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Database: UniProt
Entry: A0A094RPB6_9ACTN
LinkDB: A0A094RPB6_9ACTN
Original site: A0A094RPB6_9ACTN 
ID   A0A094RPB6_9ACTN        Unreviewed;       502 AA.
AC   A0A094RPB6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KGA06753.1};
DE   Flags: Fragment;
GN   ORFNames=GM42_3135 {ECO:0000313|EMBL:KGA06753.1};
OS   actinobacterium acMicro-1.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1504316 {ECO:0000313|EMBL:KGA06753.1, ECO:0000313|Proteomes:UP000029316};
RN   [1] {ECO:0000313|EMBL:KGA06753.1, ECO:0000313|Proteomes:UP000029316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT   "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT   sequencing.";
RL   Submitted (MAY-2014) 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:KGA06753.1}.
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DR   EMBL; JNSC01000029; KGA06753.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094RPB6; -.
DR   STRING; 1504316.GM42_3135; -.
DR   PATRIC; fig|1504316.4.peg.626; -.
DR   Proteomes; UP000029316; 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: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; 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}.
FT   DOMAIN          27..385
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          411..502
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   NON_TER         502
FT                   /evidence="ECO:0000313|EMBL:KGA06753.1"
SQ   SEQUENCE   502 AA;  54653 MW;  EF2C310D78973EB7 CRC64;
     MTAASPFGIN EETRARALEV MTSRELDILV VGAGIVGTGT ALDAATRGLT VGLLEARDFA
     SGTSGLSSKL VHGGIRYLEQ LNFGLVREAL AERGLLLQHI APHLVTPIRF LYPVHHHVWE
     RAYIGAGMML YDGMSYLGGR LPGVPHHRHL SKRQVMLAAP GLAEHATVGG MTYYDGHVDD
     ARYAATLART AAHYGAQIAT RTFVSELLRD GDRVIGVRAR DNMTGDMFEV RAKQVIVAAG
     VWTSTLQDMI GDPETFEVRM SKGVHILVEK DKFRSLMGLL LRTEKSVLFV IPWGRFWIIG
     TTDTAWTLDA AHPVATRADI DYILGHVNKV LSTPLTHDDV VGVYAGLRPL LAGDSDETSK
     LSREHIVSNP APGVTIVAGG KWTTYRVMAK DAVDAALDNL PLSLAARVPA SVTANVALLG
     ADGYSAAVNR RAEWARRTGL GRYQITRLLG RYGSEIEAIV EIIEAQPELA TTLPGTKDYR
     EAEVVFAARY EMALRLDDVL MR
//
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