ID A0A1H3ASN3_9ACTN Unreviewed; 875 AA.
AC A0A1H3ASN3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:SDX32653.1};
GN ORFNames=SAMN05660209_00169 {ECO:0000313|EMBL:SDX32653.1};
OS Geodermatophilus africanus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137993 {ECO:0000313|EMBL:SDX32653.1, ECO:0000313|Proteomes:UP000198921};
RN [1] {ECO:0000313|EMBL:SDX32653.1, ECO:0000313|Proteomes:UP000198921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45422 {ECO:0000313|EMBL:SDX32653.1,
RC ECO:0000313|Proteomes:UP000198921};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNOT01000001; SDX32653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3ASN3; -.
DR STRING; 1137993.SAMN05660209_00169; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000198921; 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:SDX32653.1};
KW Pyruvate {ECO:0000313|EMBL:SDX32653.1};
KW Transferase {ECO:0000313|EMBL:SDX32653.1}.
FT DOMAIN 31..242
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 248..296
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 795..866
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 875 AA; 91531 MW; 8BFF7F4138338160 CRC64;
MDTAPQSTRP RTGRHPVVVP LGDLDAGDLA LAGGKAANLG ELIGAGFPVP DGFCVTTDAY
AELAEAAGLA DLLDDPAADL ARTARERILA APVPASVAEA VAAAYAELGE SVPVAVRSSA
TAEDLPFASF AGQQDTYLDV VGTDAVLDAV HRCWASLWTD RAVVYRARNG VDSATTRLAV
VVQRMVDAAV AGVMFTANPV TGRRTETVVD AAPGLGEAVV SGSVDPDHVV LDSTTGAVLE
RRPGGGREAC LTDGQLRELV RLGARVQEHY GRPQDTEWAI DAAGTLWLTQ ARPVTTLFPV
PQGGAGDGGL RVWFCASLAQ GLTRPLTPMG ISVFQVVGGS VQRLAGLPPA DPVAGSPRVR
AAAGRLFFDV TTIVRSTAGR AIFPRLLDVM EARSAVVLRE LFDDPRLSLV HRSWLPVVRR
LARVAARYGV PLQVVQALVR PAAARRRVDR VGARLRARRL PGDEAPAAER YDAVLGLLGD
AMPAVAPRVL PPAAAGFAAW GLAGKLLGDA ARPGELGTVL RGLPHNVTTE MDLGLWRLAT
AVRADEPSAA AVRGGTPADL AERYRSGALP AVLQRGLRVF LARYGIRAVA EIDVGVPRWA
EDPAHLLGVL GNYLRLDDPD RAPDVVFARS VAEAEDVVAT LTARARLRGR ARGAVVGLAL
DRTRQLAGLR ELPKYDLVLV LDRVRTLLTS IGADLASDGV LARADDVFFL SLAEVRDALD
DGRPLRDVVT ERRRSHEREM ARRHVPRVLL SDGTEPEAVS AGPAVAEGAL VGTAASAGTM
TGRARVVLEP TGAHLEPGEV LVAPSTDPGW TPLFLTAGGL VMEMGGANSH GAVVAREYGI
PAVVGVPGAT SRLATGQEVT VDGTRGVVTA GAAPD
//