ID S4XG56_SORCE Unreviewed; 872 AA.
AC S4XG56;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:AGP32112.1};
GN ORFNames=SCE1572_04785 {ECO:0000313|EMBL:AGP32112.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP32112.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP32112.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP32112.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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DR EMBL; CP003969; AGP32112.1; -; Genomic_DNA.
DR RefSeq; WP_020732951.1; NC_021658.1.
DR AlphaFoldDB; S4XG56; -.
DR STRING; 1254432.SCE1572_04785; -.
DR KEGG; scu:SCE1572_04785; -.
DR PATRIC; fig|1254432.3.peg.1071; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_7; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000014803; Chromosome.
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:AGP32112.1}.
FT DOMAIN 17..315
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 404..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 95644 MW; DCD7DD5763D5A869 CRC64;
MRTYVLDLQE VDRTKAKVVG GKGANLGEVS RIEGIRVPAG FCVTTGAFQR IMGEAPSIGG
LLDRLSSLEA GDRDGIRELS GELRRIIEGT AIPEDLREAL AQALSRLGAG DACAVRSSAT
AEDLPGASFA GQQDTYLNVI GTQAVLQHVR RCWASLFTER AVTYRIQHGF DHRKVHMAVV
VQKMVFAQAA GILFTADPVT SNRKVSSIEA GFGLGEALVS GLASADRYKV RDGQVIEKAI
AKKTLATRAL EEGGTEERAI EPERQGGQVL TDAQILRLER LGRQIEGHFG HPQDIEWCLV
GDELHVVQSR PITTLYPIPE AGDRGNHVYI SVGHQQMMTD PMKPLGLSFF QLAAAGHMVA
AGGRLFVDPT KQLASPASRD ALLKLIGRSD PLIEDALSTI IERGDFIEPS PGDPAASRPG
QGERGAAPSR FGAQVEDDPA IVTALIERAQ AGLEELKRDI RTKTGTALFD FILEDLQRMK
KSMFGPQNMG AIMAAMNASW WLNDKMMEWL GERNAADTLS QSVSNNVTSE MGLALLDVAD
AIRPYPDVVA HLQNVKHDGF LEELVELDGG QQARDAILAY LQKYGMRCAG EIDITRARWS
EKPTTLVPLI LSNIKNFEPH AGKRRFEQGR QEASQRAREL LDRLRQLPDG EQKASEAQRM
ISRLRNFLGY REYPKYAIVN RYFVYKQALL QEAERLAQAD VIHGLEDIYY LTFDELREVV
RTHRLDDQLV SRRRAEHELY KKMTPPRVMT SDGEIVSGAY KRANLPAGAI VGLPVSSGVV
EGRARVLLDM AHADLEAGDI LVTAFTDPSW TPLFVSVKGL VTEVGGMMTH GAVIAREYGL
PAVVSVENAT KLIRDGQRIR VNGTDGVVEI LT
//
