ID W7DRW8_9LIST Unreviewed; 845 AA.
AC W7DRW8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:EUJ53157.1};
GN ORFNames=MCOL2_11227 {ECO:0000313|EMBL:EUJ53157.1};
OS Listeria fleischmannii FSL S10-1203.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265822 {ECO:0000313|EMBL:EUJ53157.1, ECO:0000313|Proteomes:UP000019241};
RN [1] {ECO:0000313|EMBL:EUJ53157.1, ECO:0000313|Proteomes:UP000019241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1203 {ECO:0000313|EMBL:EUJ53157.1,
RC ECO:0000313|Proteomes:UP000019241};
RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Novel taxa of Listeriaceae from agricultural environments in the United
RT States.";
RL Submitted (DEC-2012) 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:EUJ53157.1}.
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DR EMBL; AODM01000039; EUJ53157.1; -; Genomic_DNA.
DR RefSeq; WP_036063769.1; NZ_AODM01000039.1.
DR AlphaFoldDB; W7DRW8; -.
DR PATRIC; fig|1265822.4.peg.2275; -.
DR Proteomes; UP000019241; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Pyruvate {ECO:0000313|EMBL:EUJ53157.1}.
FT DOMAIN 18..239
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 770..840
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT COILED 48..82
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 845 AA; 94931 MW; 12BEEF1050BA45E5 CRC64;
MNAFVINLQE INQAALSFVG GKAANLGELT QIKNLNVPEG FCVTTNVYQE IIQQSKEIQQ
TIAELSRMNA TQTEEIKQKS AKLQKLFLNE TIPSEIRSEI SIHLENAGAD ADYAVRSSAT
AEDLPGASFA GQQDTFLNIS GKEAILTHIK KCWASLFNER AILYRMQNGF SENEVQLAVV
VQKMIPAEKS GVLFTADPIS GDRLTTSIDA SVGLGEALVS GQVQADVYQV KNGKVVSQNV
AKSRENPILS EENVLELTVL GREMERYFGY PVDVEWCFFD DAFYIVQCRP ITTLFPLPEN
VHGEKRIYLS VGHQQMMTDP LLPLGMSVYI LTSFGERFIA GGRLFVDVLP RLLDENSRYM
MLDTFDSEPL TKDALITLLK RGDYLDTMYD ETKLLNQKKQ KFMSFPETIK ADATIVKRLT
EESEEALIHL KQDIKAYEGA SLIDFIQQDI LKVKGFLSQK ETMQAIMAAM DSALWLNEKM
FDWLGLVNVS DTLTKSLPDN ITSEMGLALL DVADAIRPYP DIAAFLETTE NKNFIDELPR
FKGGEVVQKA INDYLEIYGM RCPGEIDLTR TRWMEEPEVL IPMILTNLRH FKEGAHEEKH
RKGELEALDK KEELITQLAK LPDGDRKVSE TRQAVDALRH FSGFREYPKY VMVTHYFVYK
QALLKEAEKL VEKGVISEQK DIYFFTLEEL KTIFQTEKMD KDVLYKRKAE YQLYDKLTPP
RVMTADGEIL TGSYHTSDFP KDALPGLAVS SGVVEGRARV ISKMEDAKFY AGEILVTTFT
DPSFTPLFVS AKGLVTEVGG LMTHGAVIAR EYGLPAVVGV TSATELIKDG QMIRIDGTRG
FVQIL
//
