ID   A0A1W2DYZ6_9FIRM        Unreviewed;       878 AA.
AC   A0A1W2DYZ6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:SMD02669.1};
GN   ORFNames=SAMN04488500_11923 {ECO:0000313|EMBL:SMD02669.1};
OS   Sporomusa malonica.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=112901 {ECO:0000313|EMBL:SMD02669.1, ECO:0000313|Proteomes:UP000192738};
RN   [1] {ECO:0000313|EMBL:SMD02669.1, ECO:0000313|Proteomes:UP000192738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5090 {ECO:0000313|EMBL:SMD02669.1,
RC   ECO:0000313|Proteomes:UP000192738};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FWXI01000019; SMD02669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2DYZ6; -.
DR   STRING; 112901.SAMN04488500_11923; -.
DR   Proteomes; UP000192738; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
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   Pyruvate {ECO:0000313|EMBL:SMD02669.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192738}.
FT   DOMAIN          21..316
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          798..868
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   878 AA;  97562 MW;  6FD5886D703211D7 CRC64;
     MLTIKSFVLF FEHLDRSSLP VVGGKGANLG ELSKAGFPVP GGFCVTTYAY QNFIATSPEM
     NSLLDALNVI DPTDLNRLRE LGEHIRTHLT QLKIPLQIKD EIVHAWASVG EDYSYAIRSS
     ATAEDLPTAS FAGQQDTYLN IRGQHELLRH VRKCWASLFT DRAIAYRAKN GFNHHEVYLS
     VVIQRMVIPE IAGIMFTADP VSGNRTVISI DASFGLGEAI VSGLVSADLY KVKDNTIIQK
     NIAQKKLAIY ALSNGGTVTE ELPAEKQQEH ALADKQILSL VALGKKIEAH FGAPQDIEFC
     VEKGEFFIVQ SRPITSLYPL PDIPYQPLRV LLSFGHVQMA TDAMKPLGIS VLRTIFPASV
     FVEAGGRLFI DLSDLLHSKI VRIILPKILT NADEAMSRAL DEVVKRPEFL AIQPKSDAIA
     SVRKVVAPII KEVWKNFHLR DPKLAKAKVE TYMQERLLKA RQSLCGLQGA KLLQEIQHQL
     DTLMLDVMQN IVTYVAPSII ASRLLQRMLV RWLGNDTELS KLNKSLPGNV TSEMGLQIGD
     LADILRELPE VQEYLKTAKD HTFYTGLVQV AGGNKFKGAF ESFIDKYGMR CPGEIDLTNP
     RWRETPTQLI PAIFSHMRSV KRGEHRLKFS EGAKEAEEAA QCIMDHLEES YFKSKLAQRL
     IKVFRYSGGL REHHKYLLIV IIDVYKQAIM SEAEKLVATG VLQQAEDVYF LTLDELIHLL
     QGDFNYDVSK LVTDRKDRYK WQQNLKPPRV MTSEGEIVIV PQNRGRSPEG ALVGVPVSAG
     IVEGKARIIL RPENAFLSEG EILVAPHTDP GWTPLFQSAK AVITEVGGLM THGAVVAREY
     GIPAVVGVDN ATQLIKDGDL IRVDGNQGIV EFLVTGKP
//