ID A0A0F5Y6W6_9CYAN Unreviewed; 809 AA.
AC A0A0F5Y6W6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623, ECO:0000256|PIRNR:PIRNR000854};
DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996, ECO:0000256|PIRNR:PIRNR000854};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470, ECO:0000256|PIRNR:PIRNR000854};
GN ORFNames=WN50_30500 {ECO:0000313|EMBL:KKD34518.1};
OS Limnoraphis robusta CS-951.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD34518.1, ECO:0000313|Proteomes:UP000033607};
RN [1] {ECO:0000313|EMBL:KKD34518.1, ECO:0000313|Proteomes:UP000033607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-951 {ECO:0000313|EMBL:KKD34518.1,
RC ECO:0000313|Proteomes:UP000033607};
RA Willis A., Parks M., Burford M.A.;
RT "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT robusta strain CS-951.";
RL Submitted (JUN-2015) 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}.
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:KKD34518.1}.
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DR EMBL; LATL02000023; KKD34518.1; -; Genomic_DNA.
DR RefSeq; WP_046282384.1; NZ_LATL02000023.1.
DR AlphaFoldDB; A0A0F5Y6W6; -.
DR PATRIC; fig|1637645.4.peg.429; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000033607; 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; 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:KKD34518.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033607};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 32..363
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 400..471
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 493..804
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 809 AA; 89446 MW; 731A777A4757C694 CRC64;
MLKTLALQNI SPVKEQALVL WFDQVGINDI SFVGGKNASL GEMIRQLTPK GVNVPQGFAI
TAYAYRYFLK SAGLDVKLRQ LLAGLDVDDL PNLRTRAEQA RNLLINTRFP VDLESAIAQA
YLKLCDLYGM KVDVAVRSSA TAEDLPDASF AGQQETYLNI QGCKAVIEAT HKCFASVFTD
RAISYRTIKG FNHFDVALSV GVQKMVRSDL ACSGVMFSID TETGFKNAAL ITAAYGLGEN
VVQGAVNPDE YLVFKPTLHE GFHPILDKRL GTKAIKMVYD AEGTTKNIRV SPTQQQKFAL
NDHEILHLAK WGMLIEDHYS RLRGCYSPMD IEWAKDGITG ELFVVQARPE TVQSQKSTQV
LQQYKLQQKG KILITGRAVG DRIGQGKVRV ILDVKDMDQF QAGDVLVTNK TDPDWEPILK
KASAIVTNSG GRTCHAAIIA RELGIPAIVG CGDATTVLQT GETVTVSCAE GEEGHVYQGF
LPFEIEETVL ENLPKTRTQI LMNVGNPEEA FRLAAMPADG VGLARLEFII ANHIKVHPLA
LIHFNQLTDE KVKAQIEQLT VQYEHKPDYF VDKLAHGISM IAAAFYPHPV IVRMSDLKSN
EYANLLGGYQ FEPKEENPMI GWRGASRYTD PKYREAFGLE CQAIKRVRDE MGLANVIPMI
PFCRTPDEGK QVLAEMAKYG LVRGENGLQV YVMCELPSNV LLADEFCQVF DGFSIGSNDL
TQLTLGLDRD SGLVAHLFDE RNLAVRRMIK MAIETVKQQG RKIGICGQAP SDYPEFAQFL
VKLGIDSISL NPDSVVPMIL NIAEMERSA
//
