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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//