(data stored in SCRATCH zone)

SWISSPROT: D1CDK0_THET1

ID   D1CDK0_THET1            Unreviewed;       200 AA.
AC   D1CDK0;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 65.
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=Tter_0084 {ECO:0000313|EMBL:ACZ41006.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41006.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41006.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ41006.1; -; Genomic_DNA.
DR   RefSeq; WP_012874041.1; NC_013525.1.
DR   STRING; 525904.Tter_0084; -.
DR   EnsemblBacteria; ACZ41006; ACZ41006; Tter_0084.
DR   KEGG; ttr:Tter_0084; -.
DR   eggNOG; ENOG4105DHP; Bacteria.
DR   eggNOG; COG0717; LUCA.
DR   HOGENOM; HOG000228601; -.
DR   KO; K01494; -.
DR   OMA; GQLCLFR; -.
DR   OrthoDB; 1598407at2; -.
DR   BioCyc; TTER525904:G1GGS-84-MONOMER; -.
DR   UniPathway; UPA00610; UER00667.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CDK0.
DR   SWISS-2DPAGE; D1CDK0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
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:UP000000323}.
FT   DOMAIN       73    158       dUTPase. {ECO:0000259|Pfam:PF00692}.
FT   NP_BIND     104    109       dCTP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00146}.
FT   NP_BIND     130    132       dCTP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00146}.
FT   ACT_SITE    132    132       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     122    122       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     151    151       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     164    164       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     171    171       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     175    175       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   SITE        119    120       Important for bifunctional activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00146}.
SQ   SEQUENCE   200 AA;  21980 MW;  29F6003F1696432A CRC64;
     MILSDTMIID AIKTGWVSFD PPVDIDIQVQ PASVDLRLGN TFRVYNYAQQ AVIDPTEDID
     LDSISQIVRL EDKPFILHPG AFVLGSTMEY VKIPPDLVGR LEGRSSLGRL GVVVHSTAGF
     IDPGFEGNIT LEISNIGKIP VALRAGIRIC QLTLMHTGPV ARPYGPLRGS KYQGQREPTP
     SRIKNDVEFL RRGEIKVGES
//

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