ID A0A0Q9TWB0_9BACL Unreviewed; 864 AA.
AC A0A0Q9TWB0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:KRF43778.1};
GN ORFNames=ASG93_02355 {ECO:0000313|EMBL:KRF43778.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF43778.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF43778.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF43778.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF43778.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF43778.1,
RC ECO:0000313|Proteomes:UP000051948};
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:KRF43778.1}.
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DR EMBL; LMSP01000001; KRF43778.1; -; Genomic_DNA.
DR RefSeq; WP_056828422.1; NZ_LMSP01000001.1.
DR AlphaFoldDB; A0A0Q9TWB0; -.
DR STRING; 1736411.ASG93_02355; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000051948; 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:KRF43778.1}.
FT DOMAIN 18..316
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 864 AA; 96962 MW; 350FE33A0883E99A CRC64;
MSTLVLGFQG MEKTQLWLVG GKGLNLGELS KIQGIQVPEG FCVTTVGYQK AIEQNETYHA
LLDRLTMLKV EDRDQIGEIS RKIRQIVTEV EIPSDVVKAV AHYLSQFGEE HAYAVRSSAT
AEDLPHASFA GQQDTYLNII GKDAILQHIS KCWASLFTDR AVIYRMQNGF DHSQVYLSVI
IQRMVFPRAS GILFTADPIT SNRKLLSIDA SFGLGEALVS GLVSADCYQV QEEEIVEKRI
ATKKLAIYGR EEGGTETKQV DPDQQMSQTL TEQQILQLAR IGRQIEAYFG CPQDIEWCLT
DDTFYIVQSR PITTLYPIPE ANDQKNHVYL SVGHQQMMTA PIKPLGLSFY LLITPAPMRK
AGGRLFVDVA PRLATPVGRE TLLNTVGSDP LIKGALMTII ERDFIKLLPN DQTAPIPGRS
NTDMLAQFEN DPTIVSDLIK RSQTSIEELK QNIQVKSGSD LFDFILEDIQ QLKKILFDPQ
SSAVFMAAIN ATSWINENMN EWLGEKNAAD TLSQSVPGNI TSEMGLALLD VADVVRSYQE
VIDFLQHVKD DNFLDELVKF DGGQKIQDAI YAYLNKYGMR CAGEIDITKT RWSEKPITLV
PMILGNIKNF EPNAGHRKFE QGRQEALDKE QELIDRLKQL PDSEQKAKET KRMISLIRNF
IGYREYPKYG MINRYFVYKQ ALLKEAEQLV QAGVIHEKED IYYLSFEELH EVVRTNKLDY
QIINKRKDDY KFFEKLTPPR VITSDGEIIA GEYKRENLPA NAIVGLPVSS GVIEGRARVI
LNMEEAALSD GDILVTSFTD PGWTPLFVSI KGLVTEVGGL MTHGAVIARE YGLPAVVGVE
NATKLIKDGQ RIRVHGTEGY IEIL
//
