ID N4U2R3_FUSC1 Unreviewed; 797 AA.
AC N4U2R3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=FOC1_g10004137 {ECO:0000313|EMBL:ENH70153.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH70153.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB730206; ENH70153.1; -; Genomic_DNA.
DR AlphaFoldDB; N4U2R3; -.
DR STRING; 1229664.N4U2R3; -.
DR VEuPathDB; FungiDB:FOC1_g10004137; -.
DR HOGENOM; CLU_007308_6_2_1; -.
DR OMA; VQMYGDV; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000016928; 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; 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:ENH70153.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..347
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 389..459
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 483..792
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 797 AA; 87415 MW; A68C17B0D73D57E6 CRC64;
MSDDWTNEPL VLDFEHLARS DVGLVGGKNS SLGEMIRALG PKGIPVPPGF ATSSYAYWHY
VDANNIRGKI DELVDQWQSG HQTLAEIGHA IRILFLRGTW PADTAEAILS GYRDLCDKAG
VDDLSVAVRS SATAEDLPDA SFAGQQETYL NIQGSEALLD ACRRCYASLF TDRAISYRHI
KKFNHGNVAL SIGIQQMVRS DIGGAGVMFS IDTESGFDKI ILINAAWGLG ENVVQGTVNP
DEYQIFKPLL SNEKLSPILS KKLGDKAIKM VYGDKCVRTR NVPTSRAERA AYVLKDEEIL
QLSRWACLIE EHYSCPMDME WARDGSSGKL YIVQARPETV QSRRDTAAFK TYTVGERGHT
LTTGLSIGDK AVAGRICLLT SVSDIDKFID GSILVTEATD PDWVPVMKRA AAIVTDYGGR
TSHAAIVSRE LGVPAVVGTG NATYVLHTGQ DVTVSCAEGD SGLVYDGISE ITTQMVHISE
LPSVRTKIML NLANPSAAYR WWRLPVDGIG LARMEFVVSN SIRVHPMALI HYDHLEDEAA
KKEITNLTAG YTCKPDYFVD KLASGLATLC SSVYPKPAII RMSDFKTNEY ARLIGGAEFE
LKEENPMIGF RGASRYYSPR YKEGFALECR AVKKVREEMG LTNAIVMIPF CRTVKEARKV
LDIMEENGLK RGENGLMVYV MCEIPSNVIL ASSFTQHFDG FSIGSNDLAQ LTLGVDRDSG
ELASLFDEQD EAVKWMIARA ITVARREGCK IGLCGEAPSN HPEFAKFLVN SGIDSISVSP
DSFVQVMKHV VASEKGL
//