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
//