ID A0A0D0F2G3_9SPHI Unreviewed; 871 AA.
AC A0A0D0F2G3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:KIO75753.1};
GN ORFNames=TH53_18895 {ECO:0000313|EMBL:KIO75753.1};
OS Pedobacter lusitanus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1503925 {ECO:0000313|EMBL:KIO75753.1, ECO:0000313|Proteomes:UP000032049};
RN [1] {ECO:0000313|EMBL:KIO75753.1, ECO:0000313|Proteomes:UP000032049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL19 {ECO:0000313|EMBL:KIO75753.1,
RC ECO:0000313|Proteomes:UP000032049};
RA Santos T., Caetano T., Covas C., Cruz A., Mendo S.;
RT "Draft genome sequence of Pedobacter sp. NL19 isolated from sludge of an
RT effluent treatment pond in an abandoned uranium mine.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIO75753.1}.
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DR EMBL; JXRA01000085; KIO75753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0F2G3; -.
DR STRING; 1503925.TH53_18895; -.
DR Proteomes; UP000032049; 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:KIO75753.1}.
FT DOMAIN 22..320
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"
FT REGION 417..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 97991 MW; 1BCA53D473776ED2 CRC64;
MRQKKGNTYL ICFQETDRSG VMLVGGKGAN LGELSRINEI QVPEGFCITT KAYKKITRNN
QEFNNLLDEL IQLKTEERKS ITTISAKIRT VIESTPIPKE ITGEILYYLT KFDRKTAFAV
RSSATAEDLP AASFAGQQDT YLNIIGKEEI LKHISKCWAS LFTERAVIYR LQNGFDHRKV
QLSVIIQQMV FPEAAGIMFT ADPVTSNRKV LSIDASFGLG EAMVSGLVNT DLYKVCNSTI
TEKKISTKKL AVHALKGGGT KEQEIEPQWQ NKQVLTDRQI LQLEQTGRKI EAHFGQPQDI
EWCLADELFY IVQSRPITTL YPIPEVNDNE NHVFVSVGHN QMMTDAMKPL GLSFFLSATF
GPMHQAGGRL FVDITARLAS AESRKTIMNT LGKSDLLIKD ALITIIEREG FIKFAPDDKN
KDDKTVSPAS LKPQPENGPA IVSDLIQHSR ASIEELKLNI RTKSGVELFD FIQEDIPQLR
KTLFAPQSLN VIMNAIDASF WINEKMNEWL GEKNAADILS QSVPNNITSE MGLELLNVAD
IIRPYPAVTA YLQQVKEDDF LEELTRFDGG KQALDAINAY LNKYGMRCTG EIDITRMRWS
EKPLTLVPAI LNNIKNFEPG AGRQRFEQGL QEALKKEKYL LERLSQLEDG KEKARETKQK
ISLIRSTIGY REYPKYGMVN RYFIYKQALL KEAEQLLQAN IIQQKEDIYY LTIEEFREAV
RTGKPDYRII NARKEEYKLY EKLSPPRVIT SDGEIITGKY RCENLPDGAI AGLAVSSGII
EGRARVILNI EDAELEDGDI LVTSFTDPSW TPLFVSIKGL VTEVGGLMTH GAVIAREYGL
PAIVGVENAT RLIKDGQRIR VNGTDGYIEI L
//
