ID   A0A1I2XRA9_9FIRM        Unreviewed;       901 AA.
AC   A0A1I2XRA9;
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:SFH15246.1};
GN   ORFNames=SAMN05660649_04073 {ECO:0000313|EMBL:SFH15246.1};
OS   Desulfotruncus arcticus DSM 17038.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfotruncus.
OX   NCBI_TaxID=1121424 {ECO:0000313|EMBL:SFH15246.1, ECO:0000313|Proteomes:UP000199337};
RN   [1] {ECO:0000313|Proteomes:UP000199337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17038 {ECO:0000313|Proteomes:UP000199337};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOOX01000018; SFH15246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2XRA9; -.
DR   STRING; 341036.SAMN05660649_04073; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000199337; 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:SFH15246.1};
KW   Pyruvate {ECO:0000313|EMBL:SFH15246.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199337};
KW   Transferase {ECO:0000313|EMBL:SFH15246.1}.
FT   DOMAIN          22..339
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          822..890
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   901 AA;  100596 MW;  EEB2AB0EAD92FC7E CRC64;
     MDSGEEKLFL RWDEAFRAGP EAAGGKGWNL GRLDRYGFDL PAGGVLSTLA YGIFIEANKL
     QESLEDVSRS STAEKITNPE ITLILDNMRG KINNGIFPPI VRKALARRLK KLGLWEKPVA
     VRSSASAEDS QKASFAGMHD SFLNVKGLDN ILESVKACYA SLWTPRAVAY RRKMNISDNK
     VLPAVVIMQM VEARAAGIAF SCDPRTGRED LLVINANYGL GESVVGGLVE PDQYLLDTTD
     IQHKIKGTVI GSKKTVTIPA DCGGTMLVTE KDSKWFELQE KMQSKQVLSN IEITRLGLII
     LRVLDSLGEG ECHQDIEWAL DGEKFYLVQA RPVTALPQYT YPAIKSQPEI WSNANTRDAL
     PVVLSTLAHR DNKIILTKMM DGFYKYLGVQ QLPGIQRFKC FNGRLYANMS VFQWEAYKYY
     AMTPAESNHH MGGHQQEITI PENQKHGRAS LLKIKLLHFK LVFLLNRLRK KVASSSANIR
     SYTDEMRGKD LTLVEDKDLL NYFMDLAQTT YTYSPMVPLF NLFAGGTMMT LTGVLENYFP
     TESKALISYL MAGAGNITSA THGYRLIELA ELAGKDPDAL MFFTSASYNP LNWEYALPDN
     TPFKQVFKGY IKDFGHRAVY EADTINPRWR ENPSYLLNTV KTLLDNANTA SIKAGQEKKR
     KTSWDRINTK LPFYLKVLVK YLVSQLIENS EMREMTKSEI IRLAEVHRKI CLEIAGRLVK
     WGLLTERNDI FHCSWYDIIP ILTDDWDGRG LQNLVSDRKK RRKELEALSP PDLIINDTPV
     YSTPLARGPG DTLEGLGVAA GKASGQARIV MHPEEGKKLG CGEVLAAPST DPAWTPLFLK
     ASAIVMETGG FLSHGAIVAR EYGIPAVVNI PGVLKLVQDG QETTVDGDEG KIYLKPIHEN
     N
//