ID Q1MSE4_LAWIP Unreviewed; 1194 AA.
AC Q1MSE4;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470};
GN Name=ppsA {ECO:0000313|EMBL:CAJ54081.1};
GN OrderedLocusNames=LI0025 {ECO:0000313|EMBL:CAJ54081.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54081.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54081.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54081.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001518};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; AM180252; CAJ54081.1; -; Genomic_DNA.
DR RefSeq; WP_011526108.1; NC_008011.1.
DR AlphaFoldDB; Q1MSE4; -.
DR STRING; 363253.LI0025; -.
DR KEGG; lip:LI0025; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_271342_0_0_7; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002430; Chromosome.
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:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; 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; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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; IPR006319; PEP_synth.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000002430};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 40..437
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 489..562
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 843..1066
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT COILED 704..772
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1194 AA; 133712 MW; ED9505AA713B309B CRC64;
MSKKTLSTHH DSINSVETIR KQLVLTGSDI ITIGEDAELL VGGKNYNTAL LGQIKEIKTP
QFRAISSLAF HQILDETKVC AALIRSKVEE HYTHINWNNP EVVQDHEFLP KFVRNIASII
QYELDGNTNK LPLIRLRTFI EHVVDGFASS QENIDQLRKR SILVQCAILS VPLPPQVIEA
VKIAYKEICN EAEENNVPVA VRSSAAGEDS RKKAFAGLQD TYLNMVGEDA VVLAYHWDCA
SAYNLRSMIY RREAILDALT KSESTGDEQF AIQAKQEWAI ENTSLSVCIM RMINPVVSGT
AFSADTATGC RGTTRNDLVS IDVSYGLGEA IVGGMVTPDK MYVYQKDDAN EVIIRFMGNK
TLKIIYDEKG GTKKIPVSER ESIMWALSPT QAEQIAKGVR AISKAYKDII MDTEFCIDTK
GTIWFVQARP ETRWNDELML YPNTIFMHRC EVDPQAAATA KIVLEGNGAS RGAGQGKVRF
LNSALELNKI QKGDILAAER TDPDMVPGMR VASAILADVG GDTSHAAITS RELGIPAIIG
IQNSAALKAL DGLEVTVDGT RGHVYHGLLP LYQTGGEINI NELPKTKTKV GLVLADIGQS
LFLSRLRNVP DFEVGLLRAE FMLGNVGVHP SALEAFDNGS LESIIQKKID ELEVHLRKTI
QEHLCLGLVN LDLHLREHVG HISGYTEELE RLHKRNDPHN PEAVIATYRQ IKELEKRLDE
LTELAASSLD TLKVSSDLSE HVKIIMGYQK QLLSLNDESP QLKKRRIDLE KEIETYTADI
AQNPIVQKTI SQIEQLRKEV SERCGINKKI KELQSIPLAI GSLIRSCGHK TGREHYIQTL
SQGLALFSMA FYGKPIIYRT TDFKTNEYRN LLGGILFEDF EDNPMLGYRG VARDIHDWEI
DAFKAARSLY GAKNLQLMLP FVRTIEQARS MRSYLSEVHN LRSGEDNLQI FLMSELPSNA
ILARQFIQEF DGFSIGSNDM TQMVLATDRD NQSLSHIYDE EDPAVVWAIL VTIFTGQKYG
KKVGFCGQGV ANSAILRGIV TISGITSASV VPDTYYQTKQ EIADIEASNI SLSELGQWLT
KQHKNNLKKL LEEHGYNLFN TNPTNQDIQL WYNKNISTLC TQLQKNLTTS QAPKIAKTLK
EFRTLFHKAV IYATWPWEET VNDALYQAGF RSFEEQKVAL EQQRKHIMNT ISYK
//
