ID   A0A345HSV2_9ACTN        Unreviewed;       568 AA.
AC   A0A345HSV2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase/oxidase {ECO:0000313|EMBL:AXG79776.1};
GN   ORFNames=DVK44_21345 {ECO:0000313|EMBL:AXG79776.1};
OS   Streptomyces paludis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2282738 {ECO:0000313|EMBL:AXG79776.1, ECO:0000313|Proteomes:UP000253868};
RN   [1] {ECO:0000313|Proteomes:UP000253868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSSD-12 {ECO:0000313|Proteomes:UP000253868};
RA   Zhao J.;
RL   Submitted (JUL-2018) 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}.
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DR   EMBL; CP031194; AXG79776.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345HSV2; -.
DR   KEGG; spad:DVK44_21345; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000253868; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253868}.
FT   DOMAIN          24..381
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          404..528
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          540..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   568 AA;  61807 MW;  A93BBE915F9C6839 CRC64;
     MRTATLGPAE RARALAAMTE RELDVLVVGA GVVGAGTALD AVTRGLATGL VEARDWAAGT
     SSRSSKLIHG GLRYLEMLDF ALVREALKER GLLLEKLAPH LVKPVPFLYP LKHKGWERLY
     AGSGVALYDA MSVSSGHGRG LPVHRHLSRR HALKVAPCLK KDALVGALQY YDAQMDDARY
     VATLVRTAAT YGAQVANGAR VVGFLREGER VVGARVRDVE AGGEYEIRAR QVVNATGVWT
     DDTQGLIAER GQFHVRASKG IHLVVPKDRI HSTTGLILRT EKSVLFVIPW GRHWIVGTTD
     TDWDLDKAHP AASSADIDYL LEHVNSVLSV PLTRDDVQGV YAGLRPLLAG ESDATSKLSR
     EHTVAHPVPG MVVIAGGKYT TYRVMAKDAV DEAVHGLDQR VADCVTEDVP LLGAEGYHAL
     WNGRAGMAAR TGIHVARVEH LLNRYGTLVE ELLELIAGDP GLGEPLAGAD DYLRAEVVYA
     ASHEGARHLE DVLTRRTRIS IETFDRGTRS ARECAELMAP VLGWDTDQIE REVTHYEKRV
     EAERESQRQP DDQTADAARL GAPDIVPI
//