ID W7N6Z6_GIBM7 Unreviewed; 798 AA.
AC W7N6Z6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=FVEG_13461 {ECO:0000313|EMBL:EWG55464.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG55464.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG55464.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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; DS022264; EWG55464.1; -; Genomic_DNA.
DR RefSeq; XP_018761655.1; XM_018902830.1.
DR AlphaFoldDB; W7N6Z6; -.
DR STRING; 334819.W7N6Z6; -.
DR EnsemblFungi; FVEG_13461T0; FVEG_13461T0; FVEG_13461.
DR GeneID; 30070810; -.
DR KEGG; fvr:FVEG_13461; -.
DR VEuPathDB; FungiDB:FVEG_13461; -.
DR eggNOG; ENOG502QREJ; Eukaryota.
DR HOGENOM; CLU_007308_6_2_1; -.
DR OMA; HFFHEVG; -.
DR OrthoDB; 5474086at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000009096; Chromosome 8.
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 Pyruvate {ECO:0000313|EMBL:EWG55464.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..349
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 390..460
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 485..792
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 798 AA; 87260 MW; 787582D7935AC593 CRC64;
MMSDDWTAEP LVLDFEHLAR NDVGLVGGKN SSLGEMIRAL GPKGIPVPPG FATSSYAYWH
YVDANNIRGK IDELVDQWQS GHQTLAEIGH AIRTLFLRGT WPADTAEAIL SGYRDLCDKA
GVDDLSVAVR SSATAEDLPD ASFAGQQETY LNIQGSEALL DACRRCYASL FTDRAISYRH
IKKFNHGNVA LSIGIQQMVR SDIGGAGVMF SIDTESGFDK IVLINAAWGL GENVVQGTVN
PDEYHVFKPL LSNEKLSPIL SKKLGDKAVK MVYGDKCVPT RNVPTSRAER ASHVLEDEEI
LQLARWACLV EEHYGCPMDM EWARDGSSGK LYIVQARPET VQSRRDAAAF KTYKVGERGH
TLTTGLSIGD KAVAGRICLL TSVSDRDKFI DGSILVTDST DSDWVPVMKR AAAIVTDYGG
RTSHAAIVSR ELGVPAVVGT GNATYVLHTG QDITVSCAEG DSGLVYDGIS DITTEMVNIS
DLPSVRTKIM LNLANPSAAY RWWRLPVDGI GLARMEFVVS NSIRVHPMAL VHFDHLEDEA
AKKEIANLAA GYAYKPDYFV DKLASGLATL CSAVYPKPAI IRMSDFKTNE YARLIGGAEF
ELKEENPMIG FRGASRYYSP RYKEGFALEC RAVKKVREEM GLTNAIVMIP FCRTVKEARK
VLDMMEQNGL KRGENGLMVY VMCEIPSNVI LASSFTQHFD GFSIGSNDLA QLTLGVDRDS
GELASLFNEQ DEAVKWMIAR AIAVARREGC KIGLCGEAPS NHPEFAKFLV NAGIDSISVS
PDSFIQVMKH VVASEKGL
//
