ID A0A0R2WZ35_9FLAO Unreviewed; 520 AA.
AC A0A0R2WZ35;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KRP29176.1};
GN ORFNames=ABS28_03080 {ECO:0000313|EMBL:KRP29176.1};
OS Cryomorphaceae bacterium BACL22 MAG-120619-bin32.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655630 {ECO:0000313|EMBL:KRP29176.1, ECO:0000313|Proteomes:UP000052139};
RN [1] {ECO:0000313|EMBL:KRP29176.1, ECO:0000313|Proteomes:UP000052139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL3 MAG-120619-bin32 {ECO:0000313|EMBL:KRP29176.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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 FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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:KRP29176.1}.
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DR EMBL; LIDG01000069; KRP29176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2WZ35; -.
DR Proteomes; UP000052139; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 18..340
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 367..501
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 520 AA; 58162 MW; 1E7C21DB64E04B56 CRC64;
MFKRETLVKQ IEENSEWDVI VIGGGATGLG VALDSVTRGY KTLLLEQVDF SKGTSSKSTK
LLHGGVRYLA QGNIDLVKEA LYERGLLLKN ASHLVSIQSF IIPNYRWWDN FFYAFGLKVY
DLLAGKLSFG KSIRINKKDT ISRLKTIKKQ HLKGGVVYHD GQFDDARLAI NIAQTSIEYG
AVILNHFKVK QLLKNNDGIV NGVVANDSET NMSYNLKAKV IINATGIFTD KIMQMDNVEA
KNTVRPSQGI HLVLDKSFLP GNDAIMIPKT NDGRVLFLVP WHNRVIVGTT DTLLNSYSLE
PTALDEEVNF IISTANKYLN KKVCKEDVLS IYAGLRPLAA SKENSKKSKE ISRSHKIIVS
NSELITITGG KWTTFRRMAE DTINKAISIG KLPNVSCKTT VLQIHGSKES LHNTHHLNIY
GSDQDSIQKL IIETPELGEK LHFLLPYTKA EIIWGIRKEM ARTVDDILAR RVRALFLDAK
AAIEVAPLVA SMLAKELGKD KLWQQQQIKE FTAIASHYIL
//
