ID V5BBD4_TRYCR Unreviewed; 794 AA.
AC V5BBD4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
GN ORFNames=TCDM_00696 {ECO:0000313|EMBL:ESS70555.1};
OS Trypanosoma cruzi Dm28c.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS70555.1, ECO:0000313|Proteomes:UP000017861};
RN [1] {ECO:0000313|EMBL:ESS70555.1, ECO:0000313|Proteomes:UP000017861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dm28c {ECO:0000313|EMBL:ESS70555.1,
RC ECO:0000313|Proteomes:UP000017861};
RX PubMed=24482508;
RA Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL Genome Announc. 2:e01114-13(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000853-3};
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:ESS70555.1}.
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DR EMBL; AYLP01000004; ESS70555.1; -; Genomic_DNA.
DR AlphaFoldDB; V5BBD4; -.
DR EnsemblProtists; ESS70555; ESS70555; TCDM_00696.
DR VEuPathDB; TriTrypDB:TCDM_00696; -.
DR Proteomes; UP000017861; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 1.20.80.30; -; 1.
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 Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR PIRSF; PIRSF000853; PPDK; 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; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:ESS70555.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Pyruvate {ECO:0000313|EMBL:ESS70555.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017861};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 65..384
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 450..529
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 544..790
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
SQ SEQUENCE 794 AA; 87846 MW; 22DF0F9A93E77483 CRC64;
MESKKFVYYF GGQKADGNRD MKELLGGKGA NLAEMVNLGI PVPPGFTITT EVCGIYQRTK
GLPQEVVEQV KANVRRVEAD MGTKFGDVEN PLLFSVRSGA AASMPGMMDT VLNLGMNKAT
AEAWIRRAPH LERFVYDSYR RFITMYADIV MQVGREDFEE AIGHMKEKRG TKFDTDLTAK
DLKELTEEYL VLFQRKTGFP FPEDPMTQLF AAINAVFRSW GNPRAVVYRR LNNITGLLGT
AVNVQAMVFG NINDRSATGV AFSRSPSTGE NFFFGEYLVN AQGEDVVAGI RTPQQIGQSL
SLRWAKGHGV SEEERRHRYP SMEETMPENY RLLCEIRAKL ENHYRDMQDI EFTVQDGRLW
MLQCRNGKRT IHAAVRVAID MVREGLITKE EAVLRIDPLQ VDHLMHPNIE PGAAKSNKPI
GKGLAASPGA AVGQIVFDAD SAKEWSARGK KVIMVRLETS PEDLAGMDAA RGILTARGGM
TSHAAVVARG MGKCCVSGCG DLVIKGKQFT LSGRVFREGD YITLDGSKGL IYAGQLKLQS
PNLKGDFETI LQWCREVKRL GVRANADTPN DATKARSFGA EGVGLCRTEH MFFEGSRIDA
IREMILADTL EGRKAAIQKL LPVQRGDFLG IFRAMKGLPV TIRLLDPPLH EFVPHEDAAQ
AELAKKMNVS AEKIRNRVKS LHEMNPMLGH RGCRLGITYP EVYNMQVQAI MEAAVAVSKE
GCKVVPEIMI PLVGKKEELT FTKQQAVKTA EETLAAAGQR VDYIVGTMIE VPRAAITADQ
IAEEADFFSL VPTI
//
