ID A0A176L0I7_9ACTN Unreviewed; 551 AA.
AC A0A176L0I7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=A6P39_25785 {ECO:0000313|EMBL:OAA97991.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA97991.1};
RN [1] {ECO:0000313|EMBL:OAA97991.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA97991.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-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:OAA97991.1}.
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DR EMBL; LWRP01000135; OAA97991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176L0I7; -.
DR STRING; 710705.A6P39_25785; -.
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}.
FT DOMAIN 7..360
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 387..511
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 523..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 60038 MW; 35607E50CB3083BB CRC64;
MAERELDLLV VGGGVVGAGT ALDAVTRGLS TGLVEARDWA SGTSSRSSKL IHGGLRYLEM
LDFALVREAL KERGLLLERL APHLVKPVPF LYPLQHKGWE RLYAGSGVAL YDAMSMARGH
GRGLPLHRHL THRHALRVAP CLKKDALVGA LQYYDAQMDD ARFVATLVRT AASYGAKVAN
RARVSGFLRE GDRVVGARVQ DVEGGGEYEI RAKQIVNATG VWTDDTQAMV GERGQFHVRA
SKGIHLVVPK DRIHSTTGLI LRTEKSVLFV IPWGRHWIIG TTDTDWDLDK AHPAASSADI
DYLLEHVNSV LAVPLGRDDV QGVYAGLRPL LAGESDATSK LSREHTVAHP APGLVVVAGG
KYTTYRVMAK DAVDEAVHGL DMRVADCVTE ETPLLGAEGY QALWNARARI AARTGLHVAR
VEHLLNRYGS MAEEVLDLVA ADPALGEPLA AADDYLRAEV VYAASHEGAR HLDDALTRRT
RISIETFDRG TRSAREAAGL MAPVLGWDKD QIEREVEHYE KRVEAERESQ LQPDDLTADA
ARLGAPDIVP L
//
