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Database: UniProt
Entry: A0A1H3ASN3_9ACTN
LinkDB: A0A1H3ASN3_9ACTN
Original site: A0A1H3ASN3_9ACTN 
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
//
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