ID S7ZBR8_PENO1 Unreviewed; 804 AA.
AC S7ZBR8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00011996};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470};
GN ORFNames=PDE_01072 {ECO:0000313|EMBL:EPS26136.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26136.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS26136.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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; KB644408; EPS26136.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZBR8; -.
DR STRING; 933388.S7ZBR8; -.
DR eggNOG; ENOG502QREJ; Eukaryota.
DR HOGENOM; CLU_007308_6_2_1; -.
DR OrthoDB; 5474086at2759; -.
DR PhylomeDB; S7ZBR8; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000019376; 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};
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 Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 29..350
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 396..466
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 491..800
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 804 AA; 88347 MW; AEACDEBF23E78640 CRC64;
MAKSKDNQIN GSVVNLTIPF EHLRRKDVAL VGGKNASLGE MIGNLAAEGI SVPPGYATTS
QAYWQYVEHN GIQDKIASLI AEWKSGQARL DDTGHAIRDL FLRGSWPSNI ADEIVKGYHT
IEHQTGIQGL SVAVRSSATA EDLPDASFAG QQESYLNISG VDALLHACKS CYASLFTDRA
IGYRQAKGFD HLRIALSIGI QRMVRSDASC SGIMFSIDTE TGFDKIVLIN ASWGLGENIV
QGMVNPDEYR VFKPLLHMDK FEPIIEKKRG DKSRKLIYGN GNAPTRNVPT SKAEQAAFTL
SDSEVLQFSR WACTIEKHYE CPMDIEWAKD GLTNELFIVQ ARPETVHSSR DMCGEFKTYE
VTDKGRVLTT GLAIGDAAVS GQLCLIEGKH DLEKFVTGSV LVAKVTDPDW VPFMKRAVAI
ITDLGGRTSH AAIVSRELGL PAVVGTGDAT YTLHSGQNVT VSCAEGDRGI VYEGTSRIVT
RTLDVNSLPP VNTKIMINLA NPGAAYRWWR LPVDGIGLAR MEFVISNAIR IHPMALAYFD
QLKDSKAKSE IAKLTSEYKH KPDYFVEHLS RGFAALCSTV YPKPAILRLS DFKTNEYSDL
IGGSEFEPVE ENPMLGFRGA SRYYSPHYKE GFALECRAIK RLREKMGFTN AIVMVPFCRT
VYEAEDVLKV MAQNGLVRGG NGLQVYVMGE IPSNVILAAQ FARHFDGFSI GSNDLTQLTL
GVDRDSAELG DLFNEQDEAV KWMIERVIRV AHENGCKVGI CGQAPSDHPE FAAFLVNCGI
DSVSVSPDSY IPVRKVIAGV QKMR
//
