ID   A0A1H1ZYF2_9ACTN        Unreviewed;       811 AA.
AC   A0A1H1ZYF2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:SDT38442.1};
GN   ORFNames=SAMN04488543_4076 {ECO:0000313|EMBL:SDT38442.1};
OS   Friedmanniella luteola.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Friedmanniella.
OX   NCBI_TaxID=546871 {ECO:0000313|EMBL:SDT38442.1, ECO:0000313|Proteomes:UP000199092};
RN   [1] {ECO:0000313|EMBL:SDT38442.1, ECO:0000313|Proteomes:UP000199092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21741 {ECO:0000313|EMBL:SDT38442.1,
RC   ECO:0000313|Proteomes:UP000199092};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT629749; SDT38442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1ZYF2; -.
DR   STRING; 546871.SAMN04488543_4076; -.
DR   Proteomes; UP000199092; Chromosome i.
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; 2.
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; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SDT38442.1};
KW   Pyruvate {ECO:0000313|EMBL:SDT38442.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199092};
KW   Transferase {ECO:0000313|EMBL:SDT38442.1}.
FT   DOMAIN          67..210
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          724..795
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   811 AA;  86139 MW;  DD8234D0996C1A14 CRC64;
     MRGSTSAEDP GPVLVRWLDA TATAAEVGGK GLGLARLTAA GLPVPAGFCL TTAAFARWRS
     DGEPDAVPEP VAAALRQAHR DLAVDVVAVR SSATTEDRAG ASAAGQQDTV LGVRDQDALL
     AAVLTCWRSL RGVRAVAYRA HRGLAEDGGA MAVVVQRQVD ADAAGVAFSL DPVHGDRSAV
     VLEAVPGLGE ALVAGTAAAE EIRVDRATGA VTPPVPVLLT AAEARRLAAL VRRVEEVLDG
     DVDVEWCRAD GELSLVQARP VTAAAPADPW NDSLGGDFLW TSTNVGEAIP DVMTPATWSM
     VQVFLRDAMA TASIPPHVGW GRIGGRVYLN VSVMATLSRV VGVGEQRYRR LTAEVFGRLP
     PELEIPPVPV RRLAVLAAVV PMALHVLGEA RRDARRLDGY LADHHARCER RHAEIAAVLE
     PGALGRLWTA VLEPEFHRVS WMLSAATRSS GASFVTTRYR LQRLVGDADA NLLTAATGGR
     AGPLASLGLL DGLDALARGE IDAATFARRY GHRGPHEFEL RWPRPAEDPD WLAGQLAARA
     GDPTHRDRLR AQREARDAAW QRLRAAHPVR ARLLGRALTR WGRIARDRER ARSEVIRYFG
     VLRAFTLRAG ELTGLGDDVF FLELPELLRA LAGEPPAARL AAGRRAVHAA YSALPPYPGL
     IRGRFDPFRW AADPDRRADL FLPSPRPEPV GGPADVAVRG FPGSAGVVEG PVRVLTDPDR
     ADALRPGEVL VTPVTNVGWT PYFPRAAAVV TDVGAPLSHA AIVARELGIP AVVGCGNATT
     LLRTGDRVRV DGAAGTVERL GPDRAVSPGS S
//