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DCD_ECOLI
ID   DCD_ECOLI               Reviewed;         193 AA.
AC   P28248;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=dCTP deaminase {ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000303|PubMed:1324907};
DE            EC=3.5.4.13 {ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000269|PubMed:1324907};
DE   AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000255|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000303|PubMed:1324907};
GN   Synonyms=dus {ECO:0000303|PubMed:1324907}, paxA;
GN   OrderedLocusNames=b2065, JW2050;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP   CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=1324907; DOI=10.1128/jb.174.17.5647-5653.1992;
RA   Wang L., Weiss B.;
RT   "dcd (dCTP deaminase) gene of Escherichia coli: mapping, cloning,
RT   sequencing, and identification as a locus of suppressors of lethal dut
RT   (dUTPase) mutations.";
RL   J. Bacteriol. 174:5647-5653(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
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   [4]
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   [5] {ECO:0007744|PDB:1XS1, ECO:0007744|PDB:1XS4, ECO:0007744|PDB:1XS6}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH DUTP
RP   AND OF MUTANT ALA-138 IN COMPLEXES WITH DCTP AND DUTP, FUNCTION, CATALYTIC
RP   ACTIVITY, ACTIVITY REGULATION, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF
RP   ARG-115 AND GLU-138.
RX   PubMed=15539408; DOI=10.1074/jbc.m409534200;
RA   Johansson E., Fano M., Bynck J.H., Neuhard J., Larsen S., Sigurskjold B.W.,
RA   Christensen U., Willemoes M.;
RT   "Structures of dCTP deaminase from Escherichia coli with bound substrate
RT   and product: reaction mechanism and determinants of mono- and
RT   bifunctionality for a family of enzymes.";
RL   J. Biol. Chem. 280:3051-3059(2005).
RN   [6] {ECO:0007744|PDB:2J4H, ECO:0007744|PDB:2J4Q}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANT ALA-121 IN COMPLEX WITH
RP   DCTP AND OF MUTANT ALA-138 IN COMPLEX WITH DTTP, FUNCTION, CATALYTIC
RP   ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS OF HIS-121 AND
RP   VAL-122.
RX   PubMed=17651436; DOI=10.1111/j.1742-4658.2007.05945.x;
RA   Johansson E., Thymark M., Bynck J.H., Fano M., Larsen S., Willemoes M.;
RT   "Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP
RT   binding to an inactive form of the enzyme.";
RL   FEBS J. 274:4188-4198(2007).
RN   [7] {ECO:0007744|PDB:2V9X}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT ASP-138 IN COMPLEX WITH
RP   DUTP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   ACTIVE SITE, AND MUTAGENESIS OF SER-111; ARG-115 AND GLU-138.
RX   PubMed=17996716; DOI=10.1016/j.abb.2007.10.013;
RA   Thymark M., Johansson E., Larsen S., Willemoes M.;
RT   "Mutational analysis of the nucleotide binding site of Escherichia coli
RT   dCTP deaminase.";
RL   Arch. Biochem. Biophys. 470:20-26(2008).
CC   -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP.
CC       {ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000269|PubMed:1324907,
CC       ECO:0000269|PubMed:15539408, ECO:0000269|PubMed:17651436,
CC       ECO:0000269|PubMed:17996716}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCTP + H(+) + H2O = dUTP + NH4(+); Xref=Rhea:RHEA:22680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:61481, ChEBI:CHEBI:61555; EC=3.5.4.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00146,
CC         ECO:0000269|PubMed:1324907, ECO:0000269|PubMed:15539408,
CC         ECO:0000269|PubMed:17651436, ECO:0000269|PubMed:17996716};
CC   -!- ACTIVITY REGULATION: Inhibited by dTTP, which binds to the active site
CC       and stabilizes the inactive form of the enzyme (PubMed:17651436).
CC       Inhibited by inorganic phosphate (PubMed:15539408).
CC       {ECO:0000269|PubMed:15539408, ECO:0000269|PubMed:17651436}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Note=kcat is 1.24 sec(-1). {ECO:0000269|PubMed:17996716};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 1/2. {ECO:0000255|HAMAP-Rule:MF_00146,
CC       ECO:0000269|PubMed:1324907}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00146,
CC       ECO:0000269|PubMed:15539408, ECO:0000269|PubMed:17651436,
CC       ECO:0000269|PubMed:17996716}.
CC   -!- DISRUPTION PHENOTYPE: Mutant accumulates dCTP.
CC       {ECO:0000269|PubMed:1324907}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00146, ECO:0000305}.
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DR   EMBL; M90069; AAA23669.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75126.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15918.1; -; Genomic_DNA.
DR   PIR; A42940; A42940.
DR   RefSeq; NP_416569.1; NC_000913.3.
DR   RefSeq; WP_001234768.1; NZ_LN832404.1.
DR   PDB; 1XS1; X-ray; 1.80 A; A/B/C/D/E/F=1-193.
DR   PDB; 1XS4; X-ray; 2.53 A; A/B/C/D/E/F=1-193.
