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Database: UniProt
Entry: A0A0G3A8Z9_9ACTN
LinkDB: A0A0G3A8Z9_9ACTN
Original site: A0A0G3A8Z9_9ACTN 
ID   A0A0G3A8Z9_9ACTN        Unreviewed;       527 AA.
AC   A0A0G3A8Z9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:AKJ08787.1};
GN   ORFNames=ABB07_01655 {ECO:0000313|EMBL:AKJ08787.1};
OS   Streptomyces incarnatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ08787.1, ECO:0000313|Proteomes:UP000035366};
RN   [1] {ECO:0000313|EMBL:AKJ08787.1, ECO:0000313|Proteomes:UP000035366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX   PubMed=26159526;
RA   Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA   Tamura T.;
RT   "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT   the Nucleoside Antibiotic Sinefungin.";
RL   Genome Announc. 3:e00715-e00715(2015).
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; CP011497; AKJ08787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3A8Z9; -.
DR   STRING; 665007.ABB07_01655; -.
DR   PATRIC; fig|665007.5.peg.382; -.
DR   Proteomes; UP000035366; 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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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          31..397
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          440..521
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   527 AA;  55510 MW;  2E65D848B9F060D0 CRC64;
     MSHTRAGAGS SLSAHRRRRE LAEATDGRVV DVLVVGLGAT GAGAALDAAA RGLDVAAVDA
     HDLAFGTSRW SSKLIHGGLR YLASAQFDVA HESAVERGVL MTRTAPHLVA AQPFVLPLTP
     LVSRAQASLA WAGFRAGDML RLAARTPRQV LPAPRRLSAT EARHLAPAVR PAGLRGGLLS
     WDGKVADDAR LVTALARTAA AQGARVLTRV RVLELTGTGA RIRDELTGDE GEIRARAVIN
     ATGVWAGDLV EGIRIRPSRG THLVLRSERL GTLPAGLHIP IPGETNRFVL VLPQGDGRVY
     VGLTDEPVEG GIPDVPDVPE TDIGFLLDVL GSVLDTPVTR EEVVGAFAGL RPLLDTSALD
     GRDGEPARTS DISRRHAVLT SPDGITTIVG GKLTTYRRMA QDAVDAATAA RGLPAPPSPT
     ATLPLVGAAA PGRLRGLSAP RRLIRRYGTE AEAVHALAAD DPALAERVLP GHPVTRAELL
     WAVRHEGALD ESDLLDRRTR IGLVPEDRAE VLPVAREVLA EAESVRP
//
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