ID A0A0E3SDK2_9EURY Unreviewed; 805 AA.
AC A0A0E3SDK2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|PIRNR:PIRNR000854};
DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE EC=2.7.9.2 {ECO:0000256|PIRNR:PIRNR000854};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|PIRNR:PIRNR000854};
GN ORFNames=MSHOH_1694 {ECO:0000313|EMBL:AKB78177.1};
OS Methanosarcina horonobensis HB-1 = JCM 15518.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434110 {ECO:0000313|EMBL:AKB78177.1, ECO:0000313|Proteomes:UP000033101};
RN [1] {ECO:0000313|EMBL:AKB78177.1, ECO:0000313|Proteomes:UP000033101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB-1 {ECO:0000313|EMBL:AKB78177.1,
RC ECO:0000313|Proteomes:UP000033101};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988,
CC ECO:0000256|PIRNR:PIRNR000854}.
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 ECO:0000256|PIRNR:PIRNR000854};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000854};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000854}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000854}.
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DR EMBL; CP009516; AKB78177.1; -; Genomic_DNA.
DR RefSeq; WP_048139043.1; NZ_CP009516.1.
DR AlphaFoldDB; A0A0E3SDK2; -.
DR STRING; 1434110.MSHOH_1694; -.
DR GeneID; 24830907; -.
DR KEGG; mhor:MSHOH_1694; -.
DR PATRIC; fig|1434110.4.peg.2137; -.
DR HOGENOM; CLU_007308_6_2_2; -.
DR OrthoDB; 23397at2157; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000033101; 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; IPR018274; PEP_util_AS.
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 NCBIfam; TIGR01418; PEP_synth; 1.
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 PIRSF; PIRSF000854; PEP_synthase; 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.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000854};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000854};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000854};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000854};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000854}; Pyruvate {ECO:0000313|EMBL:AKB78177.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 21..353
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 393..464
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 488..796
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 805 AA; 89619 MW; 9B8476308A2F66D6 CRC64;
MPGDKNKYIR WFEETTIEDV PLVGGKNASI GEMYRELTSK GVRIPNGFSV TADAYWHMLE
KGGILENLKK TMEGLDTSDV SDLAKRGKAA RDLILDAGLP DDLWQEIKGA YDRLCEQYGE
NTDVAVRSSA TAEDLPTASF AGQQETYLNI RGYPGLRDAC IRCFASLFTD RAISYRVTNN
FDHFKVALSI GIMKMVRSDL ASSGVIFTLD TETGFRDVVF ITGAYGLGEN IVQGQVNPDE
FYVFKPTFRE GYKPIIQKKL GSKEIKMIYG RGDSKVLTRN VEVPEADRLR FCISDDEVLK
LAEYAIDIED HYSNKYRESR PMDIEWAKDG ITGELFIVQA RPETVQSQRE KDVLETYVLE
EKSEVLAKGR SVGDKIASGK AHVIPDVSDL PSFRPGEILI ADTTTPDWEP VMKTAAAIVT
NKGGRTCHAA IVSRELGIPA VVGAGNATEV LETGREITVS CAEGEDGLVY AGILPFHKDT
ISLKDLERPR TELMMNLGNP ESAFALSMIP NDGIGLARLE FIITSYIKVH PMALVHPEKV
KDPRELGEIE KLTRGYEKKE DYFVEQLSRG VGMIAAAFYP KPVVVRMSDF KTNEYASLVG
GSYFEMEENN PMIGFRGASR YFDERYREGF ALECRAMKRV RGEMGLTNLI LMVPFCRTVE
EARKVVAEME KNGLRRGENG LQVYVMCEIP NNVLLVDEFS EFFDGFSIGS NDLTQLTLGV
DRDSELLAAE FDERDPGVMK IMSMAVQGAK RNGRHSGICG QAPSDFPEIA EFLVKEGIDS
ISLNPDSVMK ITLKVLETEK ELGKN
//
