ID A0A1B4V7R3_9GAMM Unreviewed; 936 AA.
AC A0A1B4V7R3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=SVA_0825 {ECO:0000313|EMBL:BAU47404.1};
OS Sulfurifustis variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Sulfurifustis.
OX NCBI_TaxID=1675686 {ECO:0000313|EMBL:BAU47404.1, ECO:0000313|Proteomes:UP000218899};
RN [1] {ECO:0000313|EMBL:BAU47404.1, ECO:0000313|Proteomes:UP000218899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skN76 {ECO:0000313|Proteomes:UP000218899};
RA Miura A., Kojima H., Fukui M.;
RT "Complete genome sequence of Sulfurifustis variabilis.";
RL Submitted (AUG-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}.
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DR EMBL; AP014936; BAU47404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B4V7R3; -.
DR KEGG; sva:SVA_0825; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000218899; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:BAU47404.1};
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:BAU47404.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218899};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 94..328
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 334..390
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 459..540
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 572..928
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 492
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 890
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 613
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 669
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 804
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 804
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 825
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 826
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 827
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 828
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 828
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 936 AA; 102905 MW; 4AECB54FE6FE621A CRC64;
MARPGTRNEG TSKATRPRAA GATTRRGARP RLAKAGKHVY FFGGGKADGD RTMRDLLGGK
GAGLAEMTRA GLPVPPGFTI STDVCALFYA QGGRVPDAVE REMAAGLERL EKLAGARLGA
SDGPLLLSVR SGAKFSMPGM MDTILNLGLN DETVEGLKAR TGNGRFAYDS YRRFLQMFGS
VVLQVPKDAF DQKFESVKRL RGARLDTDLD EQALRDVVVE YQHVVRQHTD REFPQDPREQ
LRMARDAVFS SWNNPRAIEY RRIYEIPDDI GTAVNVQTMV FGNTGERSAT GVGFTRNPAT
GAKEFYGEFL VNAQGEDVVA GIRTPQPIRE LERLMPEAYA QLREYTSTLE RHYQDVQDFE
FTIEDGRLYM LQTRSGKRTG YAAVVIATDL VDEGVVEPRQ ALLLVEPASL SQLLAPVFDP
AAWKAVAVAT RGLPASPGAA CGQAVFSADE AVRWSEHGKR VVLVRKETAP DDIHGMYVAE
GILTATGGMT SHAAVVGRQM GKPAVVGAGG LSIDEAGRTL RIGDQTIGEG DWLSFDGLSG
EVKIARIATR PSEILQVLAG EMRPESSDIH RRFTRLLEWA DRERRLEIRA NADLPDQAAL
AYAFGARGIG LCRTEHMFFG EDRLPIVQRM ILSQREADRR QALAELLPLQ REDFYGVFKA
MHGCPVTIRT IDPPLHEFLP KREEVMVDIA RLEAAGKTGR ELEEKLALLR RVEQLHEFNP
MLGHRGVRVG ITFPEITEMQ ARAIFEAACR LAREGQAVVP EIMIPLVSDV RELRDQKAIV
DRVAAEVTKA HGVEIPYLVG TMIEVPRGAL TADSIAREAR FFSFGTNDMT QLAFGFSRDD
IGKFLPAYRQ KKILERDPFA SLDVEGVGEL VRIAVEKGRR ARPDLALGVC GEHGGDPSSI
HFFEEVGLDY VSASPYRVPV ARLAAAQAAL KTRVGD
//
