Reviewed, UniProtKB/Swiss-Prot P46893 (PPSA_STAMF)

Names and origin

Protein names

Recommended name:
    Probable phosphoenolpyruvate synthase
      Short name=PEP synthase
    EC=2.7.9.2
Alternative name(s):
    Pyruvate, water dikinase

Gene names

Name:	ppsA
Ordered Locus Names:	Smar_0141

Organism

Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP]

Taxonomic identifier

399550 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Staphylothermus

Protein attributes

Sequence length	834 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate By similarity.
Catalytic activity	ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate.
Cofactor	Magnesium By similarity.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homooligomer. Forms a large complex of about 2000 kDa.
Domain	The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.
Post-translational modification	The N-terminus is blocked.
Miscellaneous	The reaction takes place in three steps, mediated by a phosphocarrier 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 By similarity.
Sequence similarities	Belongs to the PEP-utilizing enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: InterPro phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyruvate, water 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 – 834	834	Probable phosphoenolpyruvate synthase		PRO_0000147038
Sites
	Active site	447	1	Tele-phosphohistidine intermediate By similarity
	Active site	772	1	Proton donor By similarity
	Metal binding	699	1	Magnesium By similarity
	Metal binding	723	1	Magnesium By similarity
	Binding site	550	1	Substrate By similarity
	Binding site	598	1	Substrate By similarity
	Binding site	699	1	Substrate By similarity
	Binding site	720	1	Substrate; via carbonyl oxygen By similarity
	Binding site	721	1	Substrate; via amide nitrogen By similarity
	Binding site	722	1	Substrate By similarity
	Binding site	723	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P46893-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4F6C80446D4D327C	FASTA	834	93,736
	10 20 30 40 50 60 MSNVPKEKRF IVWLDEVTKD DVVLVGGKNA NLGEMIRAGI PVPPGFAVTA YAYKYFIEKT 70 80 90 100 110 120 GLKDKIYPLL NSIDVNDKKV LDETTAKIRQ WIMDTPMPPE VEEEIRKYYR ELAKKIGMEP 130 140 150 160 170 180 EKLRVAVRSS ATAEDMPEAS FAGQQDTYLN VYGEDNVVYY VKRCWASLFT SRAVFYRVAQ 190 200 210 220 230 240 GIPHEKSLMS VTVQKMVNSR TAGVMFTLHP VTGDEKVVVI EASWGLGESV VGGKVTPDEW 250 260 270 280 290 300 VVDKQTLQIV DQKIHHKTLA IVFDPKKGKN VEIRWDENKQ AWVSEEGPVD IEMVKHFHPD 310 320 330 340 350 360 KPALKEEEVK RLAELALLIE KHYGRHMDIE WAVDYDIPFP DNVFIVQARL ETVWSVRKEK 370 380 390 400 410 420 EKAEKKAEIK GKNIVKLSEA KVLVRGLPAS PGIGAGVAKV IFDPHSKEAQ EFKEGEVLVT 430 440 450 460 470 480 KMTDPDWVPL MKKAVAIVTD EGGMTSHAAI VSRELGIPAI VGTGNATQVI KSGIEVTVDG 490 500 510 520 530 540 SRGVVYEGIV EDLVKPKEEV KAEVAGVGIS PEQLLPLYPV TATKIYMNLG EPDAIEKYKD 550 560 570 580 590 600 LPFDGIGLMR IEFIITDWVQ YHPLYLIEQG KESLFIDKLA EGIAKVAQAI YPRPVVVRFS 610 620 630 640 650 660 DFKTNEYRGL KGGEKYEPEE RNPMIGWRGV SRYIHPKYEP AFRLEVRAIK KVREEMGLTN 670 680 690 700 710 720 VWVMFPFVRT TWELERALKI MEEEGLKRGK DFKVWAMAEV PSIVLLADKF AEYVDGFSIG 730 740 750 760 770 780 SNDLTQLILG ADRDSNILAE MGYFDERDPA VLAGIKMIIE KAHSKGATVS ICGQAPSVYP 790 800 810 820 830 EIVEFLVEAG IDSISVNPDA VIATRRLVAS IERKIMLKRL NKIMDKLNKL ELGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of a multimeric protein, homologous to the PEP-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium." Cicicopol C., Peters J., Kellermann J., Baumeister W. FEBS Lett. 356:345-350(1994) [PubMed: 7805870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 296-320; 528-546; 625-636; 638-647; 657-661; 682-694; 698-720 AND 742-752.
[2]	"Complete sequence of Staphylothermus marinus F1." Copeland A., Lucas S., Lapidus A., Barry K., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Huber H., Woese C., Anderson I.J., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	S74619 Genomic DNA. Translation: AAB32888.1. CP000575 Genomic DNA. Translation: ABN69254.1.
PIR	S51006.
RefSeq	YP_001040162.1.
3D structure databases
HSSP	HSSP built from PDB template 1H6Z based on UniProtKB O76283.
ModBase	Search...
Protein-protein interaction databases
STRING	P46893.
Genome annotation databases
GeneID	4907183.
GenomeReviews	Gene locus Smar_0141 in contig CP000575_GR.
KEGG	smr:Smar_0141.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	NKYVGIC.
Family and domain databases
InterPro	IPR013815. ATP_grasp_subdomain_1. IPR008279. PEP_mobile. IPR018274. PEP_mobile_CS. IPR006319. PEP_synth. IPR000121. PEP_utilizers. IPR002192. PPDK_PEP_bd. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
Pfam	PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF01326. PPDK_N. 1 hit. [Graphical view]
ProDom	PD000940. PEP_utilizers. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01418. PEP_synth. 1 hit.
PROSITE	PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPSA_STAMF

Accession

Primary (citable) accession number: P46893
Secondary accession number(s): A3DKU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)