ID F2NUY5_TRES6 Unreviewed; 965 AA.
AC F2NUY5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=Tresu_0123 {ECO:0000313|EMBL:AEB13089.1};
OS Treponema succinifaciens (strain ATCC 33096 / DSM 2489 / 6091).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=869209 {ECO:0000313|EMBL:AEB13089.1, ECO:0000313|Proteomes:UP000006852};
RN [1] {ECO:0000313|EMBL:AEB13089.1, ECO:0000313|Proteomes:UP000006852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33096 / DSM 2489 / 6091
RC {ECO:0000313|Proteomes:UP000006852};
RX PubMed=21886863;
RA Han C., Gronow S., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Zeytun A., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Mikhailova N.,
RA Huntemann M., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Treponema succinifaciens type strain (6091).";
RL Stand. Genomic Sci. 4:361-370(2011).
RN [2] {ECO:0000313|Proteomes:UP000006852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33096 / DSM 2489 / 6091
RC {ECO:0000313|Proteomes:UP000006852};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Treponema succinifaciens DSM 2489.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CP002631; AEB13089.1; -; Genomic_DNA.
DR RefSeq; WP_013700400.1; NC_015385.1.
DR AlphaFoldDB; F2NUY5; -.
DR STRING; 869209.Tresu_0123; -.
DR KEGG; tsu:Tresu_0123; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_12; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000006852; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
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; 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.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:AEB13089.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006852};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEB13089.1}.
FT DOMAIN 23..303
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 312..365
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 431..511
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 542..889
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT REGION 906..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 464
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 852
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 582
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 638
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 766
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 766
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 787
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 788
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 789
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 790
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 790
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 965 AA; 104629 MW; 186915371809C3EF CRC64;
MAKTKYVYYF GDGDAEGDES MRPILGGKGA NLAQMAKKPL SLPVPSGFTI SIDVCQEYYK
LGKKYPAGLD AEVAKYLAKL EKSMGKKLGD AKDPLLVSVR SGAAESMPGM MDTILNLGLN
DNSVLGLANK TQNPRFAWDA YRRFIQMYGN VAMGVDHDKF EEIIDEVKSH RGITQDTDLT
TEELQEIVSK YKAMYKKEKG EDFPQDPHKQ MWGAIGAVFG SWMNPRAITY RKLNNIDERV
IKGTAVTVMA MVFGNMGDTS GTGVCFSRDP STGVNEFMGE YLMNAQGEDV VAGIRTPQHL
SQLAETNPKI YDQLCKIRAR LEKHYHDMQD MEFTVQEGTL YMLQCRNGKR TGPAAVKMAV
DMVAEKLITK EQALLRVKPD QLDQLLHPQF EPKALKAAAP IAEALNASPG AGAGQIVFTA
DEAVEWNKAG KKVMLVRKET SPDDIAGMYV AEGILTSTGG RTSHAAVVAR GMGTPCVCGC
AAVVFVDKET VKIGDKTFKK GDNISIDGST GKVYAGLIPV EEAKVSGDLE TFLGWADEIR
EKSVRKTASG KTVKGFDVLA NAEQNEAPQA FKFGANGIGL CRTEHMFFEE PKLSSFQKMI
ISENTEARKE NLAKILPLQE RDFYGIIKAM GGRAVTIRLL DPPLNEFIQA ATDVEAQALA
SKLGVSVATI KAKFADLNEH NPMLGHRGCR LAITYPEIYE MQVEAIALAT AHAEKDGIAH
DVRIMIPNVT SVNELKQIRA QAEAVIAKVN ETKGTNLKFQ IGSMIEFPRA ACTADQIAQY
ADFFSFGTND LTQTTFGFSR DDYGKFIDSY LDQKILEKDP FKTLDPDGPG ALMEIAEAKG
RSVKSDLHLG ICGEHGGDPD SIALCYKLGL NYVSCSPFRV PAARLAGAQA VIKALAAAKA
AKAPAKKPAA KKAVAEKKTS TAKKPATKAP AKKAPAKKPA AKSTAKKPAA KAPAKKAPAK
KTTKK
//
