ID A0A1Q4UZ74_9ACTN Unreviewed; 908 AA.
AC A0A1Q4UZ74;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138, ECO:0000256|PIRNR:PIRNR000853};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853};
GN ORFNames=AB852_30840 {ECO:0000313|EMBL:OKH90922.1};
OS Streptomyces uncialis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1048205 {ECO:0000313|EMBL:OKH90922.1, ECO:0000313|Proteomes:UP000186455};
RN [1] {ECO:0000313|EMBL:OKH90922.1, ECO:0000313|Proteomes:UP000186455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCA2648 {ECO:0000313|EMBL:OKH90922.1,
RC ECO:0000313|Proteomes:UP000186455};
RA Yan X., Huang T., Ge H., Shen B.;
RT "Cloning and characterization of the uncialamcin biosynthetic gene
RT cluster.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000853};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000853, ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000853}.
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:OKH90922.1}.
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DR EMBL; LFBV01000010; OKH90922.1; -; Genomic_DNA.
DR RefSeq; WP_073793590.1; NZ_LFBV01000010.1.
DR AlphaFoldDB; A0A1Q4UZ74; -.
DR STRING; 1048205.AB852_30840; -.
DR Proteomes; UP000186455; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule.
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; 2.
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:OKH90922.1};
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 Pyruvate {ECO:0000313|EMBL:OKH90922.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186455};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OKH90922.1}.
FT DOMAIN 68..293
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 301..352
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 426..508
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 542..894
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 459
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 858
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 584
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 639
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 771
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 771
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 792
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 793
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 794
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 795
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 795
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 908 AA; 99070 MW; 10B8B9EEAFDCCFA5 CRC64;
MSKNKGPQVV KFVYDFTEGN KDLKDLLGGK GANLAEMTNL GLPVPPGFTI TTDACKVYLD
SGEEPAALRD EVSAHLETLE QRMGKRLGQH DDPLLVSVRS GAKFSMPGMM DTVLNIGLSD
ASVEGLARQA GDERFAWDSY RRLIQMFGKT VLGVDGELFE DALEEAKAAK GVTVDTDLDA
ADLKKLVKGF KKTVRTEAGR DFPQDPREQM DLAVKAVFES WNGDRAKLYR RQERIPHDLG
TAVNICSMVF GNLGPDSGTG VAFTRDPASG QQGVYGDYLS NAQGEDVVAG IRNTVALADL
EQLDKVSYDQ LMQIMETLEN HYKDLCDIEF TIERGQLWML QTRVGKRTAG AAFRIATQLV
DQGLIDEAEA LQRVTGAQLA QLMFPKFDED AKVDKIGRGI AASPGAAVGK AVFDSYTAIK
WSRSGEKVIL IRRETNPDDL DGMIAAEGIL TSRGGKTSHA AVVARGMGKT CVCGAEELEV
DTKRRRMTAP GGIVIEEGDV VSIDGSTGKV YLGEVPVVPS PVVEYFEGRM HAGADDADEL
VAAVHRVMAY ADRVRRLRVR ANADNAEDAL RARRFGAQGI GLCRTEHMFL GERREYVERL
ILADTDEERE QALDRLLPLQ KRDFVELFEA MDGLPVTVRL LDPPLHEFLP DITELSVRVA
LAESRKDANE NDLRLLQAVH RLHEQNPMLG LRGVRLGLVI PGLFAMQVRA IAEAAAERRD
AKGDPRAEIM IPLVGTVQEL EIVRDEAEQV IDEVQRAAGL DLKLSLGTMI ELPRAALTAG
QIAEAAEFFS FGTNDLTQTV WGFSRDDVEA SFFTAYLEKG IFGVSPFETI DKDGVGALVR
AAAEAGRATR PDLKLGVCGE HGGDPESVHF FHEVGLDYVS CSPFRIPVAR LEAGRAASAG
QSKGSDHR
//
