位置:首页 > 蛋白库 > NNRD_BATDJ
NNRD_BATDJ
ID   NNRD_BATDJ              Reviewed;         318 AA.
AC   F4NZ38;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE            EC=4.2.1.93 {ECO:0000255|HAMAP-Rule:MF_03157};
DE   AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
GN   ORFNames=BATDEDRAFT_10166;
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the
CC       expense of ATP, which is converted to ADP. Together with NAD(P)HX
CC       epimerase, which catalyzes the epimerization of the S- and R-forms, the
CC       enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of
CC       NAD(P)H that is a result of enzymatic or heat-dependent hydration.
CC       {ECO:0000255|HAMAP-Rule:MF_03157}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate;
CC         Xref=Rhea:RHEA:19017, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074,
CC         ChEBI:CHEBI:456216; EC=4.2.1.93; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-NADPHX + ATP = ADP + H(+) + NADPH + phosphate;
CC         Xref=Rhea:RHEA:32231, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076,
CC         ChEBI:CHEBI:456216; EC=4.2.1.93;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03157};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03157}.
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC       Rule:MF_03157}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL882881; EGF81817.1; -; Genomic_DNA.
DR   RefSeq; XP_006677152.1; XM_006677089.1.
DR   AlphaFoldDB; F4NZ38; -.
DR   SMR; F4NZ38; -.
DR   STRING; 684364.F4NZ38; -.
DR   EnsemblFungi; EGF81817; EGF81817; BATDEDRAFT_10166.
DR   GeneID; 18236428; -.
DR   HOGENOM; CLU_030651_3_0_1; -.
DR   InParanoid; F4NZ38; -.
DR   OMA; HIPHTNE; -.
DR   OrthoDB; 1337331at2759; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047453; F:ATP-dependent NAD(P)H-hydrate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0110051; P:metabolite repair; IBA:GO_Central.
DR   GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01171; YXKO-related; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_01965; NADHX_dehydratase; 1.
DR   InterPro; IPR017953; Carbohydrate_kinase_pred_CS.
DR   InterPro; IPR000631; CARKD.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR   PROSITE; PS01050; YJEF_C_2; 1.
DR   PROSITE; PS51383; YJEF_C_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Lyase; NAD; NADP; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..318
FT                   /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT                   /id="PRO_0000416179"
FT   DOMAIN          3..313
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         119
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         172..178
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         210..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         229..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         239
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
SQ   SEQUENCE   318 AA;  34075 MW;  5826F932D5F03A98 CRC64;
     MAAREVFKRV IPPLSTRLHK GQSGRIGVVG GSLEYTGAPY YAAMAALYTG VDLCHVFCAQ
     DAAPAIKCYS PELVVHPSIV SKRDCEHLNP VAIDNCIETA VDRMSPLLCR LDSLVVGPGL
     SRDPVMLAMA KRIVEKVISL GTPLVIDADG LCLVEQTPGL VMGYQNVILT PNTNEFKRLC
     HSVNIDASEN CEVAAVQLSK ALGSVTILCK GSKDLIATGD DILFVSDPTS LRRCGGQGDV
     LAGILCAFLA WRNGYQSGRW TAQDQSTDIS LMIVASNASS FARKCAALAF EKHKRSIVAS
     SILKEIGPAF DSLYDDEL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024