NNR_ECOLI
ID NNR_ECOLI Reviewed; 515 AA.
AC P31806; Q2M6D8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme Nnr;
DE AltName: Full=Nicotinamide nucleotide repair protein;
DE Includes:
DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase;
DE EC=4.2.1.136;
DE AltName: Full=ADP-dependent NAD(P)HX dehydratase;
DE Includes:
DE RecName: Full=NAD(P)H-hydrate epimerase;
DE EC=5.1.99.6;
DE AltName: Full=NAD(P)HX epimerase;
GN Name=nnr; Synonyms=yjeF; OrderedLocusNames=b4167, JW4125;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-515.
RC STRAIN=K12;
RX PubMed=7511774; DOI=10.1111/j.1365-2958.1994.tb00300.x;
RA Tsui H.-C.T., Zhao G., Feng G., Leung H.-C.E., Winkler M.E.;
RT "The mutL repair gene of Escherichia coli K-12 forms a superoperon with a
RT gene encoding a new cell-wall amidase.";
RL Mol. Microbiol. 11:189-202(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of the
CC S- and R-forms of NAD(P)HX and the dehydration of the S-form of
CC NAD(P)HX at the expense of ADP, which is converted to AMP. This allows
CC the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that
CC is a result of enzymatic or heat-dependent hydration.
CC {ECO:0000269|PubMed:21994945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate;
CC Xref=Rhea:RHEA:32223, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=4.2.1.136;
CC Evidence={ECO:0000269|PubMed:21994945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate;
CC Xref=Rhea:RHEA:32235, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=4.2.1.136;
CC Evidence={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; Evidence={ECO:0000250};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for (S)-NADHX {ECO:0000269|PubMed:21994945};
CC KM=0.86 uM for (S)-NADPHX {ECO:0000269|PubMed:21994945};
CC KM=3.6 uM for ADP {ECO:0000269|PubMed:21994945};
CC Vmax=0.62 umol/min/mg enzyme toward (S)-NADHX
CC {ECO:0000269|PubMed:21994945};
CC Vmax=0.88 umol/min/mg enzyme toward (S)-NADPHX
CC {ECO:0000269|PubMed:21994945};
CC Vmax=0.6 umol/min/mg enzyme toward ADP {ECO:0000269|PubMed:21994945};
CC -!- INTERACTION:
CC P31806; P15005: mcrB; NbExp=3; IntAct=EBI-554188, EBI-552513;
CC P31806; P63177: rlmB; NbExp=3; IntAct=EBI-554188, EBI-562712;
CC -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD
CC family. {ECO:0000305}.
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DR EMBL; U14003; AAA97063.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77124.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78168.1; -; Genomic_DNA.
DR EMBL; L19346; AAA20095.1; -; Unassigned_DNA.
DR PIR; S56392; S56392.
DR RefSeq; NP_418588.1; NC_000913.3.
DR RefSeq; WP_001295189.1; NZ_LN832404.1.
DR AlphaFoldDB; P31806; -.
DR SMR; P31806; -.
DR BioGRID; 4262704; 126.
DR BioGRID; 852977; 1.
DR DIP; DIP-12572N; -.
DR IntAct; P31806; 9.
DR STRING; 511145.b4167; -.
DR jPOST; P31806; -.
DR PaxDb; P31806; -.
DR PRIDE; P31806; -.
DR EnsemblBacteria; AAC77124; AAC77124; b4167.
DR EnsemblBacteria; BAE78168; BAE78168; BAE78168.
DR GeneID; 66671920; -.
DR GeneID; 948685; -.
DR KEGG; ecj:JW4125; -.
DR KEGG; eco:b4167; -.
DR PATRIC; fig|511145.12.peg.4298; -.
DR EchoBASE; EB1708; -.
DR eggNOG; COG0062; Bacteria.
DR eggNOG; COG0063; Bacteria.
DR HOGENOM; CLU_024853_4_3_6; -.
DR InParanoid; P31806; -.
