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NNRE_PLAL2
ID   NNRE_PLAL2              Reviewed;         257 AA.
AC   D5SRZ4;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_01966};
DE            EC=5.1.99.6 {ECO:0000255|HAMAP-Rule:MF_01966};
DE   AltName: Full=NAD(P)HX epimerase {ECO:0000255|HAMAP-Rule:MF_01966};
GN   Name=nnrE {ECO:0000255|HAMAP-Rule:MF_01966}; OrderedLocusNames=Plim_2896;
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetes; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290;
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
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_01966}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01966};
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01966};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01966};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01966};
CC   -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01966}.
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DR   EMBL; CP001744; ADG68718.1; -; Genomic_DNA.
DR   RefSeq; WP_013111149.1; NC_014148.1.
DR   AlphaFoldDB; D5SRZ4; -.
DR   SMR; D5SRZ4; -.
DR   STRING; 521674.Plim_2896; -.
DR   EnsemblBacteria; ADG68718; ADG68718; Plim_2896.
DR   KEGG; plm:Plim_2896; -.
DR   eggNOG; COG0062; Bacteria.
DR   HOGENOM; CLU_024853_0_1_0; -.
DR   OMA; SMFRGRY; -.
DR   OrthoDB; 1748633at2; -.
DR   Proteomes; UP000002220; Chromosome.
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   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..257
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000416374"
FT   DOMAIN          26..251
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         80..84
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         81
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         149
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         153..159
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         182
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
FT   BINDING         185
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01966"
SQ   SEQUENCE   257 AA;  27895 MW;  B754687C5AE59DCD CRC64;
     MEICPFVRLL DWRTLRAADC LTARQSREVD RFAIEELGIS SLVLMENAAR SVCDWFSQHV
     QASSSEETSF VVRVVCGRGN NGGDGFAIAR LLWTMGYAVE IFATHPEAEL APDARVNAAL
     ARKLGIPWRE MREFGEAAAS ARAEDWIVDA ILGTGQSRPL SGVLAELVQG MNASLSRRLA
     VDLPTGFSAD AGPGLGNPLT EQPHELVELC VRADVTVTFV TPKMGMLHPG AREYLGETFV
     ASIGLPEKLL REAVSLQ
 
 
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