ID   A0A1K1SJI0_9BACT        Unreviewed;       831 AA.
AC   A0A1K1SJI0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:SFW84515.1};
GN   ORFNames=SAMN05661012_05569 {ECO:0000313|EMBL:SFW84515.1};
OS   Chitinophaga sancti.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW84515.1, ECO:0000313|Proteomes:UP000183788};
RN   [1] {ECO:0000313|EMBL:SFW84515.1, ECO:0000313|Proteomes:UP000183788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 784 {ECO:0000313|EMBL:SFW84515.1,
RC   ECO:0000313|Proteomes:UP000183788};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FPIZ01000024; SFW84515.1; -; Genomic_DNA.
DR   RefSeq; WP_072364727.1; NZ_FPIZ01000024.1.
DR   AlphaFoldDB; A0A1K1SJI0; -.
DR   STRING; 1004.SAMN05661012_05569; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000183788; 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; 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   Kinase {ECO:0000313|EMBL:SFW84515.1};
KW   Pyruvate {ECO:0000313|EMBL:SFW84515.1};
KW   Transferase {ECO:0000313|EMBL:SFW84515.1}.
FT   DOMAIN          15..294
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          754..825
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   831 AA;  92403 MW;  CC5D4DC85BCE081E CRC64;
     MILDFREIDH TKLSLAGGKG ANLGELLKID GIQVPEGFCI TTDVYQDLIK DVAIQIDKDN
     IPASCARIRA AIEAQPVPGE IVAVIAKLED LTYAVRSSAT AEDLPNTSFA GQQDTYLNVR
     KQDITQYIRK CWASLFTERA VVYREQHGFD HSKVLLAVVI QKMIFPEVAG IMFTADPVNG
     DRRVVAIDAS FGLGEALVGG LVNADHYKVK GNEIIDRNIG GKHLQVVASK EGGTIQQEIP
     KERQNSPVLT DNECRALNEL GRKIEAHFDQ PQDIEWCLAS GVFYMLQSRP ITTLFPIPSA
     NDSDNHVYLS VGHNQMMTDA MKPLGLSFFL MTTPARMCTA GGRLFIDVAQ QLSQPASREM
     LIGTFGRYDP LFRDALITIV EREGYIKPTG DTVPTRPQLK VENDPAIVAD LMKTTLASIE
     ALKQNIQAQK GVDLFDFIQN DLQALKNNLS NQQSLAVIMA GMEASAWVNE KMFEWLGEKG
     VADIISQSVP DNITSEMGLA LLDVADAILP FPEVIAFLQA EHGEHFLNEL KAINEKAWQA
     IADFLDRYGM RCVGEIDITK TRWREQPGML APLILSNTRN FAPGESKRKF EKGRIEAEHK
     EKELLARLHE EQAAETKEKI CLIRNFIGYR EFPKYAKICR YDIYKQAILK EVEELVQSNI
     IHEKEDIFYL TFDELRELVR THQLDEQLID QRKAEFKVFE KMTPPRVMTS DGEIISSTYD
     RAGLPAHALA GLAVSAGVIE GRARVILNME DASLEEGDIL VTTFTDPSWT PLFVAVKGLV
     TEIGGLMTHG AVIAREYGLP AVVGVANATK IIKDGMRIRV NGTDGYVEVI V
//