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Database: UniProt/TrEMBL
Entry: A0A077X6Z6_PLABA Q4YUA6_PLABA
LinkDB: A0A077X6Z6_PLABA Q4YUA6_PLABA
Original site: A0A077X6Z6_PLABA Q4YUA6_PLABA 
ID   A0A077X6Z6_PLABA        Unreviewed;       627 AA.
AC   A0A077X6Z6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   25-OCT-2017, entry version 4.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=PBANKA_040480 {ECO:0000313|EMBL:CDS44934.1};
OS   Plasmodium berghei (strain Anka).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5823 {ECO:0000313|EMBL:CDS44934.1, ECO:0000313|Proteomes:UP000074855};
RN   [1] {ECO:0000313|EMBL:CDS44934.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ANKA {ECO:0000313|EMBL:CDS44934.1};
RX   PubMed=25359557; DOI=10.1186/PREACCEPT-1233682211145405;
RA   Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA   Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA   Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA   Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A.,
RA   Berriman M., Janse C.J.;
RT   "A comprehensive evaluation of rodent malaria parasite genomes and
RT   gene expression.";
RL   BMC Biol. 12:86-86(2014).
RN   [2] {ECO:0000313|EMBL:CDS44934.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ANKA {ECO:0000313|EMBL:CDS44934.1};
RA   Aslett A.Martin., De Silva Nishadi;
RL   Submitted (MAY-2014) 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; LK023119; CDS44934.1; -; Genomic_DNA.
DR   RefSeq; XP_677816.1; XM_672724.1.
DR   GeneID; 3426371; -.
DR   KEGG; pbe:PB001022.02.0; -.
DR   HOGENOM; HOG000004813; -.
DR   KO; K00111; -.
DR   Proteomes; UP000074855; Chromosome 4.
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; 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; 2.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000074855};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217,
KW   ECO:0000313|EMBL:CDS44934.1}.
FT   DOMAIN       59    401       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      475    609       DAO_C. {ECO:0000259|Pfam:PF16901}.
SQ   SEQUENCE   627 AA;  71139 MW;  4389CF69AF758CF1 CRC64;
     MLKKALAGAG GLGMISVGGV YLLKVNFHKN MIEKDVSYKY SPIANRSEMV NRLKTNQYDI
     LIIGGGATGA GLALDCATRG IRCALIDRND FSSGTSSKST KLLHGGIRYL ENAVKKLDIS
     ELYFVWEALG ERAHAMKIAP FMSRPIPILM PIYKLWQVPY FSYNIKIYDL LADLVCYFDK
     GVPNSMYIQK QNTLDQFPLL HKDELKGSLV YYDGQHNDTR MNLNLVLTSA IDNYVPGQIG
     ATICNHMEVI SFIMDENNQK IIGVRALDKI TNKEIEIYAK VIINATGPQG DIIRKMADEN
     SKPMIQVSVG CHFILPKWYS SKNNGMIIPK TSDGRVLFLL PWENSTIVGT TDEQRPLVDN
     PKIDKKDTDF LATELSKYIN VSPEEIKNDI KAAWCGFRPL VHDSKKQKKK KNSENNNQNE
     ITTHEISRSH EIIEDENGLI SILGGKWTIY RKMAQDTIDY VLSKHSDKIQ TKNECRTKFL
     MLIGSHDENG NLNQEDLTFG CSKLGKKLVD KYSEIDYETA NYLVSNYGYL SEKVCELAKE
     LKLFNKIDQT KPYIEAEIVY ASRYEFANTI SDVIGRRFRL GFIDTNVSNQ VIHKIANLLK
     DELNWSKDQM NKNIEEAKSY IDSLSLE
//
  All links  
Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

Download RDF
ID   Q4YUA6_PLABA            Unreviewed;       627 AA.
AC   Q4YUA6;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   25-OCT-2017, entry version 61.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=PB001022.02.0 {ECO:0000313|EMBL:CAH98401.1};
OS   Plasmodium berghei (strain Anka).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5823 {ECO:0000313|Proteomes:UP000007720};
RN   [1] {ECO:0000313|EMBL:CAH98401.1, ECO:0000313|Proteomes:UP000007720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANKA {ECO:0000313|Proteomes:UP000007720};
RX   PubMed=15637271; DOI=10.1126/science.1103717;
RA   Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A.,
RA   Berriman M., Florens L., Janssen C.S., Pain A., Christophides G.K.,
RA   James K., Rutherford K., Harris B., Harris D., Churcher C.M.,
RA   Quail M.A., Ormond D., Doggett J., Trueman H.E., Mendoza J.,
RA   Bidwell S.L., Rajandream M.A., Carucci D.J., Yates J.R. III,
RA   Kafatos F.C., Janse C.J., Barrell B.G., Turner C.M.R., Waters A.P.,
RA   Sinden R.S.;
RT   "A comprehensive survey of the Plasmodium life cycle by genomic,
RT   transcriptomic, and proteomic analyses.";
RL   Science 307:82-86(2005).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CAAI01002392; CAH98401.1; -; Genomic_DNA.
DR   RefSeq; XP_677816.1; XM_672724.1.
DR   STRING; 5821.PBANKA_040480; -.
DR   EnsemblProtists; CAH98401; CAH98401; PB001022.02.0.
DR   EnsemblProtists; CDS44934; CDS44934; PBANKA_040480.
DR   GeneID; 3426371; -.
DR   KEGG; pbe:PB001022.02.0; -.
DR   EuPathDB; PlasmoDB:PBANKA_0404800; -.
DR   HOGENOM; HOG000004813; -.
DR   KO; K00111; -.
DR   Proteomes; UP000007720; 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; 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; 2.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007720};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007720}.
SQ   SEQUENCE   627 AA;  71139 MW;  4389CF69AF758CF1 CRC64;
     MLKKALAGAG GLGMISVGGV YLLKVNFHKN MIEKDVSYKY SPIANRSEMV NRLKTNQYDI
     LIIGGGATGA GLALDCATRG IRCALIDRND FSSGTSSKST KLLHGGIRYL ENAVKKLDIS
     ELYFVWEALG ERAHAMKIAP FMSRPIPILM PIYKLWQVPY FSYNIKIYDL LADLVCYFDK
     GVPNSMYIQK QNTLDQFPLL HKDELKGSLV YYDGQHNDTR MNLNLVLTSA IDNYVPGQIG
     ATICNHMEVI SFIMDENNQK IIGVRALDKI TNKEIEIYAK VIINATGPQG DIIRKMADEN
     SKPMIQVSVG CHFILPKWYS SKNNGMIIPK TSDGRVLFLL PWENSTIVGT TDEQRPLVDN
     PKIDKKDTDF LATELSKYIN VSPEEIKNDI KAAWCGFRPL VHDSKKQKKK KNSENNNQNE
     ITTHEISRSH EIIEDENGLI SILGGKWTIY RKMAQDTIDY VLSKHSDKIQ TKNECRTKFL
     MLIGSHDENG NLNQEDLTFG CSKLGKKLVD KYSEIDYETA NYLVSNYGYL SEKVCELAKE
     LKLFNKIDQT KPYIEAEIVY ASRYEFANTI SDVIGRRFRL GFIDTNVSNQ VIHKIANLLK
     DELNWSKDQM NKNIEEAKSY IDSLSLE
//
  All links  
Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

Download RDF
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