ID A0A1S2VIK4_9BACT Unreviewed; 573 AA.
AC A0A1S2VIK4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:OIN58543.1};
GN ORFNames=BLX24_13285 {ECO:0000313|EMBL:OIN58543.1};
OS Arsenicibacter rosenii.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arsenicibacter.
OX NCBI_TaxID=1750698 {ECO:0000313|EMBL:OIN58543.1, ECO:0000313|Proteomes:UP000181790};
RN [1] {ECO:0000313|EMBL:OIN58543.1, ECO:0000313|Proteomes:UP000181790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:OIN58543.1,
RC ECO:0000313|Proteomes:UP000181790};
RA Huang K.;
RT "Arsenicibacter rosenii gen. nov., sp. nov., an efficient arsenic-
RT methylating bacterium isolated from an arsenic-contaminated paddy soil.";
RL Submitted (OCT-2016) 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 -!- 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:OIN58543.1}.
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DR EMBL; MORL01000006; OIN58543.1; -; Genomic_DNA.
DR RefSeq; WP_071503652.1; NZ_MORL01000006.1.
DR AlphaFoldDB; A0A1S2VIK4; -.
DR OrthoDB; 1154541at2; -.
DR Proteomes; UP000181790; 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; 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:UP000181790}.
FT DOMAIN 95..344
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 437..560
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 573 AA; 63952 MW; 287B3291008F05F5 CRC64;
MSNLNTTVNK THTYDAIVIG SGISGGWAAK ELCEKGLKTL VLERGRMVNH VEDYPTANLE
HWEFPHRGAL TDEDKQAYHV QTRSGFVNET NKHFFNNDLD APYTETKRFD WIRGNQVGGR
SLMWGKQCYR WSDLDFEANA KEGIAIDWPI RYKDIEPWYT YAEKFVGISG EKLGLSHLPD
GYFLPPMEMN CLEKHVRKQI ESKFKGRHMT VGRVAHLTEP QPWHLELGRA QCQYRNRCSR
GCPYGAYFSS NAATLPAANL TKNLTVRPGS AVHSIIFDEK TQRATGVRIV DTETKEMIEF
YAKIIFCNAS TLGTTSILLN STSTRFPNGM GNDSGELGHN LMDHHYRLGA MGAYDGFEDQ
YYKGRRPNGI FIPRFRNLDA ATRTDKFLRG YDYQGAAGRG NWGRGVNTEG VGGAFKDALL
DPGGWGMSLV GFGECLPYHE NHVTLNQDKK DKWGLPTLTI DAEFKDNEMK MREQIKADAV
EMLEAAGLKN VAPFDYSGGI GVGVHEMGTA RMGRDPKTSV LNGNNQIHAV PNVFVTDGAC
MTSSSCVNPS ITYMALTARA VDFAVNESKK GNI
//
