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Database: UniProt/TrEMBL
Entry: F4PJE8_DICFS
LinkDB: F4PJE8_DICFS
Original site: F4PJE8_DICFS 
ID   F4PJE8_DICFS            Unreviewed;       641 AA.
AC   F4PJE8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   07-JUN-2017, entry version 18.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=DFA_06584 {ECO:0000313|EMBL:EGG24434.1};
OS   Dictyostelium fasciculatum (strain SH3) (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=1054147 {ECO:0000313|Proteomes:UP000007797};
RN   [1] {ECO:0000313|EMBL:EGG24434.1, ECO:0000313|Proteomes:UP000007797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH3 {ECO:0000313|EMBL:EGG24434.1,
RC   ECO:0000313|Proteomes:UP000007797};
RA   Gloeckner G., Schaap P., Noegel A.A., Felder M., Eichinger L.,
RA   Heidel A.J., Platzer M.;
RT   "Living fossils from the dawn of multicellularity.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol. {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; GL883007; EGG24434.1; -; Genomic_DNA.
DR   RefSeq; XP_004362285.1; XM_004362228.1.
DR   ProteinModelPortal; F4PJE8; -.
DR   EnsemblProtists; EGG24434; EGG24434; DFA_06584.
DR   GeneID; 14875926; -.
DR   KEGG; dfa:DFA_06584; -.
DR   KO; K00111; -.
DR   Proteomes; UP000007797; 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; 3.50.50.60; -; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
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; 2.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007797};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007797}.
FT   DOMAIN      113    483       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      505    625       DAO_C. {ECO:0000259|Pfam:PF16901}.
FT   COILED       77    107       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   641 AA;  71566 MW;  096C758AD9C0C280 CRC64;
     MSRLFSFAKR NKYALIAATG VTAWGTTMMY NFNPVQHETT LDRYNRINQK KANDIISKGS
     SDDVQQYFNA SSSLLTRDQQ LQRLRNLSTT NQQQQQQQQQ QQQQQQQEGP LLDMVVIGGG
     VTGSGIALDA ASRGLSVAMF ERGDFCSATS SRSTKLIHGG IRYLESAIMN FDVEDLKLVK
     EALSERSNLL NNAPHLSHPL PITIPVYSWI DLPKMWIGTK LYDYFYPGND VPSSHYLSKS
     ETMKHFPYLK DGLLGSIVYY DGQHNDARMG ISIALSASQR GAITANYTEV VGFTRVVSSD
     PKSTINGVVV RDRLTGEQIN VRAKVVVNAT GPFSDSIRKM DDPKVSSVIA GASGVHLILP
     STLCPPDIGF LNPKTKDGRL LFILPFEGKT IAGTTDQKAD ITFTPKPTSE EINFILEAIN
     QYSRDEKLIG KEDVLAAWSG VRPLVKKGGL DGGPTSKINR SHSILTSQSG LITIVGGKWT
     TYRSMAEETV DKAVQYINTF TRRGCHTSNL LIFGADKYYN DLYKYLMTEF NVDEQVAKHL
     THSYGDQSVG LLKLAKDRGL TNRLVKEYPY IEAEVIYGIR EYACTAEDIL ARRTRLAFLD
     NRKSLEALPK VVDLMANELN WNKQTKEKQL NDTKEFLQTM I
//
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