ID Q53W23_THET8 Unreviewed; 510 AA.
AC Q53W23;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Glycerol-3-phohsphate dehydrogenase {ECO:0000313|EMBL:BAD71939.1};
GN OrderedLocusNames=TTHB143 {ECO:0000313|EMBL:BAD71939.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27 {ECO:0000313|EMBL:BAD71939.1,
OG ECO:0000313|Proteomes:UP000000532}.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD71939.1, ECO:0000313|Proteomes:UP000000532};
RN [1] {ECO:0000313|EMBL:BAD71939.1, ECO:0000313|Proteomes:UP000000532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RC PLASMID=pTT27 {ECO:0000313|EMBL:BAD71939.1,
RC ECO:0000313|Proteomes:UP000000532};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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; AP008227; BAD71939.1; -; Genomic_DNA.
DR RefSeq; WP_011229156.1; NC_006462.1.
DR RefSeq; YP_145382.1; NC_006462.1.
DR AlphaFoldDB; Q53W23; -.
DR EnsemblBacteria; BAD71939; BAD71939; BAD71939.
DR GeneID; 3168413; -.
DR KEGG; ttj:TTHB143; -.
DR PATRIC; fig|300852.9.peg.2089; -.
DR HOGENOM; CLU_015740_4_1_0; -.
DR PhylomeDB; Q53W23; -.
DR Proteomes; UP000000532; Plasmid pTT27.
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};
KW Plasmid {ECO:0000313|EMBL:BAD71939.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000532}.
FT DOMAIN 15..360
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 357..494
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 510 AA; 55996 MW; 0991DC9D29F7787A CRC64;
MDREALLERL KEPFDLLVLG GGATGAGVLW EATLRGLKAA LVEAGDFASG TSSRSTKLLH
GGVRYLELAF KRLDRRQLKL VVDALHERKV VMDLAPHLAK PLTLVTPLFR PLEIPYYTLG
LKLYDLLAGK RRLAPSRYLP PEEVARLFPD LPKTLGGVAY QDGQFADFRL NLALVLSALE
RGAVALNHAE ATALLLEGGR VRGAVVRDGL SGKEVEVRAK AVVNATGSLA DRVRRLLDPH
LPPLLTASSG VHLVLDYPLE AGLLVPKTRD GRVLFLLPYR GMALLGTTDL PAEPASCPLP
REEEVAYLLE EIRPYLGDVS GRVRAVWSGL RPLVGKGETK LLVRDHYIEE RRGLYTLVGG
KWTTFRLMAL DLVERLAKDL GLALPPSKSH ATPLLGAGPR PPLPLPEEAA RRLWETYGTL
APEVLALGDR PLLPGLPYLE GEVVWAVRRE LARKPLDVLA RRMGLAFLDQ EKTREALPKV
VELMAGLLGW DERERALRLK EAEEGLPGLC
//
