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Database: UniProt
Entry: A0A1H4U9V7_9PSEU
LinkDB: A0A1H4U9V7_9PSEU
Original site: A0A1H4U9V7_9PSEU 
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
//
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