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NUDC_PASMU
ID   NUDC_PASMU              Reviewed;         264 AA.
AC   P57965;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=NAD-capped RNA hydrolase NudC {ECO:0000255|HAMAP-Rule:MF_00297};
DE            Short=DeNADding enzyme NudC {ECO:0000255|HAMAP-Rule:MF_00297};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00297};
DE   AltName: Full=NADH pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00297};
DE            EC=3.6.1.22 {ECO:0000255|HAMAP-Rule:MF_00297};
GN   Name=nudC {ECO:0000255|HAMAP-Rule:MF_00297}; OrderedLocusNames=PM1735;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: mRNA decapping enzyme that specifically removes the
CC       nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by
CC       hydrolyzing the diphosphate linkage to produce nicotinamide
CC       mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present
CC       at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing.
CC       Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis
CC       of a broad range of dinucleotide pyrophosphates. {ECO:0000255|HAMAP-
CC       Rule:MF_00297}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC         end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-
CC         nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876,
CC         Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029,
CC         ChEBI:CHEBI:144051; Evidence={ECO:0000255|HAMAP-Rule:MF_00297};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00297};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2
CC         H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC         EC=3.6.1.22; Evidence={ECO:0000255|HAMAP-Rule:MF_00297};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-
CC         ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832,
CC         ChEBI:CHEBI:456215; EC=3.6.1.22; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00297};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00297};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00297};
CC       Note=Divalent metal cations. Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-
CC       Rule:MF_00297};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00297};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00297};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00297}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00297, ECO:0000305}.
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DR   EMBL; AE004439; AAK03819.1; -; Genomic_DNA.
DR   RefSeq; WP_005724685.1; NC_002663.1.
DR   AlphaFoldDB; P57965; -.
DR   SMR; P57965; -.
DR   STRING; 747.DR93_619; -.
DR   EnsemblBacteria; AAK03819; AAK03819; PM1735.
DR   KEGG; pmu:PM1735; -.
DR   PATRIC; fig|272843.6.peg.1757; -.
DR   HOGENOM; CLU_037162_0_1_6; -.
DR   OMA; TWAREHR; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0110153; F:RNA NAD-cap (NMN-forming) hydrolase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00297; Nudix_NudC; 1.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR022925; RNA_Hydrolase_NudC.
DR   InterPro; IPR015376; Znr_NADH_PPase.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF09297; zf-NADH-PPase; 1.
DR   SUPFAM; SSF55811; SSF55811; 2.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; NAD; Reference proteome;
KW   Zinc.
FT   CHAIN           1..264
FT                   /note="NAD-capped RNA hydrolase NudC"
FT                   /id="PRO_0000056971"
FT   DOMAIN          128..252
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   MOTIF           162..183
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         161
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         177
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         177
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         181
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         181
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         195..202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         222
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         222
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00297"
SQ   SEQUENCE   264 AA;  29767 MW;  52F8A97F348620B6 CRC64;
     MNAIQPDDAG YWLLTQDSAL YLINGELPQG KAADFQLQGY NGMIIGELNG RPLWLVEEIA
     DDQRTYFSLR SLLALPEAHF NLLNRGVELN HFFKTHRFCG KCGHPTDLVQ QEWAIQCQNP
     SCSHRTYPVI CPCIIVAVRR GAQILLANHQ RHKGGIYTTL AGFVEVGETF EQAVHREVLE
     ETGIQIQNLR YFGSQPWAFP NSAMIGFLAD YAGGEICVQE MEIHDAQWFD YNAPLPELPP
     KGTIALKLIE HTLQLCAEEE RKAT
 
 
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