ID W9V8K2_9GAMM Unreviewed; 922 AA.
AC W9V8K2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=D779_3958 {ECO:0000313|EMBL:EXJ13211.1};
OS Imhoffiella purpurea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Imhoffiella.
OX NCBI_TaxID=1249627 {ECO:0000313|EMBL:EXJ13211.1, ECO:0000313|Proteomes:UP000019460};
RN [1] {ECO:0000313|EMBL:EXJ13211.1, ECO:0000313|Proteomes:UP000019460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK35 {ECO:0000313|EMBL:EXJ13211.1,
RC ECO:0000313|Proteomes:UP000019460};
RA Nupur N., Khatri I., Subramanian S., Pinnaka A.;
RT "Genome assembly of Thiorhodococcus sp. AK35.";
RL Submitted (NOV-2012) 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:EXJ13211.1}.
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DR EMBL; AONC01000079; EXJ13211.1; -; Genomic_DNA.
DR RefSeq; WP_043757755.1; NZ_AONC01000079.1.
DR AlphaFoldDB; W9V8K2; -.
DR STRING; 1249627.D779_3958; -.
DR PATRIC; fig|1249627.3.peg.4035; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000019460; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EXJ13211.1};
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:EXJ13211.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..296
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 308..361
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 426..507
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 525..917
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT COILED 296..330
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 459
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 879
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 565
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 621
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 792
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 792
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 813
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 814
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 815
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 816
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 816
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 922 AA; 100983 MW; 65AE12391B70FC88 CRC64;
MDSTKQYVFA FEEGDGKNKK LLGGKGANLC EMTQIGLNVP PGFVISTEAC LEYLDTSEHA
LPAGLIDDVH AQMRALEEKT GKGFGDPENP LLVSVRSGSA MSMPGMMDTI LNLGLNAETL
QGVIAATGDA RFGYDAYRRF IQLFGKVALS VSDEAFDKEF EAIKEAAHAK QDVDLSANDL
KEVSERFLKV VEEATGHPFP SDPYKQLEIA IKAVFNSWMG RRAVDYRKQF HITPEMADGT
AVNVVTMVFG NRGDDSATGV AFTRNPATGE NKLYGEYLIN AQGEDVVAGI RTPKPIDRLK
VEMPDLAVQL DELRDKLESH YREVQDFEFT IERGQLYCLQ TRNGKMNTVA MVRSSVEMEA
EGLISKEEAL LRIQPDSLEQ MLFPRLDPTV KAEAVAQGLP ASPGAASGIA VFDADRAEQF
GKELGRKVIL VREETKPEDI HGFFASEGIL TSRGGKTSHA AVVARGMGKP CVAGAEGISV
DVNRREARVG ITSFKEGDVI TIDGTSGKVY LGAIPTVEPD FTSELNTLLG WADEAAKLKV
MANADTPNDA RKARRYGAVG IGLARTERMF NDVERLPIVI EMIVAETPEQ RQEALDKLLP
LQRNDFRDLF EVMSPNPVTI RLLDPPIHEF LPDEHVLERE LSELRVLAQS ARGVSVLAGA
MGLLHASESL RHEVDTARRM VDPAVVEEAI AKKEAMLRKV RALYETNPML GHRGVRLGMT
FPEIYQMQVR AILEAAAECV KAGIEVHPQI KVPQVCTAQE LRKVKAFVDS IHAEVAERYG
KPVAFKFGTM IEVVRACMRA ESLAEEAEFF SFGTNDLTQA AFSFSREDAE NKFLPLYNQS
GILQDNPFEV LDVKGVGKLM RLAVEWGREV KPNLHVGICG EHGGHPASIA FCHTAGLDYV
SCSGPRVPVA RLAAAHAALK AD
//
