位置:首页 > 蛋白库 > NNR_METKA
NNR_METKA
ID   NNR_METKA               Reviewed;         499 AA.
AC   Q8TX67;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=MK0808;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009439; AAM02022.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TX67; -.
DR   SMR; Q8TX67; -.
DR   STRING; 190192.MK0808; -.
DR   EnsemblBacteria; AAM02022; AAM02022; MK0808.
DR   KEGG; mka:MK0808; -.
DR   PATRIC; fig|190192.8.peg.849; -.
DR   HOGENOM; CLU_024853_4_1_2; -.
DR   OMA; HNGGDAL; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0052857; F:NADPHX epimerase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   ATP-binding; Isomerase; Lyase; Metal-binding; Multifunctional enzyme; NAD;
KW   NADP; Nucleotide-binding; Potassium; Reference proteome.
FT   CHAIN           1..499
FT                   /note="Bifunctional NAD(P)H-hydrate repair enzyme Nnr"
FT                   /id="PRO_0000416429"
FT   DOMAIN          8..213
FT                   /note="YjeF N-terminal"
FT   DOMAIN          217..485
FT                   /note="YjeF C-terminal"
FT   REGION          1..217
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /evidence="ECO:0000250"
FT   REGION          54..58
FT                   /note="NADPHX 1; for epimerase activity"
FT                   /evidence="ECO:0000250"
FT   REGION          128..134
FT                   /note="NADPHX 1; for epimerase activity"
FT                   /evidence="ECO:0000250"
FT   REGION          217..499
FT                   /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT                   /evidence="ECO:0000250"
FT   REGION          360..366
FT                   /note="NADPHX 2; for dehydratase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
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         163
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
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         397..401
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         417..426
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
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   499 AA;  53849 MW;  BBCAEB974F16C75D CRC64;
     MFITSKEMRR IELNSRWLGF EEDFMMENAG AGVARVVIGE YSPNDVLVVC GTGGNGGDGF
     VTARHLDSEG VDVDVLLVGR REAIKNEAAE LNLRRLDRAG IPVQEVRDSE DLESVDFERD
     VVVDALLGFG IRGRLREPVR SAVLRINEAS RAGTRVVSID IPTGLDPDSG ETPDVAVEAD
     LVVSIHRHKR GVRKLRDVFL RRVNAGIPEI AERICGPGDL ITSDIWRRDP WSHKGQHGRV
     LIIGGSRKYV GAPQLAARGA LRAGVDLVFL LTVDAVPKND PNVIYRAVPA ERLEPEHLDE
     VDLEGVDTVV VGPGLGADAD SVGILRELAE SFDGMIIVDA DGLRGISGVN VDDRFVLTPH
     AGEFRREFGE ELGRSLEDRS EAVRRVSEEL GCTILLKGRV DVIGSPDGEI RWNVTGTPAM
     TVGGTGDVLA GVVAGVAARC REGFEAACIG AFVVGSAGCL AERRLSQGLT AEDVAEYVPK
     VLRNPWAAEP EAVTEVRRD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024