NNRE_YEAST
ID NNRE_YEAST Reviewed; 246 AA.
AC P40165; D6W0Y8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
DE EC=5.1.99.6 {ECO:0000269|PubMed:21994945};
DE AltName: Full=NAD(P)HX epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
DE AltName: Full=Nicotinamide nucleotide repair protein 1 {ECO:0000303|Ref.9};
GN Name=NNR1 {ECO:0000303|Ref.9}; OrderedLocusNames=YNL200C; ORFNames=N1370;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7725799; DOI=10.1002/yea.320101213;
RA Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
RT "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
RT WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8
RT new open reading frames of unknown function.";
RL Yeast 10:1639-1645(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21994945; DOI=10.1074/jbc.c111.310847;
RA Marbaix A.Y., Noel G., Detroux A.M., Vertommen D., Van Schaftingen E.,
RA Linster C.L.;
RT "Extremely conserved ATP- or ADP-dependent enzymatic system for
RT nicotinamide nucleotide repair.";
RL J. Biol. Chem. 286:41246-41252(2011).
RN [9]
RP IDENTIFICATION.
RX DOI=10.1016/j.plgene.2015.11.002;
RA Firestone K., Awonusi D., Panfair D., Roland D., Ramamurthy A.,
RA Kusmierczyk A.R.;
RT "YPL260W, a high-copy suppressor of a copper-sensitive phenotype in yeast,
RT is linked to DNA repair and proteasome function.";
RL Plant Gene 5:38-48(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of yeast hypothetical protein YNU0_yeast.";
RL Submitted (FEB-2009) to the PDB data bank.
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 ECO:0000269|PubMed:21994945}.
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:0000269|PubMed:21994945};
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:0000269|PubMed:21994945};
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 -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
CC -!- MISCELLANEOUS: Present with 1380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP-
CC Rule:MF_03159}.
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DR EMBL; X78898; CAA55508.1; -; Genomic_DNA.
DR EMBL; Z71476; CAA96099.1; -; Genomic_DNA.
DR EMBL; AY692583; AAT92602.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10354.1; -; Genomic_DNA.
DR PIR; S50731; S50731.
DR RefSeq; NP_014199.1; NM_001183038.1.
DR PDB; 1JZT; X-ray; 1.94 A; A/B=1-246.
DR PDBsum; 1JZT; -.
DR AlphaFoldDB; P40165; -.
DR SMR; P40165; -.
DR BioGRID; 35634; 24.
DR STRING; 4932.YNL200C; -.
DR MaxQB; P40165; -.
DR PaxDb; P40165; -.
DR PRIDE; P40165; -.
DR EnsemblFungi; YNL200C_mRNA; YNL200C; YNL200C.
DR GeneID; 855521; -.
DR KEGG; sce:YNL200C; -.
DR SGD; S000005144; NNR1.
DR VEuPathDB; FungiDB:YNL200C; -.
DR eggNOG; KOG2585; Eukaryota.
DR GeneTree; ENSGT00390000007227; -.
DR HOGENOM; CLU_024853_3_0_1; -.
DR InParanoid; P40165; -.
DR OMA; TIYYPKP; -.
DR BioCyc; YEAST:G3O-33209-MON; -.
DR Reactome; R-SCE-197264; Nicotinamide salvaging.
DR EvolutionaryTrace; P40165; -.
DR PRO; PR:P40165; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40165; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IDA:SGD.
DR GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Metal-binding; Mitochondrion; NAD;
KW NADP; Nucleotide-binding; Potassium; Reference proteome.
FT CHAIN 1..246
FT /note="NAD(P)H-hydrate epimerase"
FT /id="PRO_0000119061"
FT DOMAIN 12..234
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 69..73
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 70
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 138
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 142..148
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 173
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT BINDING 176
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:1JZT"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1JZT"
FT HELIX 28..46
FT /evidence="ECO:0007829|PDB:1JZT"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1JZT"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1JZT"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:1JZT"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1JZT"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1JZT"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:1JZT"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1JZT"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:1JZT"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:1JZT"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1JZT"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:1JZT"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1JZT"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1JZT"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:1JZT"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:1JZT"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1JZT"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1JZT"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:1JZT"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1JZT"
SQ SEQUENCE 246 AA; 27521 MW; 78595E7C92C5E11A CRC64;
MSTLKVVSSK LAAEIDKELM GPQIGFTLQQ LMELAGFSVA QAVCRQFPLR GKTETEKGKH
VFVIAGPGNN GGDGLVCARH LKLFGYNPVV FYPKRSERTE FYKQLVHQLN FFKVPVLSQD
EGNWLEYLKP EKTLCIVDAI FGFSFKPPMR EPFKGIVEEL CKVQNIIPIV SVDVPTGWDV
DKGPISQPSI NPAVLVSLTV PKPCSSHIRE NQTTHYVGGR FIPRDFANKF GFEPFGYEST
DQILKL
