ID A0A1J0GK35_9CLOT Unreviewed; 878 AA.
AC A0A1J0GK35;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=A7L45_15025 {ECO:0000313|EMBL:APC41296.1};
OS Clostridium estertheticum subsp. estertheticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1552 {ECO:0000313|EMBL:APC41296.1, ECO:0000313|Proteomes:UP000182569};
RN [1] {ECO:0000313|Proteomes:UP000182569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
RX PubMed=27891116;
RA Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
RA Bolton D., Fanning S.;
RT "Complete Genome Sequence of Clostridium estertheticum DSM 8809, a Microbe
RT Identified in Spoiled Vacuum Packed Beef.";
RL Front. Microbiol. 7:1764-1764(2016).
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}.
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DR EMBL; CP015756; APC41296.1; -; Genomic_DNA.
DR RefSeq; WP_071613592.1; NZ_CP015756.1.
DR AlphaFoldDB; A0A1J0GK35; -.
DR STRING; 1552.A7L45_15025; -.
DR KEGG; ceu:A7L45_15025; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000182569; Chromosome.
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; IPR023151; PEP_util_CS.
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; 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:0000313|EMBL:APC41296.1};
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:APC41296.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182569};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 63..296
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 305..357
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 423..504
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 524..871
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 456
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 832
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 562
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 618
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 746
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 767
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 768
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 769
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 770
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 878 AA; 97801 MW; 5B3B6187D67DD64D CRC64;
MEKKKYVYHF SEGNISMKNL LGGKGANLAD MTSLGIPVPK GFTVTTEACN KYYEDGQVIT
PEVVSEIYVK MTELENLTGK KFGSLENPLL VSVRSGARAS MPGMMDTILN LGLNDKTVEV
MARLTNNPRF AYDSYRRFIQ MFADVVMDVE KRNFENMMDK IKEEKGVKFD TELDASDLKK
LVVQFKEFYK ETKGVEFPSD PKIQLIEAIS AVFRSWDNPR ANVYRRLNDI PGDWGTAVSV
QEMVFGNKGE TSGTGVAFSR NPSTGEKGIF AEYLMNAQGE DVVAGIRTPQ DISQLEKDMP
KVYSEFMNIV NTLEKHNKDM QDMEFTIEDK KLFFLQTRNG KRTAQAALKI AVELVEEGML
TKREALMKVD PKQLDTLLHP NFDLVALKEA TIIAKGLPAS PGAACGKVYF TADEAKIKHE
AGEAVILVRL ETSPEDIEGM VAAEGILTVR GGMTSHAAVV ARGMGTCCVA GCSDLKVNEE
SKSFQIREMV YHEGDFISMD GSTGSVYAGV IKTVEPEING YFEIFMGWAD EVRSLKVRAN
ADTPKDAAQA VKYGAEGIGL CRTEHMFFDS DRIMIIREMI VAKNEDARRV ALDKLLPIQR
GDFVGIYEEL KEKPTTIRFL DPPLHEFLPH ADEDIKKLAK DMGITFKELK ATVESLHEVN
PMMGHRGCRL AVSYPEIAEM QTRAVIEAAI DVKNRKGYNI VPEIMIPLIG EVRELKYVKD
IVVKTADKII AESGSDLKYM VGTMIEIPRA ALTADLIAKE AEFFSFGTND LTQMTFGFSR
DDAANFLKHY YEKKVYEFDP FQKLDQVGVG KLIKMAADLG RQVRPNIKLG ICGEHGGDPS
SVEFCHNVGL NYVSCSPFRV PVARLAAAQA EINNPRKK
//
