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Database: UniProt
Entry: A0A0U3EZ59_9ACTN
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ID   A0A0U3EZ59_9ACTN        Unreviewed;       865 AA.
AC   A0A0U3EZ59;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:ALV31503.1};
GN   ORFNames=AS200_05135 {ECO:0000313|EMBL:ALV31503.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV31503.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV31503.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV31503.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP013743; ALV31503.1; -; Genomic_DNA.
DR   RefSeq; WP_058921189.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3EZ59; -.
DR   STRING; 1725411.AS200_05135; -.
DR   KEGG; scx:AS200_05135; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000068029; 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:ALV31503.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068029}.
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"
FT   REGION          406..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  94810 MW;  6847ABD77F1DDF55 CRC64;
     MSEQYVLDLR EVDETRVAVV GGKGAHLGGL ACIEGVRVPG GFCVTTDAFR RMMGRVPSMA
     DRLDELSRLD PGDREGIGTL SARIRGAIEG TAIPDDIAAE LTGALARHGE HAAFAVRSSA
     TAEDLPTASF AGQQDTYLNV VGTQAVLTHI SRCWASLFTE RAVTYRRRNG IDHRTVHMAV
     VVQRMVFPRA AGILFTADPV TGNRKVATVD AGFGLGEALV SGLVNPDVFK VRDGEVIART
     IAAKERAVHA LPDGGTREVA VDARSREQPA LTDEQVLRLV RLGRRVEAHF GRPQDIEWCL
     VDDDFHIVQS RPVTTLFPVP ETDDGENHVY VSVGHQQMMT DAMKPLGLSV WRMTAMAPMH
     EAGGRLFVDV TRQLSSPAGR AALLDLIGRG DPLTRDALES VLDQDGFVPT LPDAGPGGPP
     ARRAPASVET DPAVVTGLIK RNEEFLAALR HDIRGRSGPA LFDFLLEAFE EHKRVLTDPL
     NLPAIMAGME ATWWLNDKLR EWLGEKNAAD TLTLSAPGNV TSEMGLALLD VADAVRPHPQ
     VVAFLQSVED GNFLDDLAGL PGGTEARDAI ETYLDRYGMR CVGEIDITRP RWRERPDTLL
     PLILDNVRNF EPGAARRRFE QGRQRAREKE QEVLSRLRAL PDGDRKADET RRMIDRVRTF
     IGYREYPKYA IVSRYFVYKQ ALLEEAERLV RAGVLRNKED VFYLTLPEFH EAARTMRVDE
     ALVRRREEAF RSYQALTPPR VLTSDGECLD GAYRRDDAPA GALIGLPVSA GTVEGRARVI
     LDMAQADLEA GDILVTACTD PSWSPLFVGI AGLVTEVGGL MTHGAVIARE YGLPAVVGVE
     GATRLIRDGQ RIRVHGTDGY VEILP
//
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