ID   A0A1C5JP59_9ACTN        Unreviewed;       828 AA.
AC   A0A1C5JP59;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Deoxycytidine triphosphate deaminase {ECO:0000313|EMBL:SCG72350.1};
GN   ORFNames=GA0070213_112171 {ECO:0000313|EMBL:SCG72350.1};
OS   Micromonospora humi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=745366 {ECO:0000313|EMBL:SCG72350.1, ECO:0000313|Proteomes:UP000199360};
RN   [1] {ECO:0000313|EMBL:SCG72350.1, ECO:0000313|Proteomes:UP000199360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45647 {ECO:0000313|EMBL:SCG72350.1,
RC   ECO:0000313|Proteomes:UP000199360};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMDM01000012; SCG72350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5JP59; -.
DR   STRING; 745366.GA0070213_112171; -.
DR   OrthoDB; 9780956at2; -.
DR   Proteomes; UP000199360; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}.
FT   DOMAIN          191..393
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
SQ   SEQUENCE   828 AA;  88472 MW;  1C42DFB534D1F19D CRC64;
     MILTGPEISR EQATGRIVIS PFTPEQVNPN SYNFRLGRRL RVYVAAELDP RRPNEFTEID
     IPDEGHVLEP GRLYLAHTEE VLGSEFYAPT FAARSSVARL GLFINLSACL GDIGFVGQWT
     LQLYAVHRVR VYPGMNIGQM MWWRPAGEIA LYDGKYQSSA GPRSSDIHLD LDRQIARGRF
     PGLRTRVEAG TVGNKFARLA WASSRVPVPE AFAVPATELT AAVPADAMRR LQQVFEELRA
     TIGSSFLEST AELADIAGGL RMPPAAREML RTRLTDVFGP EPSARFAVRS SGLAEDSAQA
     SYAGAHLTTL GVTGVDEVIE AVEAGWRSYY AAPAVSARVR AGDFDPQPRL AVVVQRMVDA
     RLAGVAMTGL TGDPERVDVE YREGLGDVLV AGADAALRGN DLAAVPTAHR PVLARVHELV
     GALRAELGED VDVEWAADDA DVYVLQVRPV TATVSRRSSA GPAVEVVRLY TEDPPAGADL
     QEVSDVYAGY VAKRGPAYRL AAAQEVPTAP GWLFGFNAEG LAGEAGAMAL KQALSVGSAA
     ECVLDLGGNL RQIIVDKDEV AARLAEVAEP GHVRYAVVRD FLRGDLGFIS RLSGDGMVVE
     YTPEGLLALN RGTAGAQRVV VRDLAVGLEV PGNVEAPAQA AGLVRHLPTI ARMTSAMQEW
     TGPVTVEWVY ALGQPYFVDF SALHGDVQLL AADDETISAG VAHGPVLRLD DAADDEWLRR
     LSIGPAVSID RSRDVTDHEG LARILGRVAA SPEPAIVYAR RPYAVLAVLI GQVAGFVFEE
     ASALCHLAIL LREARVPAAV TTVPHAAAAT AVVSNGSVTL RRVRGGNA
//