ID A0A0N1BZS9_9SPHN Unreviewed; 563 AA.
AC A0A0N1BZS9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:KPF90154.1};
GN ORFNames=IP83_00165 {ECO:0000313|EMBL:KPF90154.1};
OS Novosphingobium sp. AAP93.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF90154.1, ECO:0000313|Proteomes:UP000037906};
RN [1] {ECO:0000313|EMBL:KPF90154.1, ECO:0000313|Proteomes:UP000037906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP93 {ECO:0000313|EMBL:KPF90154.1,
RC ECO:0000313|Proteomes:UP000037906};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF90154.1}.
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DR EMBL; LJHZ01000001; KPF90154.1; -; Genomic_DNA.
DR RefSeq; WP_054120176.1; NZ_LJHZ01000001.1.
DR AlphaFoldDB; A0A0N1BZS9; -.
DR STRING; 1523427.IP83_00165; -.
DR PATRIC; fig|1523427.4.peg.35; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000037906; 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;
FT DOMAIN 74..314
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 427..550
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 563 AA; 61330 MW; FF7BAD1A634B3D2F CRC64;
MDDNLTFDAI VVGSGITGGW AAKELTEAGL KVLLLERGRK IEHQVDYETE LKAPWEMPFR
GEGDADLYAS EYAVQRLNRH FTEFTQNHFV NDAQNPYQTG EGTDFTWFRS YQLGGRSLTW
GRQSYRWSDY DFGANKRDGH GTDWPIRYAD LAPWYDKVEE FIGVSGAAEG LPQLPDGKFL
PPFALNVVEQ AAREKIMAAW PERRLTIGRT ANLTQEKDGR GPCQSRSICA RGCSYGAYFS
TQSSTLPAAQ ATGNLTLITD AAVEKIDYDP NTRRVTGVRW IDSKTKTRRQ ATARMVFLNA
GAFNSVHLLL NSASEAMPSG LANISGVLGT HIMDHANTLS AAAIMPGFEA WTTFGNRPTG
AIIPRYRNMD VMDGVGHTRG FSFQGGALQS TWTAGKREAG IGADYKARLR KPGPWRMVLV
AFADCVPRAS NRLTLDRTKF DANGIPQLHI DFAFGAEEHA ALAQAKADAT EMLTKAGGHV
IFGFDRPGAG GTAIHEMGGA RMGLDPATSV LNKWSQAHDV ANLFVTDGAQ MASSACQNPS
LTYMALTARA AAHAVSLLKS SAI
//
