ID A0A1H6VEM8_9DEIO Unreviewed; 524 AA.
AC A0A1H6VEM8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:SEJ02276.1};
GN ORFNames=SAMN04488058_103122 {ECO:0000313|EMBL:SEJ02276.1};
OS Deinococcus reticulitermitis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=856736 {ECO:0000313|EMBL:SEJ02276.1, ECO:0000313|Proteomes:UP000199223};
RN [1] {ECO:0000313|Proteomes:UP000199223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10218 {ECO:0000313|Proteomes:UP000199223};
RA Varghese N., Submissions S.;
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; FNZA01000003; SEJ02276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6VEM8; -.
DR STRING; 856736.SAMN04488058_103122; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000199223; 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}.
FT DOMAIN 25..383
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..505
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 524 AA; 57247 MW; B3CA1DF1C4888944 CRC64;
MTELLPPSDP RPAQLQAATA DHVWDLIVIG GGASGLGTAV EAATRGHRTL LLEGHDYAKG
TSSRSTKLVH GGVRYLAQGN VSLVREALRE RGLLRKNAPH LVRDLAFVVP AYDWWAGPFY
GIGLKLYDVL AGKLNLGSSK HLGRDAALER TPTLQKEGLM GGILYFDGQF DDARLAITLL
RTFEDFGGAA LNYAPVVGLL KDGEKVAGVR WRDEETGTLH EARGKVVVNA TGVWVDDIRR
METPDAKPML SPSQGVHIVV NKRFLPGQSA IMIPRTDDGR VLFAVPWHDH VVIGTTDTPV
PDTHFEPRAL EEEVEFILKT AGRYLDPAPT RADVLSVYAG LRPLVKGENT DGAGSTAALS
RDHVIRISDG GLITLTGGKW TTYRRMGEDT VNRAEVLGGL PERLTTTPGL HLHGWSEDDR
PDHWKVYGSE AEALQALPGA DRFLHRELPY TEAELRWGVR FESARTVEDL LSRRTRALLL
GAEASAEAAP RAAAILAEEL GRDQAWQDAQ VTTYRALAKG YRLS
//
