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Database: UniProt
Entry: A0A0B1ZET1_9SPHN
LinkDB: A0A0B1ZET1_9SPHN
Original site: A0A0B1ZET1_9SPHN 
ID   A0A0B1ZET1_9SPHN        Unreviewed;       527 AA.
AC   A0A0B1ZET1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=LK12_22960 {ECO:0000313|EMBL:KHK89005.1};
OS   Novosphingobium malaysiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1348853 {ECO:0000313|EMBL:KHK89005.1, ECO:0000313|Proteomes:UP000031057};
RN   [1] {ECO:0000313|EMBL:KHK89005.1, ECO:0000313|Proteomes:UP000031057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 273 {ECO:0000313|EMBL:KHK89005.1,
RC   ECO:0000313|Proteomes:UP000031057};
RA   Lee L.-H.;
RT   "Genome sequence of Novosphingobium malaysiense MUSC 273(T).";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KHK89005.1}.
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DR   EMBL; JTDI01000011; KHK89005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1ZET1; -.
DR   STRING; 1348853.LK12_22960; -.
DR   Proteomes; UP000031057; 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; PS00624; GMC_OXRED_2; 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:UP000031057}.
FT   DOMAIN          87..110
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          249..263
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         97..100
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         214
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   527 AA;  56742 MW;  199D7CDE5D8EE6B1 CRC64;
     MEPPLTYGDF DYVVIGAGSA GCVVAARLSQ DPSVRVLLLE AGPEPRSPWI RIPGAVSKVI
     GPGKYNWGYT SDPEPHLGGR QIYWPRGRTL GGSGAINGMV YLRGHPRDFE AWKQAGNPGW
     GWDDVLPLFK KAEDAIGVSP AVTRYAFGDL FLAAAQDSGL PVRASLNTDG PAFEDGVGYL
     EFSIRHGLRR TSYDAYLAPI RKRRNLEILT SAMVQRIAMD EGRAKGVLFN RNGETCLAKA
     RREVVLCGGA VNSPQLLMLS GIGPAQHLQD HGIGVHADAA AVGQNLHDHT NTPLVFNSPR
     AQSINHRIVW PRLSLEVGRY FLRRTGILAV GTSAASAFAS SDGTSGYPDI QISVRPFSFV
     FTEKGLSVAK KPCVTVSVYQ MRPESRGRVL LKSSDPAQAP SILANYLQTP GDQERVLAGV
     RLAQRIMSQP RMKGFSPAVP IPEDDEALLE RVRGVLGPVF HPVGTCKMGS AQDSVVDPRL
     KVRGITGLRI ADASIMPEIV STNINAACIM IGEKAASMIA EDARSCS
//
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