ID A0A0N0N1V8_9ACTN Unreviewed; 551 AA.
AC A0A0N0N1V8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KPI16488.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:KPI16488.1};
GN ORFNames=OK074_8422 {ECO:0000313|EMBL:KPI16488.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI16488.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI16488.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI16488.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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}.
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:KPI16488.1}.
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DR EMBL; LJCV01000096; KPI16488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0N1V8; -.
DR PATRIC; fig|1592327.3.peg.3145; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
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: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; SSF51905; FAD/NAD(P)-binding domain; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KPI16488.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
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 522..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 60432 MW; 55E946E1E2CC5E27 CRC64;
MAERELDVLV VGGGVVGAGT VLDAATRGLA TGLVEARDWA SGTSSRSSKL IHGGLRYLEM
LDFALVREAL KERGLLLERL APHLVKPVPF LYPLQHQGWE RLYAGSGVAL YDAMSMARGH
GRGLPTHRHL SRRHALRVAP CLKKESLVGA LQYYDAQMDD ARYVATLVRT AASYGAKVAN
RARVTGFLRE GERVVGAKVQ DVEAGGEYEI RAKQVVNATG VWTDDTQAMV GERGQFHVRA
SKGIHLVVPK DRIHSTTGLI LRTEKSVLFV IPWGRHWIVG TTDTDWDLDK AHPAASSADI
DYLLEHVNSV LAVPLTRDDV QGVYAGLRPL LAGESDATSK LSREHTVAHP VPGLVVVAGG
KYTTYRVMAK DAVDEAVHGL DQRVAECVTE DVPLLGAEGY RALWNARARI SARTGLHVAR
IEHLLNRYGS MAEELLELVT ADPSLGEPLQ AADDYLRAEV VYAASHEGAR HLDDVLTRRT
RISIETFDRG TRSAREAAEL MAPVLGWDKD QIEREVEHYQ KRVEAERESQ RQPDDLTADA
ARLGAPDIVP L
//
