ID H0QWQ8_9ACTN Unreviewed; 506 AA.
AC H0QWQ8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:GAB17259.1};
GN ORFNames=GOEFS_022_00400 {ECO:0000313|EMBL:GAB17259.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB17259.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB17259.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB17259.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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:GAB17259.1}.
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DR EMBL; BAEH01000022; GAB17259.1; -; Genomic_DNA.
DR RefSeq; WP_007316597.1; NZ_BAEH01000022.1.
DR AlphaFoldDB; H0QWQ8; -.
DR STRING; 1077974.GOEFS_022_00400; -.
DR eggNOG; COG0578; Bacteria.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000035034; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 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.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000035034}.
FT DOMAIN 24..348
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..503
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 506 AA; 52489 MW; B62D90D18EE2D6C6 CRC64;
MSALTAQRRR ADLQTLADRR EPLDVLVIGG GVTGCGAALD AASRGLSVAL VEAHDLAFGT
SRWSSKLVHG GLRYLASASV GIAYESAIER HHLMTTIAPH LVSPLRQVVP DFGERRTKQL
VWTGFRAGDA LRRVARTPKS VLPGPGNLSV EEMATVTPTV ARAGLRGGVG TYDGQLIDDA
RLVVGIARTA AAFGAHICTY TKASKVSGAG ATLTDSLTGE SFDISARSVI NATGVWAGDV
DSTLTIRPSR GTHLVFDAAA FGNPTAALTV PVAGSISRFV FAMPEQLGRV YLGLTDVDAP
GAIPDVPDAD DEEIDFLLDT VNVALRQPLT RSDIRGTYSG LRPLIDGAGG DGGSLADVSR
KHAVRVNDST LVSIVGGKLT TYRRMAQDAV DAAVKAAGLQ SGSCITTSTP LIGATGGAVR
RGLPASLVAR FGTESARVLD SASIPDATAS IANGIDVTRA EVEYAVTHEG ALSADDVIER
RTRIGLVPDD AARVRQAVED VVAAAS
//
