ID A0A1H1WCV7_9ACTN Unreviewed; 801 AA.
AC A0A1H1WCV7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:SDS94953.1};
GN ORFNames=SAMN04489716_2063 {ECO:0000313|EMBL:SDS94953.1};
OS Actinoplanes derwentensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=113562 {ECO:0000313|EMBL:SDS94953.1, ECO:0000313|Proteomes:UP000198688};
RN [1] {ECO:0000313|EMBL:SDS94953.1, ECO:0000313|Proteomes:UP000198688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43941 {ECO:0000313|EMBL:SDS94953.1,
RC ECO:0000313|Proteomes:UP000198688};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT629758; SDS94953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1WCV7; -.
DR STRING; 113562.SAMN04489716_2063; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000198688; 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; 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:SDS94953.1};
KW Pyruvate {ECO:0000313|EMBL:SDS94953.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198688};
KW Transferase {ECO:0000313|EMBL:SDS94953.1}.
FT DOMAIN 54..188
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 195..242
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 723..794
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 801 AA; 84259 MW; 10A8290C2FE965E1 CRC64;
MSLIVALSEV SVELAYLVGG KAAGLGELIR NGERVPPGFC VTTRAHRSGT LPRAEILAAY
QRLGAGPVAV RSSATAEDLP DASFAGQQDT VLDVTGPDAL LAAVETCWAS LHSARAIAYR
RAHDMDDPTV AMAVIVQRMV DAQAAGVLFT ANPLTGRRTE MLVDAAPGPG SAVVDGAGAA
DHYVLDGSPP DAGGCLTAAH LDELRSVGAR VQTQFGVPQD VEWAIDRQGT TWLLQSRPIT
TLFPAPPATG TEPRVYLEFG HVQGMLQPAT PLGMSTLRTL IAGMLAPLGV RADIVDIGGR
LYGDLTDMAR DPATRGRLVK ILAVDFGPRA QAAMEHVLLD PRFAPRRPTK RGSGAATPSL
RTAGQALAGI SRALARPQAA RARMMRAVDR LRLASAPPPD LRTTADRLCF VQDDDPTDVA
GELTWPIVAG MLAAALPARL LTGVATADEI HTVLAGMPHN VTIEMDLALW RLAQDAATHK
ELLLNTPPDE LAARYLDGEL PEIGLAEFLD TYGHRGAAEV DLGVPRWAED PTPVLAAVAN
YLRLDDPEQA PDRRFARAAA AAEAALPGLI ARARHRRPVR GRLAGFLLRR ARALAGLRES
GKFAGLYRLR AMRAQLLIIG ADLAAGGLLA APGDIVFLTL DEVHTAVHQG ADHRDTVTAR
RRVHQRELRR KTVPVALLSD GTDVEAVLPA AAADDGALIG VGAAAGRATG PARIVDDPAT
ARIEPGEILV AATTDPGWTP LFLTAAALVT ETGAIMAHGP TVAREYGIPA VICVPGVTHR
IRTGQVITVD GATGTVTIDR P
//