ID A0A1J0LTM0_THEBO Unreviewed; 511 AA.
AC A0A1J0LTM0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Putative glycerol-3-phohsphate dehydrogenase {ECO:0000313|EMBL:APD09686.1};
GN ORFNames=A0O31_01577 {ECO:0000313|EMBL:APD09686.1};
OS Thermus brockianus.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=56956 {ECO:0000313|EMBL:APD09686.1, ECO:0000313|Proteomes:UP000182993};
RN [1] {ECO:0000313|Proteomes:UP000182993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE-1 {ECO:0000313|Proteomes:UP000182993};
RA Schaefers C., Blank S., Wiebusch S., Elleuche S., Antranikian G.;
RT "Whole genome sequencing of Thermus brockianus strain GE-1.";
RL Submitted (JUN-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; CP016312; APD09686.1; -; Genomic_DNA.
DR RefSeq; WP_071677351.1; NZ_CP016312.1.
DR AlphaFoldDB; A0A1J0LTM0; -.
DR STRING; 56956.A0O31_01577; -.
DR KEGG; tbc:A0O31_01577; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000182993; Chromosome.
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: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 16..375
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 358..495
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 511 AA; 56292 MW; DC4BF1B322897C2D CRC64;
MADREALWER LKEPWDLLVL GGGATGAGVL WEATLRGLKA ALVEARDFAS GTSSRSTKLL
HGGVRYLELA LRRLDRRQLR LVMDALRERK VVMDLAPHLA YPLPLLTPLF RPLELPYYGT
GLLLYDLLSG QRRLGPTRYL PPRGVAELFP DLPPTLGGIL YWDGQFQDHR LVLALLLSAL
RRGALALNHA EAHAFLLKGG RVVGAVVRDH LTGREVEVHA KAVVNATGPF TDATRRLLDP
HLPPLLTPSS GAHLVLDYPL RTGLLLPRTR DGRVLFLLPY RGKALLGTTD RPAEASFCPL
PKEEEVAYLL EEVRPYLGDL SPHIRAVWSG LRPLVGRGET RLLVRDHLIA EERGLYTLTG
GKWTTFRLMA QDLVDRLDRD LGLGLPPSPS HATPLLGAGP KPPLDLPEGV AEHLYRTYGR
EAQAVAALGD RPLLPGRPYL EGEVVYAVRE ELAQKPLDVL ARRMGLALLD QEAAREALPR
VVALMAPLLG WDEGRARAEL EEARAALPGL C
//