P37213 (PPDK_ENTHI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate, phosphate dikinase
EC=2.7.9.1

Alternative name(s):
Pyruvate, orthophosphate dikinase

Gene names

Name:

PPDK

Organism

Entamoeba histolytica

Taxonomic identifier

5759 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Archamoebae › Entamoebidae › Entamoeba

Protein attributes

Sequence length	885 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.
Catalytic activity	ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by light-induced dephosphorylation. Inhibited by dark-induced phosphorylation. Both reactions are catalyzed by PDRP1 By similarity.
Subunit structure	Homodimer By similarity.
Domain	The N-terminal domain contains the ATP/Pi active site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate active site By similarity.
Post-translational modification	Phosphorylation of Thr-452 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme By similarity.
Miscellaneous	The reaction takes place in three steps, each mediated by a carrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain.
Sequence similarities	Belongs to the PEP-utilizing enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	pyruvate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyruvate, phosphate dikinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 885	885	Pyruvate, phosphate dikinase		PRO_0000147051
Regions
	Region	1 – 342	342	N-terminal
	Region	343 – 399	57	Linker 1
	Region	400 – 497	98	Central
	Region	498 – 533	36	Linker 2
	Region	534 – 885	352	C-terminal
Sites
	Active site	454	1	Tele-phosphohistidine intermediate By similarity
	Active site	839	1	Proton donor By similarity
	Metal binding	752	1	Magnesium By similarity
	Metal binding	776	1	Magnesium By similarity
	Binding site	91	1	ATP Potential
	Binding site	561	1	Substrate By similarity
	Binding site	617	1	Substrate By similarity
	Binding site	752	1	Substrate By similarity
	Binding site	773	1	Substrate; via carbonyl oxygen By similarity
	Binding site	774	1	Substrate; via amide nitrogen By similarity
	Binding site	775	1	Substrate By similarity
	Binding site	776	1	Substrate; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	452	1	Phosphothreonine; by PDRP1 By similarity
Experimental info
	Sequence conflict	539 – 540	2	AG → NA in AAA19026. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P37213 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 6F5FEAD7C21CC8DC	FASTA	885	98,060
	10 20 30 40 50 60 MQRVYAFEDG DGTNKKLLGG KGAGLCTMTK IGLPVPQGFV ITTEMCKQFI ANGNKMPEGL 70 80 90 100 110 120 MEEVKKEYQL VEKKSGKVFG GEENPLLVSV RSGAAMSMPG MMDTILNLGL NDKTVVALAK 130 140 150 160 170 180 LTNNERFAYD SYRRFVSLFG KIALNACDEV YDKTLENKKV EKGVKLDTEL DANDMKELAQ 190 200 210 220 230 240 VFIKKTEEFT KQPFPVDPYA QLEFAICAVF RSWMGKRAVD YRREFKITPE QADGTAVSVV 250 260 270 280 290 300 SMVYGNMGND SATGVCFTRD PGTGENMFFG EYLKNAQGED VVAGIRTPQI ISKMAEDRDL 310 320 330 340 350 360 PGCYEQLLDI RKKLEGYFHE VQDFEFTIER KKLYMLQTRN GKMNATATVR TGVDMVEEGL 370 380 390 400 410 420 ITKEQAIMRI APQSVDQLLH KNMPANYAEA PLVKGLPASP GAATGAVVFD ADDAVEQAKG 430 440 450 460 470 480 KKVLLLREET KPEDIHGFFV AEGILTCRGG KTSHAAVVAR GMGKPCVSGA EGIKVDVAKK 490 500 510 520 530 540 IAKIGSLEVH EGDILTIDGS TGCVYKGEVP LEEPQVGSGY FGTILKWANE IKKIGVFAAG 550 560 570 580 590 600 DLPSAAKKAL EFGAEGIGLC RTERMFNAVE RLPIVVKMIL SNTLEERKKY LNELMPLQKQ 610 620 630 640 650 660 DFIGLLKTMN GLPVTVRLLD PPLHEFLPTL EELMREIFEM KLSGKTEGLA EKEVVLKKVK 670 680 690 700 710 720 ELMEVNPMIG HRGIRLGTTN PEIYEMQIRA FLEATREVIK EGINDHREIM IPNVTEVNEL 730 740 750 760 770 780 INLRKNVLEP VHEEVEKKYG IKVPFSYGTM VECVRAALTA DKIATEASFF SFGTNDLTQG 790 800 810 820 830 840 TFSYSREDSE NKFIPKYVEL KILPANPFEI LDRPGVGEVM RIAVTKGRQT RPELLVGICG 850 860 870 880 EHGGEPSSIE WCHMIGLNYV SCSSYRIPVA RIAAAQAQIR HPREN

References

[1]	"Primary structure of the pyruvate phosphate dikinase in Entamoeba histolytica." Bruchhaus I., Tannich E. Mol. Biochem. Parasitol. 62:153-156(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 30459 / HM-1:IMSS.
[2]	"Partial nucleotide sequence of the enzyme pyruvate, orthophosphate dikinase of Entamoeba histolytica HM1:IMSS." Saavedra-Lira E., Robinson O., Perez-Montfort R. Arch. Med. Res. 23:39-40(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 442-626. Strain: ATCC 30459 / HM-1:IMSS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74596 Genomic DNA. Translation: CAA52673.1. L03389 Unassigned DNA. Translation: AAA19026.1.
PIR	S36601.
3D structure databases
ProteinModelPortal	P37213.
SMR	P37213. Positions 2-881.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG0574.
Enzyme and pathway databases
BRENDA	2.7.9.1. 2080.
SABIO-RK	P37213.
Family and domain databases
Gene3D	3.20.20.60. 1 hit. 3.30.1490.20. 2 hits. 3.30.470.20. 1 hit.
InterPro	IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR008279. PEP-util_enz_mobile_dom. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR002192. PPDK_PEP-bd. IPR010121. Pyruvate_phosphate_dikinase. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
PANTHER	PTHR22931:SF9. PTHR22931:SF9. 1 hit.
Pfam	PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF01326. PPDK_N. 1 hit. [Graphical view]
PIRSF	PIRSF000853. PPDK. 1 hit.
SUPFAM	SSF52009. PEP_mobile. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01828. pyru_phos_dikin. 1 hit.
PROSITE	PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPDK_ENTHI

Accession

Primary (citable) accession number: P37213

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)