ID A0A1H4U9V7_9PSEU Unreviewed; 747 AA.
AC A0A1H4U9V7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04489727_4562 {ECO:0000313|EMBL:SEC65536.1};
OS Amycolatopsis tolypomycina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=208445 {ECO:0000313|EMBL:SEC65536.1, ECO:0000313|Proteomes:UP000199622};
RN [1] {ECO:0000313|EMBL:SEC65536.1, ECO:0000313|Proteomes:UP000199622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44544 {ECO:0000313|EMBL:SEC65536.1,
RC ECO:0000313|Proteomes:UP000199622};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNSO01000004; SEC65536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4U9V7; -.
DR STRING; 208445.SAMN04489727_4562; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000199622; 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:InterPro.
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; 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:SEC65536.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..316
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 354..425
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 450..738
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 747 AA; 79945 MW; C9C409C510F70835 CRC64;
MTYVRDLAEI RLTDDETVGG KGANLGELIS AGFPVPGGFV ISRDGYWAAL EKAGVRAEVA
DLHAKALANV DDAELLAEHC DRIRDLVRLA GLTGDLREEI AQAYRGLGSA TPVAIRSSAT
GEDGAEASFA GMNATYTNIW GDHAVAEHVV DCWTSLFSPR VVSYRASRGF TGEPAIAVVV
QRMIRSERSG VIFTADPRTG DRDRVVVEAV FGQGEAIVSG AVEPDTYVVG KQDLLILSVR
IGRQTHKIVA DEGGGDVTIQ LPEPAGGRRV LSETVVLELA RMASRVEEHY GVPQDIEFAI
ADSEIFLVQS RPITTLPPLT PASTVALVTG LGASPGEGSG AVRVLHDPVE AKHLRDGEIL
VAPMTNPDWV PAIRRAAAVV TDGGGMTCHA AVVARELGVP AVVGTGDATR VLVDRSLVTV
DGTQGEVRPG AAKKAPAHTA PVAAPVAPEA IGTKLYVNLA MPEHAEEVAA QAVDGVGLLR
AEFLLTEALG GRHPRDLLAK GDERSFVDNM AESLLKITKP FGTRPVVYRA TDLRTNEFRG
LAGGEEFEPV ESNPMIGYRG CYRYVRERDL FALELETLAR VREHTPNLHL MIPFVRTKWE
LEECLELVDA SPLGRQRGLH RWVMAEVPSV VHWLGEYAGM GIDGVSIGSN DLTQLMLGVD
RDSGQCAELF DEADPAVLDA IERIIRVARH RGITSSLCGQ APSTKPGFAE HLVRFGITSI
SVNPDVIGPA RAAIASAERR ILLEATR
//