ID A0A1V2RHX6_9ACTN Unreviewed; 563 AA.
AC A0A1V2RHX6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=STBA_27390 {ECO:0000313|EMBL:ONK12003.1};
OS Streptomyces sp. MP131-18.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK12003.1, ECO:0000313|Proteomes:UP000189065};
RN [1] {ECO:0000313|EMBL:ONK12003.1, ECO:0000313|Proteomes:UP000189065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP131-18 {ECO:0000313|EMBL:ONK12003.1,
RC ECO:0000313|Proteomes:UP000189065};
RA Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT "New natural products identified by combined genomics-metabolomics
RT profiling of marine Streptomyces sp. MP131-18.";
RL Submitted (JUN-2016) 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:ONK12003.1}.
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DR EMBL; LZNS01000001; ONK12003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2RHX6; -.
DR STRING; 1857892.STBA_27390; -.
DR Proteomes; UP000189065; 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: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: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.
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:UP000189065}.
FT DOMAIN 19..372
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 399..523
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 530..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 61542 MW; FE1006814E2D2255 CRC64;
MGPEQRAEAL ARMAERELDV LVIGGGVVGA GTALDAVTRG LATGLVEARD WASGTSSRSS
KLIHGGLRYL EMLDFGLVRE ALKERGLLLS RIAPHLVRPV PFLYPLRHRG WERLYAGSGV
ALYDAMSMSS GHGRGLPRHR HLSRHRALRV APCLKKEALV GALQYYDAQV DDARYVAALV
RTAAGYGAHV ANRARVAEFL REGERVVGVR VRDLEQDGTY EVRAKQVVNA TGVWTDDTQS
MIAERGQFHV TASKGIHLVV PKDRIHSSTG LILRTETSVL FVIPWGRHWI VGTTDTAWDL
DKAHPAASSA DIDYLLDHVN SVLAVPLSRD DVEGVYAGLR PLLAGESDAT SKLSREHTVA
HPVPGLVVVA GGKYTTYRVM AKDAVDAAVH GLDQRVAACC TEEVRLAGAE GFHALWNARA
RLAARAGLHE ARVEHLLHRY GSLTEELLDL VAADPALGEP LPAADDYLKA EIVYACSHEG
ARHLEDVLTR RTRISIETFD RGTRSARECA RLMAGVLGWT PEQVEREVEH YEKRVEAERE
SQLQPDDQTA DAARLGAPDT VPL
//
