ID A0A890I040_9GAMM Unreviewed; 194 AA. AC A0A890I040; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 25-MAY-2022, entry version 2. DE RecName: Full=dCTP deaminase {ECO:0000256|HAMAP-Rule:MF_00146}; DE EC=3.5.4.13 {ECO:0000256|HAMAP-Rule:MF_00146}; DE AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000256|HAMAP-Rule:MF_00146}; GN Name=dcd {ECO:0000256|HAMAP-Rule:MF_00146, GN ECO:0000313|EMBL:QRH00330.1}; GN ORFNames=JQC75_10460 {ECO:0000313|EMBL:QRH00330.1}; OS Shewanella litorisediminis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=1173586 {ECO:0000313|EMBL:QRH00330.1}; RN [1] {ECO:0000313|EMBL:QRH00330.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SMK1-12 {ECO:0000313|EMBL:QRH00330.1}; RX PubMed=22660951; DOI=10.1007/s10482-012-9754-7; RA Lee M.H., Yoon J.H.; RT "Shewanella litorisediminis sp. nov., a gammaproteobacterium isolated from RT a tidal flat sediment."; RL Antonie Van Leeuwenhoek 102:591-599(2012). RN [2] {ECO:0000313|EMBL:QRH00330.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SMK1-12 {ECO:0000313|EMBL:QRH00330.1}; RA Wang Y., Liu G.; RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00146}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP CC route): step 1/2. {ECO:0000256|HAMAP-Rule:MF_00146}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00146}. CC -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000256|HAMAP- CC Rule:MF_00146}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00146}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP069213; QRH00330.1; -; Genomic_DNA. 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; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00146}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP- KW Rule:MF_00146}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00146}. FT DOMAIN 74..175 FT /note="dUTPase" FT /evidence="ECO:0000259|Pfam:PF00692" FT NP_BIND 110..115 FT /note="dCTP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT NP_BIND 136..138 FT /note="dCTP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT REGION 171..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 138 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 128 FT /note="dCTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 171 FT /note="dCTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 178 FT /note="dCTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 182 FT /note="dCTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" SQ SEQUENCE 194 AA; 21238 MW; 8270AF1B46DE97B3 CRC64; MRLTDFEIEQ ALDAGTILIE PRPSNDAISG VSVDVRLGNQ FRVFQDHTAP FIDLSGPSAE VQAALDRVMS DKIDIKDGNA FFLHPGELAL AVTLESVTLP ADIVGWLDGR SSLARLGLMV HVTAHRIDPG WQGKIVLEFY NSGKLPLALR PGMTIGALNF ERLSGPVSRP YNKRKNAKYK DQQEAVASRI SQDS //