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NNRE_PLAVS
ID   NNRE_PLAVS              Reviewed;         289 AA.
AC   A5K3F9;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
DE            EC=5.1.99.6;
DE   AltName: Full=NAD(P)HX epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
GN   ORFNames=PVX_117475;
OS   Plasmodium vivax (strain Salvador I).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=126793;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Salvador I;
RX   PubMed=18843361; DOI=10.1038/nature07327;
RA   Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA   Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q.,
RA   Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., Feldblyum T.V.,
RA   Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA   Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., Paulsen I., White O.,
RA   Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA   Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA   Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT   "Comparative genomics of the neglected human malaria parasite Plasmodium
RT   vivax.";
RL   Nature 455:757-763(2008).
CC   -!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of
CC       NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or
CC       heat-dependent hydration. This is a prerequisite for the S-specific
CC       NAD(P)H-hydrate dehydratase to allow the repair of both epimers of
CC       NAD(P)HX. {ECO:0000255|HAMAP-Rule:MF_03159}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215,
CC         ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227,
CC         ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6;
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03159};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03159};
CC   -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP-
CC       Rule:MF_03159}.
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DR   EMBL; AAKM01000004; EDL46063.1; -; Genomic_DNA.
DR   RefSeq; XP_001615790.1; XM_001615740.1.
DR   AlphaFoldDB; A5K3F9; -.
DR   SMR; A5K3F9; -.
DR   STRING; 126793.A5K3F9; -.
DR   EnsemblProtists; EDL46063; EDL46063; PVX_117475.
DR   GeneID; 5475088; -.
DR   KEGG; pvx:PVX_117475; -.
DR   VEuPathDB; PlasmoDB:PVX_117475; -.
DR   InParanoid; A5K3F9; -.
DR   OMA; TIYYPKP; -.
DR   PhylomeDB; A5K3F9; -.
DR   Proteomes; UP000008333; Chromosome 12.
DR   Proteomes; UP000008333; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052856; F:NADHX epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10260; -; 1.
DR   HAMAP; MF_01966; NADHX_epimerase; 1.
DR   InterPro; IPR004443; YjeF_N_dom.
DR   InterPro; IPR036652; YjeF_N_dom_sf.
DR   InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR   PANTHER; PTHR13232; PTHR13232; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   SUPFAM; SSF64153; SSF64153; 1.
DR   TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   3: Inferred from homology;
KW   Isomerase; Metal-binding; NAD; NADP; Nucleotide-binding; Potassium;
KW   Reference proteome.
FT   CHAIN           1..289
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416327"
FT   DOMAIN          71..277
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         122..126
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         123
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         185
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         189..195
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         218
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         221
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
SQ   SEQUENCE   289 AA;  32254 MW;  CCD204CF3C49711D CRC64;
     MRKELLLRTT NHSAFQNSVY LLGFLRFAKF QLSSRANISN VRPFKGRRTN CAATSVHSNR
     MEVTYLSQSL AQTIDNELMS DDVGYTTEQL MELAGLSIAQ IICREYSLDR FKKVLIFCGP
     GNNGGDGLVA ARHLKHFGYD VTVAYPKEKT KVLFQRLLKL LQHYHVPVVK SATGEDLKLY
     DLVVDALFGF SFTGEPRSPF DEIIHTINQS NKPVVSVDVP SGTNIDGGSA ANALSVNSEM
     NISLMLPKEG VRHYGKKHYL GGRFIPNSIV EKYNLKVPQF AGDNSYVQL
 
 
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