P46893 (PPSA_STAMF) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Staphylothermus › Staphylothermus marinus

Protein attributes

Sequence length	834 AA.
Sequence status	Complete.
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: UniProtKB-UniPathway pyruvate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal 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 [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] [Europe PMC] [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]	"The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota." Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N. BMC Genomics 10:145-145(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43588 / DSM 3639 / F1.
[3]	"Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1." Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C. Stand. Genomic Sci. 1:183-188(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43588 / DSM 3639 / F1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S74619 Genomic DNA. Translation: AAB32888.1. CP000575 Genomic DNA. Translation: ABN69254.1.
PIR	S51006.
RefSeq	YP_001040162.1. NC_009033.1.
3D structure databases
ProteinModelPortal	P46893.
ModBase	Search...
Protein-protein interaction databases
STRING	399550.Smar_0141.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABN69254; ABN69254; Smar_0141.
GeneID	4907183.
KEGG	smr:Smar_0141.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0574.
HOGENOM	HOG000230912.
KO	K01007.
OMA	NVMERYL.
ProtClustDB	PRK06464.
Enzyme and pathway databases
BioCyc	SMAR399550:GHK2-186-MONOMER.
UniPathway	UPA00138.
Family and domain databases
Gene3D	3.20.20.60. 1 hit. 3.30.1490.20. 1 hit. 3.30.470.20. 1 hit.
InterPro	IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR008279. PEP-util_enz_mobile_dom. IPR006319. PEP_synth. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR002192. PPDK_PEP-bd. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
Pfam	PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF01326. PPDK_N. 1 hit. [Graphical view]
PIRSF	PIRSF000854. PEP_synthase. 1 hit.
SUPFAM	SSF52009. PEP_mobile. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
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:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program