ID Q57EM2_BRUAB Unreviewed; 887 AA.
AC Q57EM2;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 114.
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 Name=ppdK {ECO:0000313|EMBL:AAX73912.1};
GN OrderedLocusNames=BruAb1_0522 {ECO:0000313|EMBL:AAX73912.1};
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698 {ECO:0000313|EMBL:AAX73912.1, ECO:0000313|Proteomes:UP000000540};
RN [1] {ECO:0000313|EMBL:AAX73912.1, ECO:0000313|Proteomes:UP000000540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941 {ECO:0000313|EMBL:AAX73912.1,
RC ECO:0000313|Proteomes:UP000000540};
RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of pyruvate and
CC phosphate. {ECO:0000256|ARBA:ARBA00003144}.
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; AE017223; AAX73912.1; -; Genomic_DNA.
DR RefSeq; WP_002969462.1; NC_006932.1.
DR AlphaFoldDB; Q57EM2; -.
DR SMR; Q57EM2; -.
DR EnsemblBacteria; AAX73912; AAX73912; BruAb1_0522.
DR GeneID; 3788861; -.
DR KEGG; bmb:BruAb1_0522; -.
DR HOGENOM; CLU_015345_0_2_5; -.
DR Proteomes; UP000000540; Chromosome I.
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; 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; 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:AAX73912.1};
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:AAX73912.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..58
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 63..298
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 315..370
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 436..516
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 531..883
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 468
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 844
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 574
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 630
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 758
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 758
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 779
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 780
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 781
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 782
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 782
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 887 AA; 96298 MW; 9C2228DDF5B6834D CRC64;
MAKWVYTFGD GKAEGAASDR NLLGGKGANL AEMSSLGLPV PPGFTITTEV CTYYYNNDRV
YPSELDAQVQ AALAHIATLT GRNFGDAEKP LLVSVRSGAR ASMPGMMDTV LNLGLNDETV
QAIARESGDE RFAYDSYRRF IQMYSDVVLG VDHGFFEEIL EDTKADLGVE VDTALSADDW
KNVIGLYKAK VEEELGQPFP QDPREQLWGA IGAVFSSWMN ARAITYRRLH NIPAAWGTAV
NVQAMVFGNM GETSATGVAF TRNPSTGENK LYGEFLVNAQ GEDVVAGIRT PQNITEEARI
AAGSDKPSLE KVMPEAFAEF LKVANRLEQH YRDMQDLEFT IERGKLWMLQ TRSGKRTARA
ALKMAVEMAA EGLISEEEAV LRIDPAALDQ LLHPTIDPRA ERQVVGMGLP ASPGAATGEI
VFSSEEAEQA KAEGRNVILV RIETSPEDIH GMHAAEGILT TRGGMTSHAA VVARGMGKPC
VSGAGSLRVD YRNGTMLAAG QTFRKGDVIT IDGASGQVLK GSVAMLQPEL SGDFGKLMEW
ADRARRMKVR ANAETPADAR TARSFGAEGI GLCRTEHMFF DGSRIVAMRE MILSDTEEGR
RLALGKLLPM QRSDFAELFE IMKGLPVTIR LLDPPLHEFL PHTDEEVDEV ARSMGVDAAK
LRDRADALHE FNPMLGHRGC RLAVSYPEIA EMQARAIFEA AVEAGKKTGE PVVPEVMVPL
VGLKAELDFV KARIDAVAKE VMSEAGIKID YMVGTMIELP RAALRAAEIA ESAEFFSFGT
NDLTQTTFGI SRDDAAGFLT TYQNRGVIEQ DPFVSLDVDG VGELVQIAAE RGRKTREKIK
LGICGEHGGD PASIAFCEKT GLDYVSCSPF RVPIARLAAA QAAVRKV
//
