ID A0A1H0PNZ8_9ACTN Unreviewed; 802 AA.
AC A0A1H0PNZ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:SDP06308.1};
GN ORFNames=SAMN05216259_116110 {ECO:0000313|EMBL:SDP06308.1};
OS Actinacidiphila guanduensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310781 {ECO:0000313|EMBL:SDP06308.1, ECO:0000313|Proteomes:UP000199341};
RN [1] {ECO:0000313|EMBL:SDP06308.1, ECO:0000313|Proteomes:UP000199341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2022 {ECO:0000313|EMBL:SDP06308.1,
RC ECO:0000313|Proteomes:UP000199341};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNIE01000016; SDP06308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0PNZ8; -.
DR STRING; 310781.SAMN05216259_116110; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000199341; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
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; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SDP06308.1};
KW Pyruvate {ECO:0000313|EMBL:SDP06308.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199341};
KW Transferase {ECO:0000313|EMBL:SDP06308.1}.
FT DOMAIN 61..189
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 208..256
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 616..686
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 695..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 82317 MW; 4D491AEA0A5B2F5F CRC64;
MAIDTGMFAV AALDSEGARD PSVVGAKAAN LARSAAAGLP VLPGFVLVAS DRAPRAPAGH
QALRAAWRQL GGAERPLVVR SSSVHEDTEA SSMAGRFTSV LDVRGWEPFT AAVEQVLDSA
ADPAAEAGED PLHDMAVLVQ PMLSSTAGGV MFGADPVEGR YDHILVSAVD GGPDQLVDGS
TQGVRYQLTR HGRLLRTEPA LPRGRGPLGR QRLNRLVRLA RRTEKVHGAP QDIEFGFDGD
GRLWLFQARP ITAMAARPRR GARLLGPGPV AETLPGVLQP LEEDLWLAPM NRGLALALDI
AGAAPRRKLR RLPVATTVDG RAAADLRLLG AVPPAHPVLT FMNPAPGARR AAAAWRVGRL
RTALPLLARN LMAEVDKQLH DLAEPRQMLG GELLSAVAWG REVLASLHAQ ESLAGALLDT
DTGSTAAGEA LAVLAEGRHG GSTDEELIAH HPVLLALVPP SLDGSASLPA QAGWNGVPRG
IGFLSVREGL RLRIRWVQEM QARMVREMGI RMDERCAAGE RGRIALLRWG ELVTSAEGGA
RPADLAERVP RPRTPPLPAA FRLAGGRPQA VAARPRRRFL GLPGRGEAAG AAGQEGQGAG
GGYGTGTVWD GRGERPAGAV LVTGTLDPAL APLLPGLAGL VAETGSVLSH LAVLAREYGV
PTAVGVPRAL ARFAPGTVVT VDGATGAVRA VPGEPAGSVG SVGASSQAEP LPGGPLADAP
QAGGPSAGGP RPDESLPHGP VPEASLPGGP PPDGLLSDAS LPNGPLPDAS LPSPPPAGDR
TGGLDGADAR GAQGTRAKGA AA
//