DR OMA; HNGGDAL; -.
DR PhylomeDB; P31806; -.
DR BioCyc; EcoCyc:EG11758-MON; -.
DR BioCyc; MetaCyc:EG11758-MON; -.
DR BRENDA; 5.1.99.6; 2026.
DR PRO; PR:P31806; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052856; F:NADHX epimerase activity; IDA:EcoCyc.
DR GO; GO:0052857; F:NADPHX epimerase activity; IDA:EcoCyc.
DR GO; GO:0110051; P:metabolite repair; IDA:EcoCyc.
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 Gene3D; 3.40.50.10260; -; 1.
DR HAMAP; MF_01965; NADHX_dehydratase; 1.
DR HAMAP; MF_01966; NADHX_epimerase; 1.
DR InterPro; IPR017953; Carbohydrate_kinase_pred_CS.
DR InterPro; IPR000631; CARKD.
DR InterPro; IPR030677; Nnr.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR Pfam; PF01256; Carb_kinase; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR PIRSF; PIRSF017184; Nnr; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR SUPFAM; SSF64153; SSF64153; 1.
DR TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR PROSITE; PS01049; YJEF_C_1; 1.
DR PROSITE; PS01050; YJEF_C_2; 1.
DR PROSITE; PS51383; YJEF_C_3; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Isomerase; Lyase; Metal-binding; Multifunctional enzyme; NAD;
KW NADP; Nucleotide-binding; Potassium; Reference proteome.
FT CHAIN 1..515
FT /note="Bifunctional NAD(P)H-hydrate repair enzyme Nnr"
FT /id="PRO_0000119043"
FT DOMAIN 23..225
FT /note="YjeF N-terminal"
FT DOMAIN 234..501
FT /note="YjeF C-terminal"
FT REGION 1..227
FT /note="NAD(P)H-hydrate epimerase"
FT /evidence="ECO:0000250"
FT REGION 71..75
FT /note="NADPHX 1; for epimerase activity"
FT /evidence="ECO:0000250"
FT REGION 139..145
FT /note="NADPHX 1; for epimerase activity"
FT /evidence="ECO:0000250"
FT REGION 235..515
FT /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /evidence="ECO:0000250"
FT REGION 375..381
FT /note="NADPHX 2; for dehydratase activity"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /ligand_label="1"
FT /ligand_note="for epimerase activity"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /ligand_label="2"
FT /ligand_note="for dehydratase activity"
FT /evidence="ECO:0000250"
FT BINDING 412..416
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 432..441
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="(6S)-NADPHX"
FT /ligand_id="ChEBI:CHEBI:64076"
FT /ligand_label="2"
FT /ligand_note="for dehydratase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 515 AA; 54650 MW; 007D569D11E11530 CRC64;
MTDHTMKKNP VSIPHTVWYA DDIRRGEREA ADVLGLTLYE LMLRAGEAAF QVCRSAYPDA
RHWLVLCGHG NNGGDGYVVA RLAKAVGIEV TLLAQESDKP LPEEAALARE AWLNAGGEIH
ASNIVWPESV DLIVDALLGT GLRQAPRESI SQLIDHANSH PAPIVAVDIP SGLLAETGAT
PGAVINADHT ITFIALKPGL LTGKARDVTG QLHFDSLGLD SWLAGQETKI QRFSAEQLSH
WLKPRRPTSH KGDHGRLVII GGDHGTAGAI RMTGEAALRA GAGLVRVLTR SENIAPLLTA
RPELMVHELT MDSLTESLEW ADVVVIGPGL GQQEWGKKAL QKVENFRKPM LWDADALNLL
AINPDKRHNR VITPHPGEAA RLLGCSVAEI ESDRLHCAKR LVQRYGGVAV LKGAGTVVAA
HPDALGIIDA GNAGMASGGM GDVLSGIIGA LLGQKLSPYD AACAGCVAHG AAADVLAARF
GTRGMLATDL FSTLQRIVNP EVTDKNHDES SNSAP
