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Database: UniProt
Entry: A0A117RVB0_9ACTN
LinkDB: A0A117RVB0_9ACTN
Original site: A0A117RVB0_9ACTN 
ID   A0A117RVB0_9ACTN        Unreviewed;       538 AA.
AC   A0A117RVB0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KUO11057.1};
GN   ORFNames=AQJ58_16045 {ECO:0000313|EMBL:KUO11057.1};
OS   Streptomyces sp. DSM 15324.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO11057.1, ECO:0000313|Proteomes:UP000053431};
RN   [1] {ECO:0000313|EMBL:KUO11057.1, ECO:0000313|Proteomes:UP000053431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO11057.1,
RC   ECO:0000313|Proteomes:UP000053431};
RA   Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
RL   Submitted (OCT-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:KUO11057.1}.
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DR   EMBL; LMXA01000014; KUO11057.1; -; Genomic_DNA.
DR   RefSeq; WP_067250544.1; NZ_KQ949026.1.
DR   AlphaFoldDB; A0A117RVB0; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000053431; 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.
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:UP000053431}.
FT   DOMAIN          38..391
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          423..521
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  57521 MW;  E31B45694FFAEB14 CRC64;
     MTSQSTLSSV PALGTHPASG SNPSRAETRE QLSKASYDLL VIGGGILGIS TAWHAAQSGL
     RVALVDAGDF AGATSSASSK LLHGGLRYLQ TGAVKLVAEN HFERRAVSRQ VAPHLANPLT
     FYLPVYKGGP HGAAKLGAGV FAYSALSAFG DGVGHLLSPA KAAQDVPELR TENLKAVAVY
     GDDQMNDARM ALMTVRAAVE AGAVVLNHAE VTGLRFTRGR VTGADLKDRV SGDEFGVNAR
     LVLNATGPWV DHLRKMEDPN AAPSIRLSKG AHLVLKRTSP WKAALATPID KYRITFALPW
     EDMLLLGTTD EEFEGDPADV AVNDKDIAQI LDEAAFSVRD QQLSRDNITY AFAGLRVLPG
     GPGDTAKAKR ETVVTEGRGG MLSVAGGKWT TFRHIGRTVM QKLEALPGHP LGDDFEPISS
     LPKKLPLPGV ANPRAVAHRL LVDNPAPGPR MAADTAKHLA THYGSLAFDI ARLANDNPEL
     GRRVHPDAPE IWAQVVYARD HEWAQTADDV LRRRTTLTIR GLATDEVRGK VQGLLDKR
//
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