DR   PDB; 1XS6; X-ray; 2.00 A; A/B/C/D/E/F=1-193.
DR   PDB; 2J4H; X-ray; 2.70 A; A/B=1-193.
DR   PDB; 2J4Q; X-ray; 2.60 A; A/B=1-193.
DR   PDB; 2V9X; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-193.
DR   PDBsum; 1XS1; -.
DR   PDBsum; 1XS4; -.
DR   PDBsum; 1XS6; -.
DR   PDBsum; 2J4H; -.
DR   PDBsum; 2J4Q; -.
DR   PDBsum; 2V9X; -.
DR   AlphaFoldDB; P28248; -.
DR   SMR; P28248; -.
DR   BioGRID; 4259684; 5.
DR   IntAct; P28248; 2.
DR   STRING; 511145.b2065; -.
DR   DrugBank; DB03258; 2'-Deoxycytidine 5'-triphosphate.
DR   DrugBank; DB02333; Deoxyuridine-5'-Triphosphate.
DR   jPOST; P28248; -.
DR   PaxDb; P28248; -.
DR   PRIDE; P28248; -.
DR   EnsemblBacteria; AAC75126; AAC75126; b2065.
DR   EnsemblBacteria; BAA15918; BAA15918; BAA15918.
DR   GeneID; 946593; -.
DR   KEGG; ecj:JW2050; -.
DR   KEGG; eco:b2065; -.
DR   PATRIC; fig|1411691.4.peg.186; -.
DR   EchoBASE; EB1389; -.
DR   eggNOG; COG0717; Bacteria.
DR   HOGENOM; CLU_087476_2_0_6; -.
DR   InParanoid; P28248; -.
DR   OMA; PPIERIN; -.
DR   PhylomeDB; P28248; -.
DR   BioCyc; EcoCyc:DCTP-DEAM-MON; -.
DR   BioCyc; MetaCyc:DCTP-DEAM-MON; -.
DR   BRENDA; 3.5.4.13; 2026.
DR   UniPathway; UPA00610; UER00665.
DR   EvolutionaryTrace; P28248; -.
DR   PRO; PR:P28248; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR   GO; GO:0008829; F:dCTP deaminase activity; IDA:EcoCyc.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006229; P:dUTP biosynthetic process; IDA:EcoCyc.
DR   GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IMP:EcoCyc.
DR   GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   HAMAP; MF_00146; dCTP_deaminase; 1.
DR   InterPro; IPR011962; dCTP_deaminase.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR02274; dCTP_deam; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Nucleotide metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..193
FT                   /note="dCTP deaminase"
FT                   /id="PRO_0000155984"
FT   ACT_SITE        138
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17996716"
FT   BINDING         110..115
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17651436,
FT                   ECO:0000305|PubMed:17996716"
FT   BINDING         124..128
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000305|PubMed:15539408,
FT                   ECO:0000305|PubMed:17651436, ECO:0000305|PubMed:17996716"
FT   BINDING         136..138
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17651436,
FT                   ECO:0000305|PubMed:17996716"
FT   BINDING         171..174
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000305|PubMed:15539408,
FT                   ECO:0000305|PubMed:17996716"
FT   BINDING         178
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17996716"
FT   BINDING         182
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17996716"
FT   MUTAGEN         111
FT                   /note="S->C: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17996716"
FT   MUTAGEN         111
FT                   /note="S->T: 30-fold decrease in kcat. Shows altered dTTP
FT                   inhibition."
FT                   /evidence="ECO:0000269|PubMed:17996716"
FT   MUTAGEN         115
FT                   /note="R->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:15539408"
FT   MUTAGEN         115
FT                   /note="R->Q: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17996716"
FT   MUTAGEN         121
FT                   /note="H->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17651436"
FT   MUTAGEN         122
FT                   /note="V->G: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17651436"
FT   MUTAGEN         138
FT                   /note="E->A,Q: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:15539408"
FT   MUTAGEN         138
FT                   /note="E->D: 140-fold decrease in kcat. Shows altered dTTP
FT                   inhibition."
FT                   /evidence="ECO:0000269|PubMed:17996716"
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          15..21
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:2J4Q"
FT   HELIX           58..68
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          89..98
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   HELIX           111..114
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          132..141
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          153..162
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:1XS1"
FT   HELIX           190..192
FT                   /evidence="ECO:0007829|PDB:1XS1"
SQ   SEQUENCE   193 AA;  21249 MW;  B0044051ADE7F919 CRC64;
     MRLCDRDIEA WLDEGRLSIN PRPPVERING ATVDVRLGNK FRTFRGHTAA FIDLSGPKDE
     VSAALDRVMS DEIVLDEGEA FYLHPGELAL AVTLESVTLP ADLVGWLDGR SSLARLGLMV
     HVTAHRIDPG WSGCIVLEFY NSGKLPLALR PGMLIGALSF EPLSGPAVRP YNRREDAKYR
     NQQGAVASRI DKD
 
 
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