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Database: UniProt
Entry: A0A494WFT2_9SPHN
LinkDB: A0A494WFT2_9SPHN
Original site: A0A494WFT2_9SPHN 
ID   A0A494WFT2_9SPHN        Unreviewed;       560 AA.
AC   A0A494WFT2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:BBD99509.1};
GN   ORFNames=SAMIE_1030100 {ECO:0000313|EMBL:BBD99509.1};
OS   Sphingobium amiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=135719 {ECO:0000313|EMBL:BBD99509.1, ECO:0000313|Proteomes:UP000279959};
RN   [1] {ECO:0000313|EMBL:BBD99509.1, ECO:0000313|Proteomes:UP000279959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16289 {ECO:0000313|EMBL:BBD99509.1,
RC   ECO:0000313|Proteomes:UP000279959};
RA   Ootsuka M., Nishizawa T., Ohta H.;
RT   "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT   Sphingobium amiense DSM 16289T.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AP018664; BBD99509.1; -; Genomic_DNA.
DR   RefSeq; WP_066700689.1; NZ_AP018664.1.
DR   AlphaFoldDB; A0A494WFT2; -.
DR   KEGG; sami:SAMIE_1030100; -.
DR   Proteomes; UP000279959; Chromosome.
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   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:UP000279959}.
FT   DOMAIN          107..310
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          424..547
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   560 AA;  61605 MW;  3CB75B631BFAC377 CRC64;
     MSMDFDAIVV GSGITGGWAA KELTEKGLKV LMIERGRMIE HGTDYVTETK APWEMEFRGE
     GDAELYAREY PVQRLNRHFT EFTQNHFVND KDNPYAVAEG TQFNWWRSYQ MGGRSLTWGR
     QSYRWSDYDF GANKADGYGT DWPIRYADVA PWYDHVEDFI GVSGAAEGLP SLPDGKFLPP
     MALNVVEQHV RKAIAQKWPD RCLTVGRTAN LTAPKEGRAP CQYRSICARG CSYGAYFSTQ
     SSTLPAAQKT GRLTVITDSL VEAVDYDPVS KKASGVRVLN VKTGARTRYG ARIVFLNAGA
     FNSVHILLRS RSESFQNGLA NSSGVLGTHI MDHASTLSTM AIMPGFDDRT TFGNRPTGVV
     IPRFRNLDRK DGDFTRGYSF QGGALQSGWT AAKRSAGIGK DFKEQTHKVG PWRMVFVGFA
     ESLPRVTNRL TLDPSKLDPQ GLPMLNIHFE HGDNERRALT DAKKEAAAMM EAAGGHVIMG
     FDEPGIGGSA IHEMGGARMG HDPQSSVLNR WSQAHDVPNL FVTDGAQMSS SACQNPSLTY
     MALTARACDH AVSLMKEGAL
//
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