ID A0A1S1QBW8_9ACTN Unreviewed; 833 AA.
AC A0A1S1QBW8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=BCD49_30395 {ECO:0000313|EMBL:OHV32323.1};
OS Pseudofrankia sp. EUN1h.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Pseudofrankia.
OX NCBI_TaxID=1834515 {ECO:0000313|EMBL:OHV32323.1, ECO:0000313|Proteomes:UP000179465};
RN [1] {ECO:0000313|Proteomes:UP000179465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUN1h {ECO:0000313|Proteomes:UP000179465};
RA Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA Nouioui I., Abebe-Akele F., Thomas K., Gtari M., Tisa L.S.;
RT "Sequence Frankia sp. strain EUN1h.";
RL Submitted (JUL-2016) 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:OHV32323.1}.
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DR EMBL; MBLN01000075; OHV32323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S1QBW8; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000179465; 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; 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; 2.
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, 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:OHV32323.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 21..341
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 408..479
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 505..804
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT REGION 335..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 87334 MW; 966253004C64B063 CRC64;
MSQNGPWIAW FKELSVHDVG LAGGKGANLG ELTQAGFPVP SGFVVTSAAY LRALAEGGLA
TELARRAAEV DPDDTAGLAA EAADLRARVR AVPVPGDIRR AVLGAYHELG GGGGRPMLVA
VRSSATAEDT AGTSFAGMNQ TFTDVRGDDE LIERVRDCWA SLYGERVLAY RAGQEKAGPG
SDAAEPALAV VVQRMVNSER SGVMFSADPA SGDTSRVVIE AAFGLGEVVV GGQVVPDTYI
LTKDGGAGGP ALLDARVGRQ SHQIVRGPDG HDTRVELTET EGSRRVLSGE EAVELARLAV
RVERHYGAPQ DMEWAVETGQ TYLVQSRPIT AMGTREADGA AAADQPGGAP WEPRAAVAPG
GTRPGDASGG SGSDGAGGAP LLTGLAGSPG RASGRVRILR SPEDEDQFRD GEVLVAEMTS
PDWVPVMRRA AAIVTDSGGM TCHAAIVARE MGVPCVVGAR VATSTLSAGQ MVTVDGARGE
VHAGELVAPA AAGAVAVAAE RPTAAAAQPA LAVETTATRL YVNLAVAERA EQVAALPVDG
VGLLRAEFMI ADALGGQHPR HLLASGGRAE FVERMSASLL RIVRAFAPRP VIYRATDFRT
NEFRGLRGGE RYEPVEANPM IGYRGCYRYI RDPEVFALEL EVLAKVREAS PNLHLMIPFV
RTRWELAACL EAVDRSPLGD HRRDLHRWVM AEVPSVAYWI PEYAKLGIDG VSIGSNDLTQ
LMLGVDRDSE TCAELFDESD LAVLDAIGRI ITSCREAGIT SSLCGQAPST HPEFAERLVR
LGITSISVNP DAVDTVRHTV AAAERRLVLD AALGHTMGPG PATRAAASPG RPA
//
