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Database: UniProt
Entry: A0A1C4WZ60_MICEC
LinkDB: A0A1C4WZ60_MICEC
Original site: A0A1C4WZ60_MICEC 
ID   A0A1C4WZ60_MICEC        Unreviewed;       639 AA.
AC   A0A1C4WZ60;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-JUN-2019, entry version 14.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=GA0070618_2607 {ECO:0000313|EMBL:SCF01161.1};
OS   Micromonospora echinospora (Micromonospora purpurea).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=1877 {ECO:0000313|EMBL:SCF01161.1, ECO:0000313|Proteomes:UP000198253};
RN   [1] {ECO:0000313|EMBL:SCF01161.1, ECO:0000313|Proteomes:UP000198253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43816 {ECO:0000313|EMBL:SCF01161.1,
RC   ECO:0000313|Proteomes:UP000198253};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT607413; SCF01161.1; -; Genomic_DNA.
DR   Proteomes; UP000198253; Chromosome i.
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:UP000198253};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198253}.
FT   DOMAIN       62    408       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      458    581       DAO_C. {ECO:0000259|Pfam:PF16901}.
FT   REGION      596    639       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1C4WZ60}.
SQ   SEQUENCE   639 AA;  68813 MW;  9A89E19A504B9FA6 CRC64;
     MRADTRAACP YGTQTGSGCA VDRRSRYRER VRDPNISRTV AGQLSPVRRA ADLRRLRAER
     FDVLVIGGGV TGAGAALDAA SRGLKVALVE ARDFAAGTSS RSSKLIHGGL RYLEQLEFGL
     VHEALTERGL LATRLAPHLV RPVPILVPLP DGGGVRDLPA RVWRRAYYGT GVAAYDAFAG
     LFGGGRGMPL HRHLSREGTR RAFPSLRADQ VAGAIRYFDG QVDDARLVVT LARTAASLGA
     TMVTSARAVG LIRQAREVTG VRVRDLEAPP GSPDAEFEVH ARTVIAATGV WSDDMSRMLN
     DVGLRPGLRV RASKGVHLVV PRSAITGETG LILRTPTSVL FVIPWGGHWI IGTTDTDWRL
     DRSHPAASAR DIDYLLQQVN TVLDKPLTTD DIEGVYAGLR PLLSGEADST SKLSREHAVF
     EPMLGLLLVA GGKYTTYRVM AGDVVDRAAR RLGNVRPSRT ADLPLLGADG YAAMWRDRAD
     LARRHGVPVG VVEHLLERYG SLTLDLLALI AADPLLAAPL AGAPEYLAAE VTYAAQAEGA
     LHLEDVLTRR TRISFETTHR GLESAEHTAE LMGAVLGWDA DVRAREVAHY RARVEAERQS
     QRMPDDATAD AARLGAPDVR GFAADRGTDS DLSGLPAPY
//
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