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Database: UniProt
Entry: A0A0D2E4X1_9EURO
LinkDB: A0A0D2E4X1_9EURO
Original site: A0A0D2E4X1_9EURO 
ID   A0A0D2E4X1_9EURO        Unreviewed;       862 AA.
AC   A0A0D2E4X1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=PV05_12044 {ECO:0000313|EMBL:KIW50458.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW50458.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW50458.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW50458.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; KN847323; KIW50458.1; -; Genomic_DNA.
DR   RefSeq; XP_013311042.1; XM_013455588.1.
DR   AlphaFoldDB; A0A0D2E4X1; -.
DR   STRING; 348802.A0A0D2E4X1; -.
DR   GeneID; 25333952; -.
DR   HOGENOM; CLU_007308_6_2_1; -.
DR   OrthoDB; 5474086at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000054342; 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   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:KIW50458.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          83..406
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          449..519
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          543..851
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   862 AA;  95123 MW;  2F5736BA9CE804E9 CRC64;
     MMRVFLIRIC AFVSIPSHNI KIRPTTFLQY YFFSSSTFPE YLEPHFSSSE SITFTQVFPE
     MNNINKSPVF VRNFEHLVRQ DVALVGGKNS SLGEMIGALT AKGISVPPGF ATTSNTYWHY
     VDANNIREKM TKLIGEWQSA KTSLADTGKE VRNLFLRGDW PDDAAAAIKT AYQELSAKAG
     TKNLGVAVRS SATAEDLPDA SFAGQQETFL NISGEDALLN ACRRCYASLF TDRAISYRQT
     KHFDHMKVAL SIGVQQMVRS DLSGSGVMFS LDTESGFDRV VLINAAWGLG ENIVQGTVNP
     DEYQVYKPLL VNPEYVPIIE KKRGEKEVKM IYGDEHMPTR NVPTSKHERA SFVLNDSEIL
     QLATWACTIE QHYGCPMDIE WAKDGVSGDL FIVQARPETV QARREAGVFK TYKLGKKGRV
     LTTGLSVGEA AVTGRLCLLE TAKDIDKFID GSILVTETTD PDWVPIMKRA AAIITDHGGR
     TSHAAIVSRE LGVPAVVGTG NATYLLHTGR DVTVSCAEGD EGFVYDGIAD ITTKELDVTG
     LPPTRTKIML NLANPASAYR WWRLPADGIG LARMEFVVSN HIQVHPMALV RFDHLKDEKA
     KQEIARLTKG YADKPEYFVD KLARGLACLC AAVYPKPAII RLSDFKTNEY ANLVGGEEFE
     PKEENPMLGF RGASRYYSPR YKEGFALECR AIKRLREEMG FTNAIVMVPF CRTVGEAAKV
     LRVMSENGLT RGENGLQVYV MCEIPSNVIL AAEFTKHFDG FSIGSNDLTQ LTLGVDRDSG
     ELADLFDEQD KAVKWMISTV ITEARKAGRK IGLCGQAPSN HPEFAAFLVD CGINSVSVSP
     DSFLEVKKHV IASEKAEING TG
//
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