NNR_HELPY
ID NNR_HELPY Reviewed; 466 AA.
AC P56176;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
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; OrderedLocusNames=HP_1363;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of a carbohydrate kinase (YjeF family) from Helicobacter
RT pylori.";
RL Submitted (DEC-2009) to the PDB data bank.
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 (By similarity).
CC {ECO:0000250}.
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 -!- 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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000250};
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; AE000511; AAD08403.1; -; Genomic_DNA.
DR PIR; C64690; C64690.
DR RefSeq; NP_208155.1; NC_000915.1.
DR RefSeq; WP_000954017.1; NC_018939.1.
DR PDB; 3K5W; X-ray; 2.60 A; A=2-466.
DR PDBsum; 3K5W; -.
DR AlphaFoldDB; P56176; -.
DR SMR; P56176; -.
DR STRING; 85962.C694_07035; -.
DR PaxDb; P56176; -.
DR EnsemblBacteria; AAD08403; AAD08403; HP_1363.
DR KEGG; hpy:HP_1363; -.
DR PATRIC; fig|85962.47.peg.1460; -.
DR eggNOG; COG0062; Bacteria.
DR eggNOG; COG0063; Bacteria.
DR OMA; ALECEIT; -.
DR PhylomeDB; P56176; -.
DR EvolutionaryTrace; P56176; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0052857; F:NADPHX epimerase activity; IBA:GO_Central.
DR GO; GO:0110051; P:metabolite repair; IBA:GO_Central.
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; 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 3D-structure; ATP-binding; Isomerase; Lyase; Metal-binding;
KW Multifunctional enzyme; NAD; NADP; Nucleotide-binding; Potassium;
KW Reference proteome.
FT CHAIN 1..466
FT /note="Bifunctional NAD(P)H-hydrate repair enzyme Nnr"
FT /id="PRO_0000119044"
FT DOMAIN 8..207
FT /note="YjeF N-terminal"
FT DOMAIN 215..466
FT /note="YjeF C-terminal"
FT REGION 1..207
FT /note="NAD(P)H-hydrate epimerase"
FT /evidence="ECO:0000250"
FT REGION 56..60
FT /note="NADPHX 1; for epimerase activity"
FT /evidence="ECO:0000250"
FT REGION 124..130
FT /note="NADPHX 1; for epimerase activity"
FT /evidence="ECO:0000250"
FT REGION 215..466
FT /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT /evidence="ECO:0000250"
FT REGION 342..348
FT /note="NADPHX 2; for dehydratase activity"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 151
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 154
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 300
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 385..389
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 404..413
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 414
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 STRAND 2..6
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3K5W"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:3K5W"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:3K5W"
FT TURN 350..353
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 371..376
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:3K5W"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 430..443
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:3K5W"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:3K5W"
SQ SEQUENCE 466 AA; 50737 MW; 52125FE79BA8F056 CRC64;
MLSVYEKVNA LDKRAIEELF LSEDILMENA AMALERAVLQ NASLGAKVII LCGSGDNGGD
GYALARRLVG RFKTLVFEMK LAKSPMCQLQ QERAKKAGVV IKAYEENALN QNLECDVLID
CVIGSHFKGK LEPFLNFESL SQKARFKIAC DIPSGIDSKG RVDKGAFKAD LTISMGAIKS
CLLSDRAKDY VGELKVGHLG VFNQIYEIPT DTFLLEKSDL KLPLRDRKNA HKGDYGHAHV
LLGKHSGAGL LSALSALSFG SGVVSVQALE CEITSNNKPL ELVFCENFPN LLSAFALGMG
LENIPKDFNK WLELAPCVLD AGVFYHKEVL QALEKEVILT PHPKEFLSLL KLVGINISML
ELLDNKLEIA RDFSQKYPKV VLLLKGANTL IAHQGQVFIN ILGSVALAKA GSGDVLAGLI
LSLLSQNYTP LDAAINASSA HALASLEFKN NYALTPLDLI EKIKQL
