ID   A0A1M7A0P2_PSETH        Unreviewed;       822 AA.
AC   A0A1M7A0P2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Pyruvate, orthophosphate dikinase {ECO:0000313|EMBL:SHL36179.1};
GN   ORFNames=SAMN05443637_12595 {ECO:0000313|EMBL:SHL36179.1};
OS   Pseudonocardia thermophila.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1848 {ECO:0000313|EMBL:SHL36179.1, ECO:0000313|Proteomes:UP000184363};
RN   [1] {ECO:0000313|EMBL:SHL36179.1, ECO:0000313|Proteomes:UP000184363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43832 {ECO:0000313|EMBL:SHL36179.1,
RC   ECO:0000313|Proteomes:UP000184363};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FRAP01000025; SHL36179.1; -; Genomic_DNA.
DR   RefSeq; WP_073460052.1; NZ_FRAP01000025.1.
DR   AlphaFoldDB; A0A1M7A0P2; -.
DR   STRING; 1848.SAMN05443637_12595; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000184363; 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:0050242; F:pyruvate, phosphate dikinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.80.30; -; 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   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR   PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 2.
DR   PIRSF; PIRSF000853; PPDK; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SHL36179.1};
KW   Pyruvate {ECO:0000313|EMBL:SHL36179.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184363};
KW   Transferase {ECO:0000313|EMBL:SHL36179.1}.
FT   DOMAIN          56..283
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          293..343
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          417..498
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   822 AA;  84956 MW;  48003612D1D9186A CRC64;
     MIRATLTFAE ADPADVDRLG GKGAGLARLT QLGLRVPPGY VIATDACRHY LQVGGLPEGL
     ADEVFTRLEE LERASGKAFG SGPVPLLLSV RSGAPISMPG MMDTILNLGI DRRAAVALAQ
     ATGDVRFVAD VVRRFHAMYA ETVLGALDPG QGLEVLAAAV GPDDDPGEVY DRIWAACEKQ
     LQDDCGESVP DDPRAQLLGA VEAVFRSWNT RRARTYRDFH GIPHDLGTAV VVQSMVFGNL
     SADSGSGVVF TRNPVTGAPG LFGEYLAHSQ GEDVVAGIRT PDPVAEALPA PLLEELRTTC
     AELERTYGDV LDIEFTVERS TLYFLQVRSA KRTAEAAVRI AADLAGEGTI APAAALRMVT
     AEQVRQVQRP GFADDDVAEA RAAGRLLTTG IGACPGQVSG KLVLDSDRAK ERAEAGEAVI
     LARPVTSPAD LHGMIAAEGI VTATGGSTSH AAVVARALGT TCVVGASALV VDERARTLVV
     GDRVLPEGSE VSLDGATGEL FEGAFPVATP AAATAALDGL LRIARRSGDS TVLARVTLPA
     DVAPALAAGA DGLVTAVDDV LAATGHIDGL VQSLLDGADD MSAAAFDRIA ELVEEEFTPL
     LAAAGGAEVG IRAIDLVADE ARELLQQTAV TTRHPALSVP LGRPALVAAQ LRGLAAAAAA
     AGGAARPHLA LRHVSDPAEA RALRELAAES GVPVGAYVTS PRGVHHVAEI AAAGDVLWLE
     LRALQAAVFG LPARQLLTAE PLDDYLARGL LTCDPRSSVD PAVVGLLERV AAVRSCPLGL
     RLSGTVSQET AAQLHALGFR RFAVDAAETR PLVLALGRAA AG
//