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NNR_MYCLE
ID   NNR_MYCLE               Reviewed;         473 AA.
AC   P37391; Q9CCV5;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 127.
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=ML0373; ORFNames=B229_C2_201, u229g;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17298.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U00020; AAA17298.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL583918; CAC29881.1; -; Genomic_DNA.
DR   PIR; E86955; E86955.
DR   PIR; S72984; S72984.
DR   RefSeq; NP_301366.1; NC_002677.1.
DR   RefSeq; WP_010907690.1; NC_002677.1.
DR   AlphaFoldDB; P37391; -.
DR   SMR; P37391; -.
DR   STRING; 272631.ML0373; -.
DR   EnsemblBacteria; CAC29881; CAC29881; CAC29881.
DR   KEGG; mle:ML0373; -.
DR   PATRIC; fig|272631.5.peg.630; -.
DR   Leproma; ML0373; -.
DR   eggNOG; COG0062; Bacteria.
DR   eggNOG; COG0063; Bacteria.
DR   HOGENOM; CLU_024853_4_0_11; -.
DR   OMA; HNGGDAL; -.
DR   Proteomes; UP000000806; 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; 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   3: Inferred from homology;
KW   ATP-binding; Isomerase; Lyase; Metal-binding; Multifunctional enzyme; NAD;
KW   NADP; Nucleotide-binding; Potassium; Reference proteome.
FT   CHAIN           1..473
FT                   /note="Bifunctional NAD(P)H-hydrate repair enzyme Nnr"
FT                   /id="PRO_0000119047"
FT   DOMAIN          10..205
FT                   /note="YjeF N-terminal"
FT   DOMAIN          210..473
FT                   /note="YjeF C-terminal"
FT   REGION          1..203
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /evidence="ECO:0000250"
FT   REGION          62..66
FT                   /note="NADPHX 1; for epimerase activity"
FT                   /evidence="ECO:0000250"
FT   REGION          123..129
FT                   /note="NADPHX 1; for epimerase activity"
FT                   /evidence="ECO:0000250"
FT   REGION          210..473
FT                   /note="ADP-dependent (S)-NAD(P)H-hydrate dehydratase"
FT                   /evidence="ECO:0000250"
FT   REGION          348..354
FT                   /note="NADPHX 2; for dehydratase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
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         155
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
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         382..386
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         402..411
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         412
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   CONFLICT        66..67
FT                   /note="DA -> ES (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  47227 MW;  29569CBBD666C81C CRC64;
     MRHYYSVAAI RDAEASLLAS LPDGVLMKRA AYGLASVIIR ELAVRTGGVT GRRVCAVVGS
     GDNGGDALWA ATFLRRRGAA ADAVLLNPDR VHRKALVAFR KAGGRIVENV SAATDLVIDG
     VVGISGSGPL RPAAAAVFAT VSASGVPVVA VDLPSGIDVV TGVINGPAVH AALTVTFGGL
     KPVHALADCG DVTLVDIGLD LPDSDILGLQ AADVAAYWPV PGVHDDKYTQ GVTGVLAGSS
     TYPGAAVLCT GAAVAATSGM VRYAGSAYTQ VLAHWPEVIA SATPTAAGRV QSWVVGPGLG
     IDATATAALW FALETDLPVL VDADGLTMLA AHPDLVINRN APTVLTPHAS EFARLAGTPP
     GDDRVGACRK LADSFGATVL LKGNVTVIAD PGGPVYLNPA GQSWAATAGS GDVLSGMIGA
     LLAAGLPAAE AAAAAAFVHA RAAALSAADP GPGDVPTSAS RMVSHIRTAL AAL
 
 
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