ID A0A0G3EK46_9BACT Unreviewed; 916 AA.
AC A0A0G3EK46;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:AKJ65180.1};
GN ORFNames=L21SP4_01945 {ECO:0000313|EMBL:AKJ65180.1};
OS Kiritimatiella glycovorans.
OC Bacteria; Kiritimatiellota; Kiritimatiellia; Kiritimatiellales;
OC Kiritimatiellaceae; Kiritimatiella.
OX NCBI_TaxID=1307763 {ECO:0000313|EMBL:AKJ65180.1, ECO:0000313|Proteomes:UP000035268};
RN [1] {ECO:0000313|Proteomes:UP000035268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Fru-AB {ECO:0000313|Proteomes:UP000035268};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of the first cultured
RT representative of the subdivision 5 of the Verrucomicrobia phylum.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKJ65180.1, ECO:0000313|Proteomes:UP000035268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Fru-AB {ECO:0000313|EMBL:AKJ65180.1,
RC ECO:0000313|Proteomes:UP000035268};
RX PubMed=27300277; DOI=10.1038/ismej.2016.84;
RA Spring S., Bunk B., Sproer C., Schumann P., Rohde M., Tindall B.J.,
RA Klenk H.P.;
RT "Characterization of the first cultured representative of Verrucomicrobia
RT subdivision 5 indicates the proposal of a novel phylum.";
RL ISME J. 10:2801-2816(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP010904; AKJ65180.1; -; Genomic_DNA.
DR RefSeq; WP_052882443.1; NZ_CP010904.1.
DR AlphaFoldDB; A0A0G3EK46; -.
DR STRING; 1307763.L21SP4_01945; -.
DR KEGG; vbl:L21SP4_01945; -.
DR PATRIC; fig|1609981.3.peg.2021; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000035268; 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; 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; 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; 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:AKJ65180.1};
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:AKJ65180.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035268};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AKJ65180.1}.
FT DOMAIN 63..303
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 315..357
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 448..529
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 569..912
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 481
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 874
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 603
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 659
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 788
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 788
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 809
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 810
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 811
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 812
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 812
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 916 AA; 101292 MW; 4CB01182E33FDFAA CRC64;
MAKKYVYFYG LSEEQTEGDR SMKAILGGKG ANLAEMSNAG LPVPPGFTLS TEACKYYSEH
GGKYPQGLEK EIRAHLDQLE KGMGKKLGDP DNPLLVSVRS GAAISMPGMM DTVLNLGLND
KSVQGFIKQT GSERAGWDCY RRFIDMFGDV VMGPYTGLKH EHFEHEIEKL KKKYGAKEDT
DLTAEQLKEL VGIYKKVYQD KVKKPFPQDP EQQLDLSIRA VFGSWDSDRA VKYRQINKIS
GLLGTAVNVC TMVFGNMGDD CGTGVAFTRD PSTGESVAYG DYLKNAQGED VVAGIRTPKH
MNDMAKDKSP AWRKTHKELI QIMKRLEKHY KHPQDIEFTV ERGKLWLLQT RNAKRTGIAG
VRWAVEMATG KDVFTGKKQT KILSQKDALM NVGGSDLEQL LFPVFDMKEE KKANVIAEGL
PAGPGAASGT IVFDADDAEA AVEKDKNARV ILVRRDTSPE DVGGMWAARG VLTSTGGMTS
HAAVVARGWG KCCICGASAL NIDYKKKQVT VGKKVYKEGD SISLNGSTGK VYEGEIPLQS
SPVVEAVIGG KAAAKKHPYY RMYEMLSGWS DTHRKMKVRT NADAPKDAAA AKGFGAEGIG
LCRTEHMFFE GDRIWSIREF ILAEDREGRE KALKDLLKHQ QKDFEGIFKE MDGLPVTVRL
LDPPLHEFVP HEKKEQQEMA RRLGVSARKV ADRVRQLHEF NPMLGHRGCR LSITYPELCV
MQTKAIIGAA CKVSKLKNAV KVHPEIMVPL VGSKTELDYL ENVIRTTADE IIERTGAKVK
YMVGTMIEVP RAALTADQIA DRAEFFSFGT NDLTQMTFGF SRDDVGTFLP EYTNRKILDV
DPFQHLDQEG VGQLVKMGVE RGRSVRGDLK CGICGEHGGD PDSVRFCYES GLDYVSCSPY
RVPIARLAAA QAAIEE
//
