DCD_ANAPZ
ID DCD_ANAPZ Reviewed; 185 AA.
AC Q2GLJ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=dCTP deaminase {ECO:0000255|HAMAP-Rule:MF_00146};
DE EC=3.5.4.13 {ECO:0000255|HAMAP-Rule:MF_00146};
DE AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000255|HAMAP-Rule:MF_00146};
GN Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146}; OrderedLocusNames=APH_0130;
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP.
CC {ECO:0000255|HAMAP-Rule:MF_00146}.
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 -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 1/2. {ECO:0000255|HAMAP-Rule:MF_00146}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00146}.
CC -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP-
CC Rule:MF_00146}.
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DR EMBL; CP000235; ABD43468.1; -; Genomic_DNA.
DR RefSeq; WP_011450283.1; NC_007797.1.
DR PDB; 3KM3; X-ray; 2.10 A; A/B=1-185.
DR PDBsum; 3KM3; -.
DR AlphaFoldDB; Q2GLJ4; -.
DR SMR; Q2GLJ4; -.
DR STRING; 212042.APH_0130; -.
DR EnsemblBacteria; ABD43468; ABD43468; APH_0130.
DR GeneID; 56368308; -.
DR KEGG; aph:APH_0130; -.
DR eggNOG; COG0717; Bacteria.
DR HOGENOM; CLU_087476_4_0_5; -.
DR OMA; FENHRYP; -.
DR OrthoDB; 1598407at2; -.
DR UniPathway; UPA00610; UER00665.
DR EvolutionaryTrace; Q2GLJ4; -.
DR Proteomes; UP000001943; Chromosome.
DR GO; GO:0008829; F:dCTP deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006229; P:dUTP biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR SUPFAM; SSF51283; SSF51283; 1.
DR TIGRFAMs; TIGR02274; dCTP_deam; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Nucleotide metabolism; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..185
FT /note="dCTP deaminase"
FT /id="PRO_1000009677"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 107..112
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 131..133
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 152
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 166
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 176
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 40..52
FT /evidence="ECO:0007829|PDB:3KM3"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:3KM3"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3KM3"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3KM3"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:3KM3"
SQ SEQUENCE 185 AA; 20591 MW; CEB4032A48EEE38F CRC64;
MSVMPDHWIK ERALKDGMIS PFVDHKEGTG VLSYGLSSYG YDARLDNKFK IFANTHSVVV
DPKNFSQDSF VDREGDFCII PPNSFMLAKT VEYFNIPRDV MVVCVGKSTY ARCGIVVNVT
PLEPGWSGYV TLEFSNTSPL PVKVYAFEGA CQFLFFSGKE RCSKSYDEAG GKYMGQSDVT
LPIIS
