ID A0A120AGQ2_9GAMM Unreviewed; 656 AA.
AC A0A120AGQ2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glucose-methanol-choline (GMC) oxidoreductase:NAD binding site {ECO:0000313|EMBL:KWS04938.1};
GN ORFNames=AZ78_2488 {ECO:0000313|EMBL:KWS04938.1};
OS Lysobacter capsici AZ78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS04938.1, ECO:0000313|Proteomes:UP000023435};
RN [1] {ECO:0000313|EMBL:KWS04938.1, ECO:0000313|Proteomes:UP000023435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ78 {ECO:0000313|EMBL:KWS04938.1,
RC ECO:0000313|Proteomes:UP000023435};
RX PubMed=24762937;
RA Puopolo G., Sonego P., Engelen K., Pertot I.;
RT "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT to Plant-Pathogenic Oomycetes.";
RL Genome Announc. 2:0-0(2014).
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}.
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:KWS04938.1}.
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DR EMBL; JAJA02000001; KWS04938.1; -; Genomic_DNA.
DR RefSeq; WP_036108290.1; NZ_JAJA02000001.1.
DR AlphaFoldDB; A0A120AGQ2; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000023435; 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; 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;
FT DOMAIN 261..382
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 504..646
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 61..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 71426 MW; 6CE70A6797D42806 CRC64;
MSITIPAGGF DVVIVGSGIS GSIIAYQLGK AGKQVLILEG GPPVPKSRED YMQTFFTANA
KTPESPYPPT MQGAGSKDNS LGQPDPATLN TPRYTVLQIK SWQNPAQCYF EYEEQQATHA
DDPKMTFAFG SSYERVAGGT TWHWLGTSLN HLPNDFQLKT KYGQGVDWPG GVKFYEALLP
YYRKATETIG VSSDKQPMVD LYKTFNVQPD GTYGPNYDFP MPGIVPSMND VLYADNVKSL
KIDDIGLFVT PTPQGRNSQP GKRRQCAGNT NCIPICPIQA KYDGTVTLAE ALQTGNVQIQ
YKTVASNISL KGDQVSGIDY LTYDSQTGKS TGKDTAVGKR YVLAAHAIET PKLLLMSKGN
PGYPNGVANR SDQVGRNLMD HVMYLAWGLA KDPIYAFRGP LSTSGIESVR DGAFRGQRAA
YRIEIGNEGW NWATNDPYTT LADFVFGQNN TQLNGDSVNQ QGQSLRFDPN LPAFSQLYGS
QLVKTLNAVY TRQLRLGYLI EQLPNPDNRV ELSDKHVDHL GLPRPKVTYR IRENYVRNGF
VSAKAASTAI FKALGATEYT KVPDAPVLSG PSSSPTTFQY LGDTFTFYGA GHIIGTYRMG
DSAATSVLNA RQQSWDHSNL YMVGSGVFPT TATANPTLTI AALALQAADN ILADLG
//
