ID W0SEI5_9PROT Unreviewed; 931 AA.
AC W0SEI5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-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=SUTH_01857 {ECO:0000313|EMBL:BAO29649.1};
OS Sulfuritalea hydrogenivorans sk43H.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Sulfuritalea.
OX NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO29649.1, ECO:0000313|Proteomes:UP000031637};
RN [1] {ECO:0000313|EMBL:BAO29649.1, ECO:0000313|Proteomes:UP000031637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM22779 {ECO:0000313|EMBL:BAO29649.1};
RX PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA Watanabe T., Kojima H., Fukui M.;
RT "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT sulfur oxidation pathway of betaproteobacteria.";
RL Syst. Appl. Microbiol. 37:387-395(2014).
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; AP012547; BAO29649.1; -; Genomic_DNA.
DR RefSeq; WP_041098759.1; NZ_AP012547.1.
DR AlphaFoldDB; W0SEI5; -.
DR STRING; 1223802.SUTH_01857; -.
DR KEGG; shd:SUTH_01857; -.
DR HOGENOM; CLU_015345_0_2_4; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000031637; 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; 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:BAO29649.1};
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:BAO29649.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031637};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 56..294
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 304..357
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 421..502
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 518..919
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 880
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 560
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 616
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 793
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 793
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="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 817
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 817
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 931 AA; 102426 MW; 4DE2B75A52878CC0 CRC64;
MKRQWVFAFE EGDGKNKMLL GGKGANLCEM TQIGLNVPPG FTLTTEACQA YLEHDELPKG
AWEEVLKSMK DLEKKTGKQF GGTDNPLLIS VRSGSSMSMP GMMDTILNLG LNKATLQGII
KLTNNPRFGY DAWRRFIQLF GKIALGVEDK HFDDAMAAMK KKVGVADDVD LKAEHLSELA
DQFAQIIEAN TGKPFPEDPY KQLEIAIGAV FRSWNGKRAI DYRRQFKITR EMANGTAVNI
CTMVFGNMGN DSGTGVGFTR NPGTGENMIY GEYLVNAQGE DVVAGIRTPK AIAEMEHDMP
EIYRQLLELH NRLETHYKEV QDFEFTIERG TLYCLQTRNG KMNAAAMVRT SVEMFKEGLI
TKEKALMRID PAMLEQLLVP QLSPDFRGKP LATGLPASPG AASGKIVFDA DTAESRGMAG
EKIILVREET KPEDIHGFFQ AQGILTSRGG KTSHAAVVAR GMGKPCVSGC EAIHINDIKR
SATIGDTTLH EGDVVTIDGG NGNVYAGEVP TVQAEFSHDM ETLLKWADQV SRLKVMANAD
TPEDALRARG FGAMGIGLCR TERMFNATDR LPIVQEMILA ESIEERQAAI DRLLPIQRAD
FKGIFKAMKG LPVTVRLMDP PLHEFLPTAA QLELEIAHLH HLRDSLKALE ELPETLKLLN
PKLYMQYADG LTKLGRSMTD FKEGHLEEDV IHKKEKTLKK VRALSEVNPM LGHRGVRLGI
TYPEIYSMQI QAVLEAAALC AREGIEVHPE IMVPQVATVE ELVRIHSYVK RIHKVVELTH
GIKVDVKFGS MLEVVRACLR AGRMAQDAEF FSFGTNDLTQ ATFSFSREDA ENKFLPGYVE
AGILVDNPFE VLDQKGVGEL MKLAVSEGRK TNPDLKVGIC GEHGGHPGSI AFCHSIGLTY
VSCSGPRVPI ARLAAAQAQL METGGAVTKN A
//
