ID   F2RE01_STRVP            Unreviewed;       534 AA.
AC   F2RE01;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   28-JAN-2026, entry version 63.
DE   SubName: Full=Aerobic glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:CCA54541.1};
DE            EC=1.1.5.3 {ECO:0000313|EMBL:CCA54541.1};
GN   OrderedLocusNames=SVEN_1254 {ECO:0000313|EMBL:CCA54541.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA54541.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA54541.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA54541.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
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}.
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DR   EMBL; FR845719; CCA54541.1; -; Genomic_DNA.
DR   RefSeq; WP_015032459.1; NC_018750.1.
DR   AlphaFoldDB; F2RE01; -.
DR   STRING; 953739.SVEN_1254; -.
DR   GeneID; 51861845; -.
DR   KEGG; sve:SVEN_1254; -.
DR   PATRIC; fig|953739.5.peg.3319; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:TreeGrafter.
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:SF31; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 2; 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.
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:CCA54541.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT   DOMAIN          35..388
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          422..517
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  57410 MW;  F3FFAA27F21D9362 CRC64;
     MTTLQSVPAL GTHPASGSLP SRAETREQLS KATYDLLVIG GGILGISTAW HAAQSGLRVA
     LVDAGDFAGA TSSASSKLLH GGLRYLQTGA VKLVAENHFE RRAVSRQVAP HLANPLTFYL
     PVYKGGPHGA AKLGAGVFAY SALSAFGDGV GHLLSPAKAA QDVPELRTDN LKAVAVYGDD
     QMNDARMALM TVRAAVDAGA TVLNHAEVTG LRFTRGRVTG AELKDRTSGD EFGVTARLVL
     NATGPWVDHL RKMEDPNAAP SIRLSKGAHL VLKRTSPWKA ALATPIDKYR ITFALPWEDM
     LLLGTTDEEY EGDPGQVEVT EKDTAQILDE AAFSIRDQQL SRDLITYAFA GLRVLPGGPG
     DTSKAKRETV VTEGRGGMLS VAGGKWTTFR HIGRTVMKKL EQLPGHPLGE DYEPVSTLPK
     RLPLPGIANP NAVAHRLLVD GPAPGPRMAA DTAKHLATHY GSLSFDIARM ANENPELARR
     IHPDAPEIWA QVAYARDHEW AETADDVLRR RTTLTIRGLA TDEIRADVER MLKK
//