ID U2L9N4_TRESO Unreviewed; 966 AA.
AC U2L9N4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
DE AltName: Full=Pyruvate, orthophosphate dikinase {ECO:0000256|ARBA:ARBA00032883};
GN Name=ppdK {ECO:0000313|EMBL:ERF59376.1};
GN ORFNames=HMPREF1325_0323 {ECO:0000313|EMBL:ERF59376.1};
OS Treponema socranskii subsp. socranskii VPI DR56BR1116 = ATCC 35536.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=1125725 {ECO:0000313|EMBL:ERF59376.1, ECO:0000313|Proteomes:UP000016412};
RN [1] {ECO:0000313|EMBL:ERF59376.1, ECO:0000313|Proteomes:UP000016412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VPI DR56BR1116 {ECO:0000313|EMBL:ERF59376.1,
RC ECO:0000313|Proteomes:UP000016412};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERF59376.1}.
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DR EMBL; AUZJ01000072; ERF59376.1; -; Genomic_DNA.
DR RefSeq; WP_021331651.1; NZ_AVQI01000060.1.
DR AlphaFoldDB; U2L9N4; -.
DR STRING; 1125725.HMPREF1325_0323; -.
DR PATRIC; fig|1125725.3.peg.2676; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000016412; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
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 Kinase {ECO:0000313|EMBL:ERF59376.1};
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:ERF59376.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERF59376.1}.
FT DOMAIN 24..60
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 66..303
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 308..359
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 427..506
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 547..889
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT REGION 925..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..966
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 460
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 851
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 765
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 789
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
SQ SEQUENCE 966 AA; 105359 MW; 21B8F66E7DCECAFF CRC64;
MAKTKLVYFF GNKKAEGNAD MRAELGGKGA NLAEMTNIGV PVPPGFTIST DVCKMYYDND
RKYPKELYSD VSANLVKLER AFGKKLGAED DPLLVSVRSG AAISMPGMMD TILNLGLNDK
SVLGLAKKTN NPRFAWDAYR RFIQMFGDVA MGVPHDEFEK ILSEAKARAG KKLDNELDTS
ELQEIVGKYK ALYQKTTGTE FPQDPEKQMW HAINAVFGSW MNARAIKYRE LNNIKGLKGT
AVTVMAMVFG NMGNDSGTGV CFSRSPSTGE NKFFGEYLIN AQGEDVVAGI RTPEEISQLK
KDNPKIYDEL IKIRNNLEKH YHDMQDMEFT VQQGKLYMLQ CRNGKRTGPA AVKMAVDMVG
EKLITKEEAI LRVDAEQIDQ LLHPMIDKDA AKRSGVIASG LNASPGAGCG QIVFTADEAE
KLAKEGKKVL LVRKETSPDD IAGMAAAQGI LTATGGRTSH AAVVARQMGK PCVSGVEAIQ
FSAGGITVNG KSYRQGDWLT IDGSTGNVYA GQIPTKEPQI TGDFGTFMKW CDEIRNGSVR
KVGKSTIKGF GVRANADQPD QAQAAFNFGA EGVGLCRTEH MFFDPAKLVY FQAMIASDTT
AAREKALAKI MPLQKKDFSG IFDAMKGRPV IIRFLDPPLH EFIPKDEEGT RKVQQVLKEE
GIDVSVETLT ARFNSLKEFN PMLGHRGCRL TITYPEIYKM QTEAVTLAAI ECKKRGVPVR
PMIMIPIVCE PTELATIRKE CEEVIAKIEK ESGMKVAIEI GTMIEVPRAA LLSGEIAKVA
DFYSFGSNDL TQLTFGFSRD DAGKFLDAYY HRNILDDDPF KTLDEKGVGK LMDMAVAAAR
EVKPEMHLGI CGEHGGDPAT IDFCYRVGLD YVSCSPYRVP IARLSAAQAV IRAVKAKKTA
AKKTAAKKAP AKKIAAKTVK KAAQKKAVGK TTAKASAKKA AGKKPVAKKA AAKKPVAKKT
AKKAKK
//
