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Database: UniProt
Entry: A0A257B6I0_9BACT
LinkDB: A0A257B6I0_9BACT
Original site: A0A257B6I0_9BACT 
ID   A0A257B6I0_9BACT        Unreviewed;       752 AA.
AC   A0A257B6I0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CFK52_06745 {ECO:0000313|EMBL:OYT71929.1};
OS   Chloracidobacterium sp. CP2_5A.
OC   Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX   NCBI_TaxID=2012633 {ECO:0000313|EMBL:OYT71929.1, ECO:0000313|Proteomes:UP000216393};
RN   [1] {ECO:0000313|EMBL:OYT71929.1, ECO:0000313|Proteomes:UP000216393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP2_5A {ECO:0000313|EMBL:OYT71929.1};
RA   Ward L.M., Mcglynn S.E., Fischer W.;
RT   "Draft genome of Chloracdibacterium sp. CP2_5A, a phototrophic
RT   Acidobacteria from a Japanese hot spring.";
RL   Submitted (JUN-2017) 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:OYT71929.1}.
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DR   EMBL; NKPT01000015; OYT71929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257B6I0; -.
DR   Proteomes; UP000216393; 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; 3.50.30.10; 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;
FT   DOMAIN          80..181
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          660..729
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   752 AA;  82529 MW;  477B08EA14A2C454 CRC64;
     MSSEFIWLGQ SLSASFGVGS KASLLDQATA AGLPVPRGGV LLEAFFALSL REGNLRRTED
     GFAFQDAAAI REALPVLALP PKLAVRSAFS AEDGLSESFA GRFDSVLNVA PDELPDALCK
     VWASSLRHAS PLRRDVLIMA MVEARQAGVA ITEPSHEDDV VNFTPGLADR LVSGAVAGET
     LSLPKLRVFE SPTESGFAGR LQALLREVRR VFGEGSWDVE FADDGRQCWL IQARPLTRPV
     TRNEWFTYAN HREILPPLPS RFMTSLIASC AGDLFDYYRG FDPRLPGDRP FIEVFAGRPF
     INLSLLLDMM RRWGLPTRLV TDSIGGRDVC AQGWRWGRLW RSLPTLLRLG WSQLLAASSA
     QRRIAWLAEV GGAPARSDSF ANCISDLRMA YTALVREMFS LTQAISGPLA ILRRLGALAP
     LAARHETMTT RMFNDLNPLR DYARRHPAVA TSIAQGKVPD DEGFGRLWQA YLDRYGFRGV
     FESDIAQPRY RERPETLLAS LATEPRASSA PPVPWLAWLA LPVWRQARGA LDARERLRHA
     AMQAFDRIRQ RLLRLAVVAR DAGKLPTTDA LWLLEVDELA RLDGDWSVAP DFLAARRREQ
     EADARYDFPD VFRRFDDFSA FGSAALDEPG PRHVQGIGLT RGLVEGRAWV CEAPTLPPPF
     SDPVILVARA VDAGWIAVFS AVAGVVVEIG GDLSHGSIAL REIGLPSVTN ARGATRVIQT
     GDWIRVRADI GSVELVEPAA RSTSLASAPA GE
//
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