ID A0A127VJV9_9SPHI Unreviewed; 566 AA.
AC A0A127VJV9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:AMQ01616.1};
GN ORFNames=AY601_4788 {ECO:0000313|EMBL:AMQ01616.1};
OS Pedobacter cryoconitis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMQ01616.1, ECO:0000313|Proteomes:UP000071561};
RN [1] {ECO:0000313|EMBL:AMQ01616.1, ECO:0000313|Proteomes:UP000071561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMQ01616.1,
RC ECO:0000313|Proteomes:UP000071561};
RA Lee J., Kim O.-S.;
RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014504; AMQ01616.1; -; Genomic_DNA.
DR RefSeq; WP_068406080.1; NZ_CP014504.1.
DR AlphaFoldDB; A0A127VJV9; -.
DR KEGG; pcm:AY601_4788; -.
DR PATRIC; fig|188932.3.peg.4964; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000071561; 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; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 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:UP000071561}.
FT DOMAIN 104..339
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 430..553
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 566 AA; 63579 MW; F4FDB8DFD1B27A5D CRC64;
MNLNTKATAQ NTYDAIVVGS GISGGWAAKE LTEKGLKVLL LERGRNIEHI KDYTTAMKKP
WEFEHRGKLT EVQKDAHPVQ KRDYPYQEFN ESFWVNDHEC PYTEVKRFDW YRGFHVGGKS
LMWGRQSYRF SDLNFEDNKK DGHGNDWPIR YKDLSPWYDH VEKFAGISGQ VENWPALPDG
HFLPPMEMNC VEKDVKKRIE DKWKKSRIMT IGRTANLTVP HGGRGSCQYR DRCSRGCPFG
AYFSTQSSTL PAAVATGNLT LRPFSLVDHI VYDKETQKAT GVVIIDSETK ENIEYFAKIV
FVNGSTLGST FLLLNSTSAE HPNGLGNASG ELGHNLMDHH FRCGASGDAE GFDDKYTYGR
RANGIYVPRY QNMGGDKRDY LRGFGYQGGA SRTGWHKDVA ELAFGGDFKD LMTQPGAWKM
GLGGFGESLP YHENRVYIDK TKKDKWGMPV LAIDCEFKGN EEKMRIDMMN DAAEMLEAAG
IKNIQTYDAG STPGMAIHEQ GTARMGNDPK TSVLNKWNQM HEVKNVFVTD GSCMPSIACQ
NPSLTFMALT ARAADFAVSE LKKGNL
//
