKQSAMT TFHYAGTCKM
GTHPSDPVDT QLRLKAARNV RIADASVIPE IPVAAINAPS MMIGWRVADF IIEEIERAQL
VPAPNIASAS DNLPAEAKPK NSRKAASKGR AKKTKQARSR RPVPTL
//
