ID G4T0V6_META2 Unreviewed; 916 AA.
AC G4T0V6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:CCE23390.1};
GN OrderedLocusNames=MEALZ_1703 {ECO:0000313|EMBL:CCE23390.1};
OS Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylotuvimicrobium.
OX NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE23390.1, ECO:0000313|Proteomes:UP000008315};
RN [1] {ECO:0000313|Proteomes:UP000008315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC {ECO:0000313|Proteomes:UP000008315};
RX PubMed=22207753; DOI=10.1128/JB.06392-11;
RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA Trotsenko Y.A., Kalyuzhnaya M.G.;
RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT Methylomicrobium alcaliphilum 20Z.";
RL J. Bacteriol. 194:551-552(2012).
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; FO082060; CCE23390.1; -; Genomic_DNA.
DR RefSeq; WP_014148183.1; NC_016112.1.
DR AlphaFoldDB; G4T0V6; -.
DR SMR; G4T0V6; -.
DR STRING; 1091494.MEALZ_1703; -.
DR KEGG; mah:MEALZ_1703; -.
DR PATRIC; fig|271065.3.peg.1746; -.
DR HOGENOM; CLU_015345_0_2_6; -.
DR Proteomes; UP000008315; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
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:InterPro.
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; 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; 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};
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:CCE23390.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCE23390.1}.
FT DOMAIN 19..57
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 62..291
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 519..906
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT COILED 292..326
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 454
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 867
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 780
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 780
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 801
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 802
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 803
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"
SQ SEQUENCE 916 AA; 101717 MW; 417C487BC9B9F7E4 CRC64;
MTEKYIYSFQ KGDGKNKMLL GGKGANLCEM TQIGLNVPPG FVITTTACLD YINNQRLPDG
LMDEVKAHIT EVETQTEKQF GGRDNPLLVS VRSGSAISMP GMMDTILNLG LNKQTLAGLI
DQTGDPRFAY DAYRRFIQLF GKVALGIDDE KFDQHFDAIK KQAGIKADVG LDSEHLRQIS
ELFLQVVHEE TGKPFPEDVY EQLELSIKAV FNSWMGKRAV DYRREFHITP KMANGTAVNV
VTMVFGNMGN DCATGVGFTR NPGTGANEMY GEYLVNAQGE DVVAGIRTPK PVHELANEMP
DLYRQLVELR NKLETHYKEV QDYEYTIERG ILYCLQTRNG KMNAAAMVRT SVEMVAEGLI
DKKRALLRIN PELLEQLLHP QLDPNSTAEA VAQGLPASPG AACGKCVFEA DTAEQLGRAG
EAVILLREET KPEDIHGFFA AQGILTSRGG KTSHAAVVAR GMGKACVAGA EDIKIDVRSR
QAIIGELHIR EGDMITIDGS TGLIFLGRIP TIEPSFSDEL KTLLSWADEV AELEVHANVD
TPERARLAAS YGATGIGLCR TERMFNASDR LPLVIDMILA GNKEARQEAL AKLFPIQRDD
FQELFEAMSP YPVTVRLLDP PMHEFLPGEH QLEDEIRALN QYKIMIQGQQ VTLDTLGSHA
LLPSPFNHLN EEVINKAIAK KELMLSKVKE LYEVNPMLGH RGVRLGMSYP EIYQMQIRSI
LEAAALCIKQ RKPILPEIMV PQVITVQELI KVKSYVDQIQ KEVEKQYGID LEFKFGTMVE
TVRACTRAAK LADVAEFFSF GTNDLTQATF SFSREDAENK FLPLYNESGL LADNPFEVLD
AKGVGQLMKM TVESGRQTRP DIKVGICGEQ GGHPESIRFC HHIKLDYVSC SAPRIPIARL
AAAHAKLLEN EYNIEY
//
