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NUDJ_ECOLI
ID   NUDJ_ECOLI              Reviewed;         153 AA.
AC   P0AEI6; P75965;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Phosphatase NudJ;
DE            EC=3.6.1.-;
GN   Name=nudJ; Synonyms=ymfB; OrderedLocusNames=b1134, JW1120;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
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   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15292217; DOI=10.1074/jbc.m404284200;
RA   Lawhorn B.G., Gerdes S.Y., Begley T.P.;
RT   "A genetic screen for the identification of thiamin metabolic genes.";
RL   J. Biol. Chem. 279:43555-43559(2004).
RN   [5]
RP   FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=16766526; DOI=10.1074/jbc.m603407200;
RA   Xu W., Dunn C.A., O'Handley S.F., Smith D.L., Bessman M.J.;
RT   "Three new Nudix hydrolases from Escherichia coli.";
RL   J. Biol. Chem. 281:22794-22798(2006).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 4-amino-2-methyl-5-
CC       hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-
CC       hydroxymethylpyrimidine phosphate (HMP-P), and hydrolysis of thiamine
CC       pyrophosphate (TPP) to thiamine monophosphate (TMP). Can hydrolyze
CC       other substrates such as MeO-HMP-PP, CF(3)-HMP-PP and MeO-TPP. Is also
CC       a non-specific nucleoside tri- and diphosphatase that releases
CC       inorganic orthophosphate. {ECO:0000269|PubMed:15292217,
CC       ECO:0000269|PubMed:16766526}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + H2O = 4-
CC         amino-2-methyl-5-(phosphooxymethyl)pyrimidine + H(+) + phosphate;
CC         Xref=Rhea:RHEA:27914, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57841, ChEBI:CHEBI:58354;
CC         Evidence={ECO:0000269|PubMed:15292217};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + thiamine diphosphate = H(+) + phosphate + thiamine
CC         phosphate; Xref=Rhea:RHEA:27998, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:37575, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:15292217};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:16766526};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.64 mM for GDP {ECO:0000269|PubMed:16766526};
CC         Vmax=12 umol/min/mg enzyme with GDP as substrate
CC         {ECO:0000269|PubMed:16766526};
CC       pH dependence:
CC         Optimum pH is about 8.5. {ECO:0000269|PubMed:16766526};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16766526}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudJ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC74218.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35956.1; -; Genomic_DNA.
DR   PIR; C64858; C64858.
DR   RefSeq; NP_415652.1; NC_000913.3.
DR   RefSeq; WP_000476093.1; NZ_STEB01000016.1.
DR   AlphaFoldDB; P0AEI6; -.
DR   SMR; P0AEI6; -.
DR   BioGRID; 4263128; 44.
DR   BioGRID; 850061; 1.
DR   DIP; DIP-35908N; -.
DR   IntAct; P0AEI6; 5.
DR   STRING; 511145.b1134; -.
DR   jPOST; P0AEI6; -.
DR   PaxDb; P0AEI6; -.
DR   PRIDE; P0AEI6; -.
DR   EnsemblBacteria; AAC74218; AAC74218; b1134.
DR   EnsemblBacteria; BAA35956; BAA35956; BAA35956.
DR   GeneID; 66670599; -.
DR   GeneID; 945689; -.
DR   KEGG; ecj:JW1120; -.
DR   KEGG; eco:b1134; -.
DR   PATRIC; fig|1411691.4.peg.1132; -.
DR   EchoBASE; EB3220; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_037162_6_1_6; -.
DR   InParanoid; P0AEI6; -.
DR   OMA; QPAGHLD; -.
DR   PhylomeDB; P0AEI6; -.
DR   BioCyc; EcoCyc:G6580-MON; -.
DR   BioCyc; MetaCyc:G6580-MON; -.
DR   PRO; PR:P0AEI6; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0002145; F:4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphatase activity; IEA:RHEA.
DR   GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:EcoCyc.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:EcoCyc.
DR   GO; GO:0016462; F:pyrophosphatase activity; IDA:EcoCyc.
DR   GO; GO:0004787; F:thiamine-diphosphatase activity; IDA:EcoCyc.
DR   CDD; cd03675; Nudix_Hydrolase_2; 1.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR033713; NudJ.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Reference proteome.
FT   CHAIN           1..153
FT                   /note="Phosphatase NudJ"
FT                   /id="PRO_0000057069"
FT   DOMAIN          3..131
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           36..57
FT                   /note="Nudix box"
SQ   SEQUENCE   153 AA;  17433 MW;  BDB7423E97D6735A CRC64;
     MFKPHVTVAC VVHAEGKFLV VEETINGKAL WNQPAGHLEA DETLVEAAAR ELWEETGISA
     QPQHFIRMHQ WIAPDKTPFL RFLFAIELEQ ICPTQPHDSD IDCCRWVSAE EILQASNLRS
     PLVAESIRCY QSGQRYPLEM IGDFNWPFTK GVI
 
 
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