ID A0A0Q4V192_9MICO Unreviewed; 694 AA.
AC A0A0Q4V192;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=ASF23_13060 {ECO:0000313|EMBL:KQO61399.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO61399.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO61399.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO61399.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO61399.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO61399.1,
RC ECO:0000313|Proteomes:UP000050821};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
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:KQO61399.1}.
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DR EMBL; LMMJ01000010; KQO61399.1; -; Genomic_DNA.
DR RefSeq; WP_055955188.1; NZ_LMMJ01000010.1.
DR AlphaFoldDB; A0A0Q4V192; -.
DR STRING; 1736311.ASF23_13060; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000050821; 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; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR11552:SF213; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000050821};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..694
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038706624"
FT DOMAIN 352..366
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 647..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 694 AA; 74030 MW; CD4E08206E3AD22A CRC64;
MSISRRSFIT GSAALTAAMA AAAAFAVSRP VPGTYGDAGP RRPVIDTDAL DTATEYDYVV
VGAGAGGVPM AVRLAEAGHS VLVLDAGPAT TDPDVYEVPA FHLFASSDPE MSWDFWVRHY
TDDRLHGSAF VRKRDGVLYP RASTLGGCTA HHALLMLAPE NDDWDRLGRI TGDPSWNALV
MAEYQARVRE WLPIETSPAA ILAEDPTLAR LVTAALVDAG QLAPPASAID LNRGTIAGTL
LDPNDPAAIE AYRQGVSLVP QSTRDGKRYG VRERLLEAAP GLQGRLAIQS DALVERIRFD
TGGPRPRAVG LEVVVAPHQY GASPVRRTLT AAARDAARRT VTARHEVIVS GGAFNTPQIM
MLSGVGPAAH LRAHGIDLVH DLPGVGGNLQ DRYEMTVVTE FDRPFSVLAG KTYGAEGDPG
MTEWRSGDPN ALYRSNGLLV GIKQTVAGGS EHPELFLFGA PSNFTGYRPG FAADGIRGGD
HFNWAVLRGY QKSMDGTVRL RSDDPTEPPA INFRYFDDGQ SSAGTALDLR AMRDGIERAR
SVNATARRLR FGDAATDHEI YPGPAVTSAD DIDAVIRRDA WGHHASCTMP MGADGDPRAV
LDARFRVRGI DGLRVVDASV FPEIPALFPL MTIFAMSERA AATILDDRAG GGAGGRTGGR
ADDRDVGART ALSGDLGHDH DLDLDHDLRT DGTR
//
