(data stored in ACNUC1104 zone)

SWISSPROT: D5US33_TSUPD

ID   D5US33_TSUPD            Unreviewed;       189 AA.
AC   D5US33;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=dCTP deaminase, dUMP-forming {ECO:0000256|HAMAP-Rule:MF_00146};
DE            EC=3.5.4.30 {ECO:0000256|HAMAP-Rule:MF_00146};
DE   AltName: Full=Bifunctional dCTP deaminase:dUTPase {ECO:0000256|HAMAP-Rule:MF_00146};
DE   AltName: Full=DCD-DUT {ECO:0000256|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000256|HAMAP-Rule:MF_00146};
GN   OrderedLocusNames=Tpau_0459 {ECO:0000313|EMBL:ADG77100.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77100.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77100.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes both the deamination
CC       of dCTP to dUTP and the hydrolysis of dUTP to dUMP without
CC       releasing the toxic dUTP intermediate. {ECO:0000256|HAMAP-
CC       Rule:MF_00146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCTP + 2 H2O = diphosphate + dUMP + NH4(+);
CC         Xref=Rhea:RHEA:19205, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61481, ChEBI:CHEBI:246422;
CC         EC=3.5.4.30; Evidence={ECO:0000256|HAMAP-Rule:MF_00146};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP:
CC       step 1/1. {ECO:0000256|HAMAP-Rule:MF_00146}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00146,
CC       ECO:0000256|SAAS:SAAS01039256}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00146, ECO:0000256|SAAS:SAAS00909595}.
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DR   EMBL; CP001966; ADG77100.1; -; Genomic_DNA.
DR   RefSeq; WP_013125142.1; NC_014158.1.
DR   STRING; 521096.Tpau_0459; -.
DR   EnsemblBacteria; ADG77100; ADG77100; Tpau_0459.
DR   KEGG; tpr:Tpau_0459; -.
DR   eggNOG; ENOG4105DHP; Bacteria.
DR   eggNOG; COG0717; LUCA.
DR   HOGENOM; HOG000228601; -.
DR   KO; K01494; -.
DR   OMA; GQLCLFR; -.
DR   OrthoDB; 1598407at2; -.
DR   BioCyc; TPAU521096:G1GKO-442-MONOMER; -.
DR   UniPathway; UPA00610; UER00667.
DR   Proteomes; UP000001213; Chromosome.
DR   GO; GO:0033973; F:dCTP deaminase (dUMP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008829; F:dCTP deaminase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006229; P:dUTP biosynthetic process; IEA:InterPro.
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   3: Inferred from homology;
DR   PRODOM; D5US33.
DR   SWISS-2DPAGE; D5US33.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00146,
KW   ECO:0000256|SAAS:SAAS01087242};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00146,
KW   ECO:0000256|SAAS:SAAS01087248};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00146,
KW   ECO:0000256|SAAS:SAAS01039263};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213}.
FT   DOMAIN       70    177       dUTPase. {ECO:0000259|Pfam:PF00692}.
FT   NP_BIND     101    106       dCTP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00146}.
FT   NP_BIND     127    129       dCTP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00146}.
FT   ACT_SITE    129    129       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     119    119       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     148    148       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     162    162       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     170    170       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     174    174       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   SITE        116    117       Important for bifunctional activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00146}.
SQ   SEQUENCE   189 AA;  20568 MW;  650F975E4CCE1FA8 CRC64;
     MLLSDRDIRA QLDSGRLGIE PFDTQLVQPS SVDVRLDGLF RVFNNTRYTH IDPAQRQDEL
     TSLVEPDPGE PFVLHPGEFV LGSTLEVCSL PDDLAGRLEG KSSLGRLGLL THSTAGFIDP
     GFSGHITLEL SNVANLPITL WPGMKIGQLC LFRLSSPADN PYGSASTGSK YQGQRGPTPS
     KAYLNFQQD
//

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