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NNRD_PONAB
ID   NNRD_PONAB              Reviewed;         329 AA.
AC   Q5R824;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE            EC=4.2.1.93 {ECO:0000250|UniProtKB:Q9CZ42, ECO:0000255|HAMAP-Rule:MF_03157};
DE   AltName: Full=ATP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_03157};
DE   AltName: Full=Carbohydrate kinase domain-containing protein {ECO:0000255|HAMAP-Rule:MF_03157};
DE   AltName: Full=NAD(P)HX dehydratase {ECO:0000250|UniProtKB:Q8IW45};
GN   Name=NAXD {ECO:0000250|UniProtKB:Q8IW45};
GN   Synonyms=CARKD {ECO:0000255|HAMAP-Rule:MF_03157};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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;
CC         Evidence={ECO:0000250|UniProtKB:Q9CZ42, 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         Evidence={ECO:0000250|UniProtKB:Q9CZ42};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03157};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03157}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03157}.
CC   -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC       Rule:MF_03157}.
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DR   EMBL; CR859931; CAH92086.1; -; mRNA.
DR   RefSeq; NP_001126217.1; NM_001132745.1.
DR   AlphaFoldDB; Q5R824; -.
DR   SMR; Q5R824; -.
DR   STRING; 9601.ENSPPYP00000006272; -.
DR   GeneID; 100173186; -.
DR   KEGG; pon:100173186; -.
DR   CTD; 55739; -.
DR   eggNOG; KOG3974; Eukaryota.
DR   InParanoid; Q5R824; -.
DR   OrthoDB; 1337331at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; 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; IEA:UniProtKB-UniRule.
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; 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; PS51383; YJEF_C_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycoprotein; Lyase; Mitochondrion; NAD; NADP;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..329
FT                   /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT                   /id="PRO_0000337023"
FT   DOMAIN          35..326
FT                   /note="YjeF C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         135
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         188..194
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         228..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         247..256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   BINDING         257
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT   MOD_RES         67
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZ42"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   329 AA;  35099 MW;  4721AA59995B0AFA CRC64;
     MALGPRYGAI RACGRVLERA FSLRKAHSIK DMENTLQLVR NIIPPLSSTK HKGQDGRIGV
     VGGCQEYTGA PYFAAISALK VGADLSHVFC ASAAAPVIKA YSPELIVHPV LDSRSAVHEA
     EKWLPRLHAL VVGPGLGRDD ALLRNVQGIL EASKARDIPV VIDADGLWLV AQQPALIQGY
     RKAVLTPNHM EFSRLYDAVL RGPMDSNDSH GSVLRLSQAL GNVTVVQKGE RDILSNGQQV
     LVCSQEGSSR RCGGQGDLLS GSLGVLVHWA LLAGPEKTNG SSPLLVAAFG ACSLTRQCNH
     QAFQKHGRST TTSDMIAEVG AAFSKLFET
 
 
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