ID I4GV74_MICAE Unreviewed; 718 AA.
AC I4GV74;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=MICAE_2080002 {ECO:0000313|EMBL:CCI13698.1};
OS Microcystis aeruginosa PCC 9806.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1160282 {ECO:0000313|EMBL:CCI13698.1, ECO:0000313|Proteomes:UP000003273};
RN [1] {ECO:0000313|EMBL:CCI13698.1, ECO:0000313|Proteomes:UP000003273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9806 {ECO:0000313|EMBL:CCI13698.1,
RC ECO:0000313|Proteomes:UP000003273};
RA Genoscope - CEA;
RL Submitted (APR-2012) 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:CCI13698.1}.
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DR EMBL; CAIL01000122; CCI13698.1; -; Genomic_DNA.
DR RefSeq; WP_002783974.1; NZ_HE973244.1.
DR AlphaFoldDB; I4GV74; -.
DR HOGENOM; CLU_007308_6_2_3; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000003273; 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; 3.20.20.60; 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 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:CCI13698.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..311
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 347..416
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 441..708
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 718 AA; 79645 MW; 834DC6057BF36C60 CRC64;
MTILCWLDRI SASDRPLVGE KAFIASELHR RGYPIIGGFA IFNRIFAEFL ETINNADSFL
TDFPQSSLYL DVDNAKALQL VAKESRGAIL QAQIPPLWLE ELEAAVAQLS MDTLVWRFSL
PANLARRTLG LFSAPISGIK ADNLENALKQ AWAELFTARS LFYWRKMGIG LENIQLSLLV
QPLLPANCAG NVLINDDNWK IQAVWGLGHS LVNGEVAPDT YIIDRPGQLR SRQLGNKSRA
YYLNSDSNLL APQLLAPSLQ ESYCLDNFAL DRLCQLVQSL LAEKPTLTSI EWLMMLDGQI
YILNCHSQEI TPTTSHYPLR GLGASPGLVS GVAKVISNFD SPEATFQDCI LVTTNLPPQK
LPHLRQIRAM ITEQGGLTSH GAILARELAI PAVVGVKNAT EIIRSGEIIL VDGTRGIISL
ASQEQISLPP PPPRETDGTA IATRLMVNLS QTESIAGIQE LPIDGIGLLR SEWMILELLS
QRNLEEWLTP EHQEALIERL SDLIAQFALS IQPKPLFYRS FDAQHSTKDS RGTHGYILDP
TLFDLELQAL RRVQTTGATN INLLLPFVRG VEEFIFCRQR VQSALLTQVP SFQLGIMVEV
PGVIFQLRDY VQAGVQLLAI GTNDLTQLLL GSDREHFSEY FNARHPAVRA ALKQIITQAK
VLQIPCSVCG MAIVQYPELI DDLIAWGVTS LSVDREAVLA TREAIVRAER RFLLENSR
//
