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Database: UniProt
Entry: A0A1I0V662_9BACT
LinkDB: A0A1I0V662_9BACT
Original site: A0A1I0V662_9BACT 
ID   A0A1I0V662_9BACT        Unreviewed;       521 AA.
AC   A0A1I0V662;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:SFA71537.1};
GN   ORFNames=SAMN04489723_10120 {ECO:0000313|EMBL:SFA71537.1};
OS   Algoriphagus aquimarinus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=237018 {ECO:0000313|EMBL:SFA71537.1, ECO:0000313|Proteomes:UP000198790};
RN   [1] {ECO:0000313|EMBL:SFA71537.1, ECO:0000313|Proteomes:UP000198790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23399 {ECO:0000313|EMBL:SFA71537.1,
RC   ECO:0000313|Proteomes:UP000198790};
RA   de Groot N.N.;
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 FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR   EMBL; FOKK01000001; SFA71537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0V662; -.
DR   STRING; 237018.SAMN04489723_10120; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000198790; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198790}.
FT   DOMAIN          18..370
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          417..501
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   521 AA;  57517 MW;  9BE2BD6699035343 CRC64;
     MNREENISQL QNTSKIWDIA VIGGGSSGLG VALDAISRGL SVILFEKSDF AKGTSSRSTK
     LVHGGVRYLA QGDVGLVFEA LKERGKLLQN APHLAHDQPF IIPIFTAKDR IMYSVGLKIY
     DWMSGRLSLG KSEFISKEET LKRLPGLKSE GLYGGVVYHD GQFDDARLAL NLAQSADEAG
     TCVLNYVSVN NLVKNEAGKI TGLQVSDKLS RKKYEVNAKM VVNATGVFAD KILQMDNPEA
     PKMIQPSQGI HLVLDLDFLG GKDALMIPKT RDGRVLFAVP WHGKLVVGTT DTLREKPKLE
     PEALQKEIDF VLETAAGYLA RNPTRADVKS VFAGLRPLAR PKEGSTKTKE ISRSHKVILS
     ESGLVTLTGG KWTTFRKMGE DTVEYFTKVT GEKLKDSKSL DMKIHGATSR VPDGHWGIYG
     FDAQPIQDLT KENKEWGAQL HPDFPNIEAE VIWAVREEMA MKVEDALARR IRMLFLDAQA
     AIDTAPKVAA LMAKEMGKDE KWIESELAEF TKTASKYLIK K
//
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