ID A0A066YV62_9ACTN Unreviewed; 902 AA.
AC A0A066YV62;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=KCH_26690 {ECO:0000313|EMBL:KDN85438.1};
OS Kitasatospora cheerisanensis KCTC 2395.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN85438.1, ECO:0000313|Proteomes:UP000027178};
RN [1] {ECO:0000313|EMBL:KDN85438.1, ECO:0000313|Proteomes:UP000027178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN85438.1,
RC ECO:0000313|Proteomes:UP000027178};
RA Nam D.H.;
RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL Submitted (MAY-2014) 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:KDN85438.1}.
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DR EMBL; JNBY01000083; KDN85438.1; -; Genomic_DNA.
DR RefSeq; WP_035862641.1; NZ_KK853997.1.
DR AlphaFoldDB; A0A066YV62; -.
DR PATRIC; fig|1348663.4.peg.2574; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_11; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000027178; 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; 3.
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:KDN85438.1};
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:KDN85438.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDN85438.1}.
FT DOMAIN 20..58
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 61..288
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 295..347
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 421..503
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 541..890
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 454
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 854
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 579
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 635
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 767
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 767
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 788
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 789
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 790
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 791
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 791
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 902 AA; 97746 MW; 7CDF011174FA5071 CRC64;
MAAKQKFVYS FTEGNKDLKD LLGGKGANLA EMTNLGLPVP PGFTITTDAC KVFLETGTEP
ASLNDEISGH LAALESHMGK RLGQADNPLL VSVRSGAKFS MPGMMDTVLN IGLSDASVTG
LAAQSGNERF AWDSYRRLVQ MFGKTVLGVD GELFEEALDE AKHAKGTAND LDLTAEDLKA
LVETFKAIVL RETGREFPQE PREQLDLAVH AVFHSWNGDR ARLYRRQERI PNDLGTAVNV
CTMVFGNLGE DSGTGVAFTR DPSTGTQGVY GDYLQNAQGE DVVAGIRNTL QLADLEQLDK
KSYDELMSIM ETLENHYRDL CDIEFTIERG KLWMLQTRVG KRTAAAAFRI AVQLVDQGLI
DLDEALHRVT GNQLAQLMFP RFAPTSETRP VAYGIAASPG AAVGKVVFDS YTAVKWSRSG
EKVILVRRET NPDDLEGMIA AGGILTSRGG KTSHAAVVAR GMGKTCVCGA EELEVDTKNR
KFTTADGQVV HEGDVVSIDG ANGKVYLGEV PVLPSPVVEY FEGTLHAGAD VQGGLVQAVH
RLMSHADGRR RLAVRANADN AEDANRARRY GAQGIGLCRT EHMFLGEERR KEVEHLILAD
NDKDREAALS SLLPRQKGDF LELFQSMDGL PVTVRLLDPP LHEFLPDITE LSVRVALAEA
RKDPNENDLR LLQAVHRLHE ANPMLGLRGV RLGLVIPGLF GMQVRAIAEA AAERKLAGGD
PRPEVMIPLV GTVQELELVR DECERVLAEV AASTGVNLDI KLGTMIELPR AAVTAGQIAE
AADFFSFGTN DLTQTVWGFS RDDVEASFFT AYLEKGIFGV SPFETIDRDG VGSLVRSAAK
AGRATRPDLK LGVCGEHGGD PDSVHFFHEV GLDYVSCSPF RIPVARLEAG RAAIETAGSD
SR
//
