ID A0A0G1SFS2_9BACT Unreviewed; 517 AA.
AC A0A0G1SFS2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative phosphoenolpyruvate synthase {ECO:0000313|EMBL:KKU68292.1};
GN ORFNames=UX89_C0005G0006 {ECO:0000313|EMBL:KKU68292.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_16.
OC Bacteria.
OX NCBI_TaxID=1618842 {ECO:0000313|EMBL:KKU68292.1, ECO:0000313|Proteomes:UP000034117};
RN [1] {ECO:0000313|EMBL:KKU68292.1, ECO:0000313|Proteomes:UP000034117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU68292.1}.
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DR EMBL; LCNX01000005; KKU68292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1SFS2; -.
DR STRING; 1618842.UX89_C0005G0006; -.
DR PATRIC; fig|1618842.3.peg.308; -.
DR Proteomes; UP000034117; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:KKU68292.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 438..509
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 517 AA; 59290 MW; 83E60CB030C4848A CRC64;
MNNFDQFKKY KWQELAKDYN SPLFRNYIWT AHPFRYPKLF GISRPVIGIV SERNRITYIS
DLTTWKKAHE DLVVKVKKDL MYIDRLIEKT NRLGERMNVW SERELYNKDL SKLSNVQLFK
LYEKTSEWLA ILYAHGVLLP LIDFGEHLFV EDNLKRILSE HVSGEEYSEY YRVFTEPSYD
SFAQDQEIAL TKLWKGFYKD KRCREAVANE SLEEVAEKFP AFHTKLLRHA EKWGWVYYVY
AGPVFGAEQF FGFIKSSLDK GIAPDRFLND LKERRLRNKK AKTLFIKTFK PDTFSKTLLA
LAGKLVWAKP RRKDFQSKTY FHSEKLMQEI GRRIGGFSVA EVRSVPPAFL REVLVENSQI
EKRIAVSAFD MHVCLPCDDG RVEVFTGKDA VTFKDLYLQK EKEIITVGIN EIKGSPACRG
KAQGIVKIIN VPDDMEKMNQ GDVLVSTATT PSIVPAMKKA AAIISDEGGL TCHAAIVSRE
LGTPCVVGTK IATKVLKDGD MVEVDAEKGV VTIIKRG
//
