ID G6EGQ7_9SPHN Unreviewed; 543 AA.
AC G6EGQ7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN ORFNames=NSU_3528 {ECO:0000313|EMBL:EHJ59500.1};
OS Novosphingobium pentaromativorans US6-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ59500.1, ECO:0000313|Proteomes:UP000004030};
RN [1] {ECO:0000313|EMBL:EHJ59500.1, ECO:0000313|Proteomes:UP000004030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US6-1 {ECO:0000313|EMBL:EHJ59500.1,
RC ECO:0000313|Proteomes:UP000004030};
RX PubMed=22275104; DOI=10.1128/JB.06476-11;
RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT pentaromativorans US6-1.";
RL J. Bacteriol. 194:907-907(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:EHJ59500.1}.
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DR EMBL; AGFM01000056; EHJ59500.1; -; Genomic_DNA.
DR RefSeq; WP_007014436.1; NZ_CP009292.1.
DR AlphaFoldDB; G6EGQ7; -.
DR KEGG; npn:JI59_21380; -.
DR PATRIC; fig|1088721.3.peg.3482; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000004030; 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 PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000004030}.
FT DOMAIN 89..112
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 99..102
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 543 AA; 59040 MW; 37619C84761DE2B9 CRC64;
MQRREEAQGE RYDYVVVGAG SAGCALAGRL AQDGRYRVLL LEAGPPNHFI WTRFALGCGK
TLNDPRVNWC LQSQPQESMG GRRLHIPAGK IVGGSSAING GVFMRGNPGD YDSWAQKGCF
GWSWADVLPV YRRMERYVGD EVDPEVRGGE GPLCVTQVPE RDPLISALIS SAGEAGLPVN
RDVNGRDQEG IWFGQATTRS GWRHSAADAY LRPQRRNSNL RVVTGALVDR VVVRDGRAEA
VVYSTRAGPA RAEASGEIIL CAGGLHSPAI LERSGIGDGR RLQSLDIPVV CDRPAVGENL
QDHWATWMKW RVHGHATLNE RTRGLRAVWE GLRFMATRRG ALSLPFGSAV AAWRSDPAVS
DCDVLFTANP FSYDNPETRK LNAFPGITIS TMLLRPHSRG NLHISASDPV RPPSVDFRGL
CDAHDVRVIA RGMKFLRQVM QGQTLSRYRP EELSPGPDVD SESGLEAFIR AAGNSCYHPS
GTCRMGSDEA AVVDPKLRVR GIAGLRVADN SIMPSIVSGN TNAVAIMIGE RASEFVLADV
PGR
//
