ID A0A0C2PPP8_9CYAN Unreviewed; 827 AA.
AC A0A0C2PPP8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=SD81_28925 {ECO:0000313|EMBL:KIJ73499.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ73499.1};
RN [1] {ECO:0000313|EMBL:KIJ73499.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ73499.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) 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}.
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:KIJ73499.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXCB01000012; KIJ73499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2PPP8; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
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; 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; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Pyruvate {ECO:0000313|EMBL:KIJ73499.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..329
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 370..440
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 526..810
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT REGION 497..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91214 MW; F8B2789805EBA0CC CRC64;
MDKLYWLDQI KLQDRAKVGD KAYYLSRIMQ RGYPVVPGFV VSAEVLREFL ETLNSSEALV
ADLPHSSLHV DVNNWRQLQQ VTGRLRQEIN TAVLPPHLLS TIVNAAKELE SAYLIFRPSI
VVPTARHGIG NTSGLLESQV CRCDEQAIAL ALKRTWSQMF RAKSLLYWQW AGIKVQQIHL
GVLVQPLKNA IASGSLYANS SQWEILATSG LGLAINQGDV LPDVYYIHPV TGSVTEQQLG
NKTLAYSVND TAAVATLQTV PASPLNSDDS SLVTYLLNED QQKQYALPEE YLQPLIGLAN
RLVKEIGRHF TFEWTVCCDP TKTLYLTQVS TPQATISNFH LLKGLAAAPG RVTATAHVII
NSQQKPEQPP KQVILVAPTI APDWLQTVQD ISGIITEQGG LTSHAAILAR ELGIPAVVRV
QHATKIIQTG ERLLIDGDKG EVYRLTREVG EAGEIGKEDK GTNQFKITED WIGGNLRSNF
SQNSKFKIWN FSSSPSSPSL PPSLSPSSPS SPSSPSSPSS PIRAIIGTQL LVNLSQTSLI
EQVQSLPVDG VGLLRSELMA LNILEGQDPY TWVREGHQTQ LLERLHEQIM QFARAFAPRP
VFYRSLDWRS HELSSFNDSL QSSTQSMLGE RGTFSYLQNP AVFELELAAL AAVHKAGYSN
VHLLLPFVRT VEEFSFCRQK VEQAKLTQVP QFQLWIMAEV PSVLFLLPEY IKAGVAGISI
GTNDLTQLLL GVDRDQGQLA KAFNERHPVV MGAVAQLIQT AKSAGIPCSI CGQAPVLYPE
IIEQLVRWGI TSISVEPEAV ERTYLAIARA EQRILLEAAR RQLNQST
//
