ID J1RX53_9ACTN Unreviewed; 534 AA.
AC J1RX53;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:EJJ03122.1, ECO:0000313|EMBL:QTZ91081.1};
GN ORFNames=SU9_006075 {ECO:0000313|EMBL:QTZ91081.1}, SU9_30674
GN {ECO:0000313|EMBL:EJJ03122.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ03122.1};
RN [1] {ECO:0000313|EMBL:EJJ03122.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ03122.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ91081.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ91081.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) 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; AJGV01000190; EJJ03122.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ91081.1; -; Genomic_DNA.
DR RefSeq; WP_006607635.1; NZ_CP072931.1.
DR AlphaFoldDB; J1RX53; -.
DR STRING; 1160718.SU9_30674; -.
DR KEGG; sauh:SU9_006075; -.
DR PATRIC; fig|1160718.3.peg.6200; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_11; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000009036; 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.
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:UP000009036}.
FT DOMAIN 35..388
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 421..531
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"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 56920 MW; 350B382D4E786444 CRC64;
MSTLQSVPAL GTHPASGSHA SRAETREQLS KATYDLLVIG GGILGISTAW HAAQAGLRVA
LVDAGDFAGA TSSASSKLLH GGLRYLQTGA VKLVAENHFE RRAVSRQVAP HLANPLTFYL
PVYKGGPHGA AKLGAGVFAY SALSAFGDGV GHVISPAKAA RDVPELRTDN LKAVAVYGDD
QMNDSRMALM TVRAAAAAGA TVLNHAEVTG LRFTQGRVTG AELKDRVEGA EFGVNARLVL
NATGPWVDHL RKMEDPNAAP SIRLSKGAHL VLKRTAPWKA ALATPIDKYR ITFALPWEDM
LLLGTTDEEF EGDPADVAVT EKDTAQILDE AAFSVRDQQL SRDLITYSFA GLRVLPGGPG
DTSKAKRETV VTEGSGGMLS VAGGKWTTFR HIGRTVMNKL AALPGHPLAE DMEPIAHLPK
KLPLPGIANP NAVAHRLLVD GGTPGPRMAP ETARHLATHY GSLSFDIARL ANENPALAER
IHPEAPEIWA QVAYARDHEW AETVDDVLRR RTTLMIRGLD TEDVRAKVKD MLAG
//
