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
//