ID   A0A221NRZ4_9ACTN        Unreviewed;       865 AA.
AC   A0A221NRZ4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:ASN22714.1};
GN   ORFNames=LK07_00215 {ECO:0000313|EMBL:ASN22714.1};
OS   Streptomyces pluripotens.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1355015 {ECO:0000313|EMBL:ASN22714.1, ECO:0000313|Proteomes:UP000031501};
RN   [1] {ECO:0000313|EMBL:ASN22714.1, ECO:0000313|Proteomes:UP000031501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 137 {ECO:0000313|EMBL:ASN22714.1,
RC   ECO:0000313|Proteomes:UP000031501};
RA   Ser H.-L., Lee L.-H.;
RT   "Genome sequence of Streptomyces pluripotens MUSC 137T.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP022433; ASN22714.1; -; Genomic_DNA.
DR   RefSeq; WP_039658330.1; NZ_CP022433.1.
DR   AlphaFoldDB; A0A221NRZ4; -.
DR   Proteomes; UP000031501; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
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; 3.50.30.10; 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   Pyruvate {ECO:0000313|EMBL:ASN22714.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031501}.
FT   DOMAIN          18..315
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          788..859
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   865 AA;  95396 MW;  894995F1DB1E2BB5 CRC64;
     MTEPYVLDLQ EIDARQVPVV GGKGAHLSRL SRIEGVRVPA GFCVTTDAFR RIMADAPSID
     DRLDQLSHMD PDDRVVVGTL SAQIRRAIEE IAIPDDLAVA ITRALTRLGE HTAYAVRSSA
     TAEDLPAASS AGQQDSYLNV LGPTAILRHI SRCWASLFTE RAVTYRQRKG IDHRTVHMAV
     VVQQMVFPHA SGTLFTADPV TGNRTVATVD AGFGLGEALV SGLVNPDVFR VREDEVVSRS
     IAAKQRAVRA LPTGGTQESA VDVQQQQQPA LTDAQAVQLV RLGRRIEAHF GRPQDIEWCL
     ADDGFQIVQS RPITTLFPIP DRGDHENHVY VSVGHQQMMT DPMKPLGLSM WQLTAMVPMH
     EAGGRLFVDV TRRLGSPESR AGLLDLMGKG DPLVRDALET VLDREDFVPT SPDPNPAGLP
     AHGASAPIET DPAIVTGLIE RSQTSVAALQ DGIRTKTGPA LFDFLVEAFE EHKRVLGDPL
     NLQAIMAGME ATWWLNDRLQ EWLGEKNAAD TLTLSAPDNI TSEMGLALLD VADVIRPHPE
     VVRFLEGVED EGFLDELVKL AGGAEARDAI EAYLNRYGMR CVGEIDITRP RWRERPTTLV
     PLILDHVRTF EPGAGQRRFE EGRQKARQKE QDVLSRLRAL PGGERKAEET RRMIDRVRTF
     IGYREYPKYT IISRYFVYKQ ALMAEAERLV RAGLLPEKED IFYVTFQELH DVVRSHQVDD
     RLIQQRKDAF RSYHALIPPR VLTSDGEALT GAYRRDDVPA GALIGLPVST GTVDGRARVI
     LDMAKADLEA GDILVTTFTD PSWSPLFVAI AGLVTEVGGL MTHGAVIARE YGLPAVVGVE
     HATRRIRDGQ RIRVHGTDGY IEILS
//