ID A0A0Q6Q1Y2_9MICO Unreviewed; 545 AA.
AC A0A0Q6Q1Y2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KQV07360.1};
GN ORFNames=ASC63_08680 {ECO:0000313|EMBL:KQV07360.1};
OS Leifsonia sp. Root112D2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV07360.1, ECO:0000313|Proteomes:UP000051914};
RN [1] {ECO:0000313|EMBL:KQV07360.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV07360.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV07360.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV07360.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQV07360.1}.
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DR EMBL; LMCU01000001; KQV07360.1; -; Genomic_DNA.
DR RefSeq; WP_055812017.1; NZ_LMCU01000001.1.
DR AlphaFoldDB; A0A0Q6Q1Y2; -.
DR STRING; 1736426.ASC63_08680; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000051914; 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:UP000051914}.
FT DOMAIN 110..309
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 418..534
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 545 AA; 59911 MW; A74BEDEFABC12DE7 CRC64;
MTSSVRERNE SAWLLPADQR RTNEALREGM RRFDDADEVD IVIVGCGAGG STFMQRLARS
GRTVVGLDAG PFWDPEEDWV SDEAGSHGLY WTEPRVITGD NPVPLGSNNS GRGVGGSMVH
YAGYVPRFHP SDFETYTRDG VGADWPIDYA DLARYYEDIE GELPVAGEDW PWGDPHSYPH
RPHPVGGNGE LFLRGALAAG ITAKVGPVAI TNGRFGNRAH CIYRGFCLQG CKVNAKASPL
ITHIPDALAH GAEIRPDSMV TRVAIDERTG RATGVHYMRD GVEHFQRARM VAVAGYSIET
PRLLLNSTSK RFANGLCNDF DQVGRYLMVQ GAPQTGGRFD DEVRMYKSPP PEVSSEQFYE
TDPSNPYKRG FSIQTVSPLP ITWAEHVAAQ GHWGRELRER MSDYVHWACL GALCEFLPQA
DNRVTLADET DARGMPVARF SYSQCDNDRQ QMKAAQEVME RILKAAGADE VITIQRYAHL
VGGARMARNE QDGVVDADCR TFAVPNLLIV DGSVLPTQGS ANPALTIMAV AARAADRLIN
SAIER
//
