ID A0A0U2J748_9BACL Unreviewed; 570 AA.
AC A0A0U2J748;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:ALS75218.1};
GN ORFNames=AUC31_08290 {ECO:0000313|EMBL:ALS75218.1};
OS Planococcus rifietoensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS75218.1, ECO:0000313|Proteomes:UP000067683};
RN [1] {ECO:0000313|EMBL:ALS75218.1, ECO:0000313|Proteomes:UP000067683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:ALS75218.1,
RC ECO:0000313|Proteomes:UP000067683};
RA See-Too W.S.;
RT "Complete genome of Planococcus rifietoensis type strain M8.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013659; ALS75218.1; -; Genomic_DNA.
DR RefSeq; WP_058381925.1; NZ_CP013659.2.
DR AlphaFoldDB; A0A0U2J748; -.
DR STRING; 200991.AUC31_08290; -.
DR KEGG; prt:AUC31_08290; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000067683; 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; 3.50.50.60; 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:UP000067683}.
FT DOMAIN 218..329
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 428..555
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 570 AA; 62880 MW; E3549733EAE1349C CRC64;
MATTLDKVDV VTVGVGWTGG IIAAECAKEG LKVVGLERGQ ERSTEDYSMV HDEYRYAIRY
ELMQDLSKET ITFRNSRDQK ALPMRQLGSF LLGEGLGGAG THWNGQNWRF LPYDFEIKSM
TDAKYGENKL PAEYTLQDWG ITYDELEPYF DKFEKTAGIS GEDKNPFWGK RSSDYPTPPM
KKTPLLSKFE TATSNLGYTP FMMPSANLSE AYENPDGQQI AACQYCGFCE RFGCEYGAKT
SPEITVVPAA RATGNYDIRF NANVVEVMKE GDRVTGVRFI DTVTFEEFIQ PAEVVVLTSY
VMNNAKLLMV SEIGQMYDPE TGEGSLGKNY AYQILPGASG FFDDQMNVFM GAGALGMTID
DFNGDSFDHS DLDFVHGASI SMTQTGSRPI ASNPLPPDTP SWGADFKKAS IENYTRTLSV
GGQGASMPHR DNYLSLDETY KDVYGVPLLQ LTYNFTDQDR ALHKYLTERA VEIMEEMGAK
TVVGRAPISD YDIVPYQTTH NTGGTIMGGD PATSVVNNYL QHWDMENLFV VGAGNFAHNG
GYNPTGTVGA LAYRCAEGII KYSQDGGSLV
//
