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Database: UniProt
Entry: A0A1G8MVI0_9BACI
LinkDB: A0A1G8MVI0_9BACI
Original site: A0A1G8MVI0_9BACI 
ID   A0A1G8MVI0_9BACI        Unreviewed;       586 AA.
AC   A0A1G8MVI0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Gluconate 2-dehydrogenase alpha chain {ECO:0000313|EMBL:SDI71914.1};
GN   ORFNames=SAMN04488123_10551 {ECO:0000313|EMBL:SDI71914.1};
OS   Natribacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Natribacillus.
OX   NCBI_TaxID=549003 {ECO:0000313|EMBL:SDI71914.1, ECO:0000313|Proteomes:UP000198853};
RN   [1] {ECO:0000313|EMBL:SDI71914.1, ECO:0000313|Proteomes:UP000198853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21771 {ECO:0000313|EMBL:SDI71914.1,
RC   ECO:0000313|Proteomes:UP000198853};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; FNEN01000005; SDI71914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8MVI0; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000198853; 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; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 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:UP000198853}.
FT   DOMAIN          210..330
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          435..557
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   586 AA;  65332 MW;  5E27AA0C279CF386 CRC64;
     MPTQLDKVEV LVVGSGWAGG IVCAEMAKAG HEVVCLERGE EKTIDDYIHV KDELRFSTRY
     EMMQNLSKET ITSRHKRDIT ALPVRTQSDM IAGNDEGGGS VHWAGATFPF LPYDFEIYSR
     TVERYGSDKI PEGMTIQDWG ITYDEFEEYY AQFELTAGIS GEPNPIGPER SIDYPNPPMV
     ETPNIALFKE AAANLGYHPY AQPSANITEV YENPDGQTIA QCQYCAFCDS YGCDYGAKAD
     PIVTVLPTAR ETGNFELRAK ANVRRVTYDG DQATGVVYVD TASGIEYEQP ADVVVLAGFT
     FTNTRLLLLS DIGTPYNPDT QEGVIGKNFT GQFSNNFLGA RAFFNEKKFN LYMGAGGLGV
     TFDDFSGDNI DHTDLDFIHG GHVEYRQYGD RPIESNSVPD GTPSWGREFK EKSLFYANRN
     MYLRFQHATL PWYHNYLDLD PTYTDPYGDP LLRVTNEYTE QDRNLQLYGI DVCREVAEEM
     GADIIDTDDV PEEFNNAYVG AHYAGGVIMG DDPETSAVNN YLQMWDAENL FVVGASAFPH
     FPNYHPTKTV GALAYRAADG IEQYLDNGGG LLVKGNTEKS QQQRKV
//
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