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Database: UniProt
Entry: A0A178ZE23_9EURO
LinkDB: A0A178ZE23_9EURO
Original site: A0A178ZE23_9EURO 
ID   A0A178ZE23_9EURO        Unreviewed;       795 AA.
AC   A0A178ZE23;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=AYL99_07117 {ECO:0000313|EMBL:OAP58027.1};
OS   Fonsecaea erecta.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP58027.1, ECO:0000313|Proteomes:UP000078343};
RN   [1] {ECO:0000313|EMBL:OAP58027.1, ECO:0000313|Proteomes:UP000078343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP58027.1,
RC   ECO:0000313|Proteomes:UP000078343};
RA   Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA   Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA   Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA   Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA   Attili D.S., Gorbushina A.;
RT   "Draft genome of Fonsecaea erecta CBS 125763.";
RL   Submitted (APR-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAP58027.1}.
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DR   EMBL; LVYI01000006; OAP58027.1; -; Genomic_DNA.
DR   RefSeq; XP_018691394.1; XM_018838626.1.
DR   AlphaFoldDB; A0A178ZE23; -.
DR   STRING; 1367422.A0A178ZE23; -.
DR   GeneID; 30011285; -.
DR   OrthoDB; 5474086at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000078343; 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:OAP58027.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078343};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          22..345
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          387..458
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          483..789
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   795 AA;  86893 MW;  619624AE62A1267A CRC64;
     MNGSNHKVLV RNFENVVRGD VASVGGKNAS LGEMIGGLKA EGIVVPPGFA TTADAYWRYV
     DANDIRGKMT RLIGEWQSGK ATLPETGHAV RNLFLRGDWP ADVSTAITNA YQQLSAQAGI
     NDLSVAVRSS ATAEDLPDAS FAGQQETFLN ISGPAALLNA CRRCYASLFT DRAISYRQTA
     HFDHLKVALS IGVQRMVRSD AAGSGVMFTL DTESGFNKVV LINAAWGLGE NVVQGTVNPD
     EYQVFKPLLT NPDLVPIIEK KRGEKAMKMV YGNEHMPTRN VPTSKAERNS FVLSDLEILN
     LARWACIIEN HYKCPMDIEW AKDGITGEMF IVQARPETVQ ARREAGVFKT YKIGKKGRVL
     ATGLSVGEAA VSGRLCLIET AKDIGKFVDG SILVTETTDP DWVPIMKRAA AIITDHGGRT
     SHAAIVSREL GVPAVVGTGN ATYILHTGQD VTVSCAEGDT AFVYEGISDI TTKEVDVTGL
     PPTRTNVMLN LANPASAYRW WRLPADGIGL ARMEFVVSSI QVHPMALVHF EKLKDEKAQA
     EITRLTAGYK DKPEYFVDKL SRGLACLCAA VYPKPAIIRM SDFKTNEYAN LIGGKDFEPH
     EENPMLGFRG ASRYYSPRYK EGFALECRAI KRIREEMGFT NAIVMIPFCR TVGEAAKVME
     VMAENGLRRG EHGLQVYVMC EIPSNVILAE EFTRQFDGFS IGSNDLTQLT LGVDRDSAEL
     ADLFDEQDAA VKWMIERVIA VARQAGRKIG LCGQAPSNHP EFADFLVKCG ISSVSVSPDS
     FLEVKRHVIA SEKAN
//
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