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Database: UniProt
Entry: A0A239D547_9ACTN
LinkDB: A0A239D547_9ACTN
Original site: A0A239D547_9ACTN 
ID   A0A239D547_9ACTN        Unreviewed;       579 AA.
AC   A0A239D547;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 10.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=SAMN05443665_1002123 {ECO:0000313|EMBL:SNS27359.1};
OS   Actinomadura meyerae.
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Actinomadura.
OX   NCBI_TaxID=240840 {ECO:0000313|EMBL:SNS27359.1, ECO:0000313|Proteomes:UP000198318};
RN   [1] {ECO:0000313|EMBL:SNS27359.1, ECO:0000313|Proteomes:UP000198318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44715 {ECO:0000313|EMBL:SNS27359.1,
RC   ECO:0000313|Proteomes:UP000198318};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         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|RuleBase:RU361217};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU361217}.
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DR   EMBL; FZOR01000002; SNS27359.1; -; Genomic_DNA.
DR   BioCyc; GCF_900188445:CHF16_RS03355-MONOMER; -.
DR   Proteomes; UP000198318; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000198318};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198318}.
FT   DOMAIN       32    386       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      413    537       DAO_C. {ECO:0000259|Pfam:PF16901}.
FT   REGION      548    579       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A239D547}.
FT   COMPBIAS    548    567       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A239D547}.
SQ   SEQUENCE   579 AA;  63238 MW;  69FA0F3515B9E3BD CRC64;
     MTASPVTGLG SSRLGPAERA AALDRMAREE FDVVVVGGGI VGAGAALDAA TRGLSVAVVE
     ARDFASGTSS RSSKLIHGGL RYLEQYNFDL VREALTERSL LLQTIAPHLV KPVPFLLPTT
     HRVWERAYLG AGVALYDALA FQMGSTRGVP HHRHLTRRGA LRLAPSLRKD AFVGAIQYWD
     AQVDDARFVM MLLRTAAQYG AQVASRTQCL GFLREGERVT GLRIRDLEGN TTSEVRAKQV
     VNATGVWTDD IQELVGGRGQ IHVKASKGIH LVVPKDRIHS STGIILRTEK SVLFVIPWGR
     HWIIGTTDTA WDLDRAHPAA SKADIDYVLD HVNAVLSTPL THDDVEGVYA GLRPLLTGET
     DETSKLSREH VVAHPVPGLV LVAGGKYTTY RVMAKDAIDA VAHGLDGKVA ESCTDRIPLV
     GGDGFQAMWN ARHRLASRSG LHVARIEHLL RRYGTLLDDL LGLIADKPDL AKPLTGADDY
     LRAEVVYAAT HEGARHLNDV LARRTRISIE TWDRGVGVAQ EAADLLAPVL GWSKKQRDRE
     IEYYRKRVEA ERASQTQEDD QEANAHRRGA PDIVPVATP
//
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