ID A0A0Q7TGR0_9BACL Unreviewed; 865 AA.
AC A0A0Q7TGR0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:KQY94201.1};
GN ORFNames=ASD24_01155 {ECO:0000313|EMBL:KQY94201.1};
OS Paenibacillus sp. Root52.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736552 {ECO:0000313|EMBL:KQY94201.1, ECO:0000313|Proteomes:UP000051734};
RN [1] {ECO:0000313|Proteomes:UP000051734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root52 {ECO:0000313|Proteomes:UP000051734};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY94201.1, ECO:0000313|Proteomes:UP000051734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root52 {ECO:0000313|EMBL:KQY94201.1,
RC ECO:0000313|Proteomes:UP000051734};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQY94201.1}.
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DR EMBL; LMFO01000001; KQY94201.1; -; Genomic_DNA.
DR RefSeq; WP_056690242.1; NZ_LMFO01000001.1.
DR AlphaFoldDB; A0A0Q7TGR0; -.
DR STRING; 1736552.ASD24_01155; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000051734; 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:KQY94201.1}.
FT DOMAIN 18..315
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 788..859
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 865 AA; 96685 MW; 9D867333B34DBC1E CRC64;
MSLFVLDFQE MHTTQLILVG GKGLNLGKLS TVEGVHVPDG FCVTTRAFQL ALEQNDTYPT
LLKQLAMLTL QDRTEIGEVS LKLHQTIMDT AIPSDVTQEV ISHLSKQGME QAYAVRSSAT
AEDLPHASFA GQQDTYLNII GQDAILHHIR KCWASLFTER AVFYRIQNGY NHTHVYCSVV
VQRMISPQAS GIMFTADPVT SNRNVISIDA SFGLGEALVS GIVSADNYKV QGDHIVDKMI
STKKLAIYGL EAGGTETRQI EPDQQRYQTL TDQQMIQLAH IGRQIETYFG CPQDIEWCLA
EDTFYIVQSR PITTLFPIPK VDDADNHVYL SVGHQQMMTD AIKPLGLSFY LLITPALMRK
AGGRLFVDIA PMLSSTAGRQ TLLNNLSSDP LIVGALKTII ERDFITVLPK DHAATPPARR
NTDTLPPFEP DSNIVSELIG RSQTSIDNLQ HNIQDKSGVE LLDFILEDVQ DLKKHLFDPQ
STAVFMAAIN ATAWINENIN EWLGEKNVAD TLTQSVEGNI TSEMGLALLD VADVIRPYPD
VIHYLQQTED DNFLDELVKL DGGQESLDAI EQFLSKYGMR CAGEIDITRP RWSEKPLTLI
PMILGNIKNF EPQAGKHKFE QGLKEALEKE QELINRLKQL PDGEQKAHET KQKIDLVRKF
IGYREYPKYG IVSRYYIYKQ ALLRDAERLV HAGLIQNAED IYYLAYEELH EVVRTNQLDQ
QMIDQRKEDY RLYEKLTPPR VMTSDGEIIT GEYNREHLPV GSIAGLPVSS GVIEGRARVI
LDMNDVDLEA GDILVTSFTD PGWTPLFVSI QGLVTEVGGL MTHGAVIARE YGLPAVVGVE
NATQLIKDGQ RIRVNGTEGY IEILS
//
