ID A0A0G0APR6_9BACT Unreviewed; 1776 AA.
AC A0A0G0APR6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=UR51_C0003G0032 {ECO:0000313|EMBL:KKP58769.1};
OS Candidatus Moranbacteria bacterium GW2011_GWF1_34_10.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618715 {ECO:0000313|EMBL:KKP58769.1, ECO:0000313|Proteomes:UP000034605};
RN [1] {ECO:0000313|EMBL:KKP58769.1, ECO:0000313|Proteomes:UP000034605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- 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:KKP58769.1}.
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DR EMBL; LBPM01000003; KKP58769.1; -; Genomic_DNA.
DR STRING; 1618715.UR51_C0003G0032; -.
DR PATRIC; fig|1618715.3.peg.288; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000034605; Unassembled WGS sequence.
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; 3.50.30.10; Phosphohistidine domain; 4.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 4.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 4.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 2.
PE 4: Predicted;
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..371
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 638..708
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 1007..1077
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 1355..1427
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 1696..1768
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT COILED 1515..1542
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1776 AA; 202936 MW; 2652B9956D001705 CRC64;
MFTKNFKELD KNDAPIAGGK GASLGEMTRA EIPVPPGFVV LSDAFEKFLS ETDLTVEIEA
LLGTVDNQKM HTVENASEKI QELILDAKMP EDIIKEIEIE FKKLDTKYVA VRSSATAEDG
AEHAWAGQLN SYLNTTKENL LENIQKCWAS LFTPRAIFYR FEKYSAQSPS PIGRGVRGEG
GKKEVQYGDE KISVAVVIQK MIQSEKSGIA FSVHPVTEDY NQLIIEAGFG LGEAIVSGSI
TPDSYVVDKS RIKNEELRIK NEELRNKEAI IDVNVNIQNK GLYRSCHLAR RGEGGISGNE
WRDIPEPQSS SQVLSEKEIL ELSDLIIKIE NHYGFPCDIE WAEENGKFYI TQSRPITTLK
SFDKDNIKKE NEGTEIILSN AQSREHSLFY AYVWTESDQN NIKKYSGKTV KNLLFKREFN
DPRLHVFYDS GEMQNIMQDI ADNFRKNENL FEKIERDIQI QSEKMLLYIN NVKKIKNIDE
LMEFKSEWLE WWSAMAMIFI IPNIDGISND IHKKALAIRG KIEKYSDDID RIFVNFFKTK
YPRSVDLVNV ITPEELFNFE NLSNKEIDKI KLRKNGFALF NGNILTLNEL GEDLKLKNII
LEKMEITSGI EEISGICAYS GTVHGKIRKI ILKNDISKIK KGEILLTHMT SPDFLSAFKK
AIAVITDEGG ATCHAAITSR ELKKPCIVGT KIATQVLKDG DLVEVDADEA VVRILKRADE
NVKEVDVLKS TKDTVFSKQI TYTFIPVICF ESAIRSYHNN PLQKKLKIKN FPKIVEILTD
KFEGWDDQNI QKITKAEDIK FVIQESRSII IQYKASLQKF LQLDYIQLSN HDLLQNVKLL
DEICMEVYQR YIFFIHEFFE TDDSEMIELL PKVRIELSEF VSDIYKCCDY IIEALAKRFD
SVSWQTFTYA TFDEIIDLLD DPQKIDEFKK ISGRSIAFIY NGKDLATIKK KELVVEIINY
LTNQEIVASG NCKIIKGNAV SGGTAKGLVI KILEYDYEKI NDALSGKSDY ILVTPMTRPE
IVSYLKDAKA IITDEGGITC HAAIVSRELK IPCIVGTKIA TQVLKDGDLV EVDADRGVVK
ILKKIEINNS EKEKYVKIFN RSLFLIGCQN YDLGERVETK KITPVKYFMN PVFNNLPKKG
TDVFYNFTDP AQNPKWIVDY FNNNRDQLLK IKETYYRDSD LLRKLINDPT YKDYQKLFDL
TIKIWPMVAI SNMLGDNRDN IQGVDEDLLG LYREMRKYSD GLIHNSHLKI AKIIKEIVPQ
KYKKYYKHLQ YEEVVNGNYP EIEELENRMK GYIFHNGKLF TNLSLEEYAQ RNNYVFVGFE
ANNNISENSI SGQIAHEGKV KGYVKVIFEV EEVDKVKKGD VLVTSMTTPD FIVAMKKASA
FVTDEGGITC HAAIVAREMG KPCIIGTKIA TQVLKDGDLV EVDANEGVVR ILKKANEKKE
INFEKVFVRD LTFLLASSGF YNYPGFEKKF DNVILNSPVL KQANGNIVEF WIQKKIADKR
IRQIGRELMD DPKKLKDTMD KYEEVSKKIK KLLNKKESKI SDVINLCKLF IEFRFPNYVM
FESSIETGWS QRVCDWSKIQ RKKDEKLWSQ SDDFIRKALH SKGFSFNQAK KISLKELIEF
EKGNFEINCL DDKEVFVEDC ASNTYLGTMS NIADENNFTL VEHDTEFVDE IKGEIAYKGK
IKGHVKKVFT REDITKVEKG DILVSSMTTP DFILAMKNAT AIVTDEGGII CHAAIFSREM
KKPCIIGTKI ATQVLKDGDL VEVDAEKGIV KILKRV
//
