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Database: UniProt
Entry: N4U2R3_FUSC1
LinkDB: N4U2R3_FUSC1
Original site: N4U2R3_FUSC1 
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
//
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