ID D5SPA2_PLAL2 Unreviewed; 907 AA.
AC D5SPA2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Plim_2420 {ECO:0000313|EMBL:ADG68246.1};
OS Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS (Planctomyces limnophilus).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctopirus.
OX NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG68246.1, ECO:0000313|Proteomes:UP000002220};
RN [1] {ECO:0000313|EMBL:ADG68246.1, ECO:0000313|Proteomes:UP000002220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC {ECO:0000313|Proteomes:UP000002220};
RX PubMed=21304691; DOI=10.4056/sigs.1052813;
RA Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT 290).";
RL Stand. Genomic Sci. 3:47-56(2010).
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; CP001744; ADG68246.1; -; Genomic_DNA.
DR RefSeq; WP_013110677.1; NC_014148.1.
DR AlphaFoldDB; D5SPA2; -.
DR STRING; 521674.Plim_2420; -.
DR KEGG; plm:Plim_2420; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_0; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000002220; 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; 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:ADG68246.1};
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:ADG68246.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADG68246.1}.
FT DOMAIN 22..59
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 65..299
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 313..366
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 442..522
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 553..901
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 474
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 863
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 596
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 650
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 777
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 777
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 798
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 799
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 800
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 801
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 801
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 907 AA; 98892 MW; 4F001AF6C757808B CRC64;
MSTKYVYFFG AGKADGNAKM KNELGGKGAN LAEMTNIGLP VPAGFTISTE VCTYYYAHEK
TYPPELEAQV DAAMAQVEKA MGKKFGDTTD PLLVSCRSGA RESMPGMMDT VLNIGLNDVT
VEALTKASGN ERFAWDSYRR FVQMYGDVVM GLKPEKKTDI DPFEELLEKK KHAAGVHFDN
ELSVAQLKEL VAEFKAAIKA KTGLDFPTDP KKQVWGAVGA VFSSWMNDRA IVYRRTYGIP
HEWGTAVNVQ AMVFGNLGDD CATGVALTRD GALGTPGYCG DYLINAQGED VVAGIRTPLR
IEETLAKDMP KAFEELDSIG KILEGHYKDV QDIEFTVEKG KVWMLQTRNA KRTGFAAVRI
AVDLVEEGKI TDKEAISPKR IPADDLNQLL QPVFDLAGKK AAQAGGKLLT KGINAGPGAA
FGQIVFHADD AEAIFLKNPK AELVLVRRET TPEDLRGMKV AKGILTAFGG ASSHAALVSR
QMGKVCVVGA SELNIDYEKA TVTVGGKTLK EGDFISIDGF TGEVFEGKVD TKPSEVIQVL
ISKTMKPEES ETYQRFAKLM SWADKYRTLK VRTNADEPKQ ATQAVSFGAE GIGLCRTEHM
FFDHVDEFRE MILAGDLPSR EKALAKLLPF QREDFYGLFK AMNGLPVTIR LLDPPLHEFL
PHDHASQADL AAKIGIPADY ISRRVHELHE SNPMLGHRGC RLGIVYPEIT AMQARAIFEA
ACKLKKEGLT VIPEVMIPLV GYVAEFKNQE KVVREQAEKV FAETGESVEY LVGTMVEVPR
ACATADQIAG AAEFFSFGTN DLTQTTLGIS RDDYGGFINH YKENDIVPND PFQMIDQAGV
GTLMKMGVEK GRSGRPGLKI GICGEHGGEP SSVVFCHKIG LDYVSCSPFR VPIARLAAAQ
AALADAK
//
