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
//