NNRD_YEAST
ID NNRD_YEAST Reviewed; 337 AA.
AC P36059; D6VX46; Q6Q5N3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 160.
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};
DE AltName: Full=Nicotinamide nucleotide repair protein 2 {ECO:0000303|Ref.12};
GN Name=NNR2 {ECO:0000303|Ref.12}; OrderedLocusNames=YKL151C; ORFNames=YKL606;
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 204508 / S288c;
RX PubMed=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=13331940; DOI=10.1016/s0021-9258(18)65307-4;
RA Meinhart J.O., Chaykin S., Krebs E.G.;
RT "Enzymatic conversion of a reduced diphosphopyridine nucleotide derivative
RT to reduced diphosphopyridine nucleotide.";
RL J. Biol. Chem. 220:821-829(1956).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=3061454; DOI=10.1021/bi00419a030;
RA Acheson S.A., Kirkman H.N., Wolfenden R.;
RT "Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent
RT dehydration.";
RL Biochemistry 27:7371-7375(1988).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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).
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, ECO:0000269|PubMed:21994945}.
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 ECO:0000269|PubMed:13331940};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03157,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP-
CC Rule:MF_03157}.
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DR EMBL; Z26877; CAA81502.1; -; Genomic_DNA.
DR EMBL; Z28151; CAA81992.1; -; Genomic_DNA.
DR EMBL; AY557915; AAS56241.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09012.1; -; Genomic_DNA.
DR PIR; S37799; S37799.
DR RefSeq; NP_012771.1; NM_001179717.1.
DR AlphaFoldDB; P36059; -.
DR SMR; P36059; -.
DR BioGRID; 33986; 50.
DR IntAct; P36059; 2.
DR MINT; P36059; -.
DR STRING; 4932.YKL151C; -.
DR iPTMnet; P36059; -.
DR MaxQB; P36059; -.
DR PaxDb; P36059; -.
DR PRIDE; P36059; -.
DR EnsemblFungi; YKL151C_mRNA; YKL151C; YKL151C.
DR GeneID; 853706; -.
DR KEGG; sce:YKL151C; -.
DR SGD; S000001634; NNR2.
DR VEuPathDB; FungiDB:YKL151C; -.
DR eggNOG; KOG3974; Eukaryota.
DR GeneTree; ENSGT00390000000917; -.
DR HOGENOM; CLU_030651_0_0_1; -.
DR InParanoid; P36059; -.
DR OMA; HIPHTNE; -.
DR BioCyc; YEAST:G3O-31923-MON; -.
DR BRENDA; 4.2.1.93; 984.
DR Reactome; R-SCE-197264; Nicotinamide salvaging.
DR PRO; PR:P36059; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36059; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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; IDA:SGD.
DR GO; GO:0110051; P:metabolite repair; IBA:GO_Central.
DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IDA:SGD.
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; PS01049; YJEF_C_1; 1.
DR PROSITE; PS01050; YJEF_C_2; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Lyase; NAD; NADP; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..337
FT /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /id="PRO_0000119053"
FT DOMAIN 11..335
FT /note="YjeF C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT REGION 224..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 182..188
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 218..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 240..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT BINDING 250
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03157"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 182
FT /note="N -> D (in Ref. 4; AAS56241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37357 MW; 472C46DB6956244E CRC64;
MLAELSHREL IKLAQKRCIP PLLPKFHKGQ SGGRVCIIGG CEDYTGAPYF SANATALMGC
DLTHVICEYN AGTVIKSYTP NLMVHPYLRM SNTKLDVDMD EQRKKINSLL DRIHVVVIGP
GLGRDPLMLK SIKDIIRYIL EKHEGKIPLV IDADGLFLVT QDSEVKEMLK SYPKGRVILT
PNVVEFKRLC DAIGKKGDSH SEMGSLIAQE LNCIVVEKGQ SDKIFSPDSE KDMLTNSEEG
SNKRVGGQGD TLTGAISCML AFSRAMYDFK ICEQEEKGES SNDKPLKNWV DYAMLSCYAG
CTITRECSRL GFKAKGRAMQ TTDLNDRVGE VFAKLFG
