ID A0A101R5H4_9ACTN Unreviewed; 570 AA.
AC A0A101R5H4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=AQJ30_01525 {ECO:0000313|EMBL:KUN42075.1};
OS Streptomyces longwoodensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN42075.1, ECO:0000313|Proteomes:UP000053271};
RN [1] {ECO:0000313|EMBL:KUN42075.1, ECO:0000313|Proteomes:UP000053271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN42075.1,
RC ECO:0000313|Proteomes:UP000053271};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT for the species Streptomyces longwoodensis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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:KUN42075.1}.
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DR EMBL; LMWS01000001; KUN42075.1; -; Genomic_DNA.
DR RefSeq; WP_067227836.1; NZ_KQ948549.1.
DR AlphaFoldDB; A0A101R5H4; -.
DR STRING; 68231.AQJ30_01525; -.
DR Proteomes; UP000053271; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 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 ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000053271}.
FT DOMAIN 25..379
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..529
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 544..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 62146 MW; BD7368477AA9EEB9 CRC64;
MANPVALSPG SRAEALVRLG EGELDVLVVG GGVVGAGAAL DAATRGLRVG LVEARDWASG
TSSRSSKLIH GGLRYLEMLD FRLVAEALKE RGLLLQVLAP HLVRPVPFLY PLQHRVRERP
YVGAGVLLYD TMATASGTSR GLPHHRHLFK RRALREAPAL RADALVGAIQ YWDAQVDDAR
HTLFLVRTAA AYGALAANRT RVSRFLRQGE RVVGAVVTDL DTGEETEVRA KQVINATGVW
TDDTQSLAGT RGQFHVRASK GVHLLVPRDR INSRTGLILR TEKSVLFVIP WGRHWIIGTT
DTDWTLDKAH PALSSKDVTY LLEHVNSVLA TPLAPEDVEG VYAGLRPLLS GEAAETSKLS
REHLVAHPVP GLVVVAGGKY TTYRVMAKDA VDEAVRGLDE KVPDCVTHRV PLLGADGYPA
LWNSRHNLAA SSGLHVARIE HLLNRYGSLV HELLALVVAD PSLGEPLPSS DDYLRVEAVY
AVTHEGARHV EDVLARRTRI SIESWDRGVD AARTVAELMA PHLGWDQADR DREVDHYLKR
VAAEREAQQQ PDDRTADAVR LGAPDISPVL
//
