ID   A0A1I2IY18_9ACTN        Unreviewed;       693 AA.
AC   A0A1I2IY18;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:SFF47402.1};
GN   ORFNames=SAMN05216574_114128 {ECO:0000313|EMBL:SFF47402.1};
OS   Blastococcus sp. DSM 46838.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1798228 {ECO:0000313|EMBL:SFF47402.1, ECO:0000313|Proteomes:UP000198589};
RN   [1] {ECO:0000313|Proteomes:UP000198589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46838 {ECO:0000313|Proteomes:UP000198589};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOND01000014; SFF47402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2IY18; -.
DR   STRING; 1798228.SAMN05216574_114128; -.
DR   Proteomes; UP000198589; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
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; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SFF47402.1};
KW   Pyruvate {ECO:0000313|EMBL:SFF47402.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198589};
KW   Transferase {ECO:0000313|EMBL:SFF47402.1}.
FT   DOMAIN          78..215
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          226..275
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          616..686
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   REGION          10..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  72339 MW;  2B74224A78AEDE48 CRC64;
     MATLLIMQAA STDDGSRTSP PSAGRSVVPL DDETAEQRDV AGAKAAALAT ASRHGLPIVP
     GFVVTTAAVD RIAAGEPLDD EILTAWRGLS QDGRHALVVR SSSTVEDLGD SSMAGRFESV
     VGVTGPDEFR RAVDVVVASR QEAAAGSDTL TGREPLAVLV QPLLDARSGG VLFGIDPVSG
     REDRLVVAAV DGGPDRLVSG EVDGDRYELD RTGRRTDVTR GDGGARLRRS QLRALARLAE
     RTADVFGGPQ DVEWAIDRAG RLRLLQSRPV TAEPRGRPVG PVLGPGPVAE TFPEPLQPLE
     TDLWVRPLRE ALRQALLLAG TAEVSAVEGS PLVTVLGGRV AVDLDLLEPR EETPRLRDRL
     DPRPRLRRLR ASWRVGRLRS ALPALAEDVL GSADHVLGGV PALHELTDRQ LVAVLHRAGP
     ALVSVHAHEV LMGMLVDPAA PRLTGVSAAM RVLARSRGAG LTDTEIVAAN PVVLALAAPR
     ICSFPQLPPD VTAPEGAPPG DGGDAGLLRE ALRLRVRWIQ EVTARVAWTL GERLAATGRL
     PRAEDVRGLR LADLTAAVQD DTLELSPEAV EPEEPLPARF RLGNTGRPIP VSGTAGGTGA
     GGGTGTGPVH IGDDPPDGAV LVVRNLDPSL APVLPRLAGL VAETGSVLAH LAILARESGV
     PTVVGFSGAM DAFAEGTTVR VDGATGAVEE ETS
//