ppsA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

PpsA

Synonyms

phosphoenolpyruvate synthase[1], B1702[2][1], PpsA[2][1], Pps[2][1] , ECK1700, JW1692, pps, b1702

Product description

PpsA[2][3];

Component of phosphoenolpyruvate synthase[2][3]

Phosphoenolpyruvate synthase[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0000166

nucleotide binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

PMID:4383554[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:16606699[6]

IPI: Inferred from Physical Interaction

UniProtKB:P60422

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002192

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013815

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0067

F

Seeded from EcoCyc (v14.0)

complete

GO:0006094

gluconeogenesis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006319

P

Seeded from EcoCyc (v14.0)

complete

GO:0006094

gluconeogenesis

PMID:4383555[7]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc (v14.0)

complete

GO:0008986

pyruvate, water dikinase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006319

F

Seeded from EcoCyc (v14.0)

complete

GO:0008986

pyruvate, water dikinase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.7.9.2

F

Seeded from EcoCyc (v14.0)

complete

GO:0008986

pyruvate, water dikinase activity

PMID:4383554[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0016310

phosphorylation

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000121

P

Seeded from EcoCyc (v14.0)

complete

GO:0016310

phosphorylation

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002192

P

Seeded from EcoCyc (v14.0)

complete

GO:0016310

phosphorylation

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008279

P

Seeded from EcoCyc (v14.0)

complete

GO:0016310

phosphorylation

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018274

P

Seeded from EcoCyc (v14.0)

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of phosphoenolpyruvate synthase

could be indirect

Protein

rplB

PMID:16606699[6]

Experiment(s):EBI-1140524

Protein

pgm

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

talB

PMID:19402753[8]

LCMS(ID Probability):99.6

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MSNNGSSPLV LWYNQLGMND VDRVGGKNAS LGEMITNLSG MGVSVPNGFA TTADAFNQFL
DQSGVNQRIY ELLDKTDIDD VTQLAKAGAQ IRQWIIDTPF QPELENAIRE AYAQLSADDE
NASFAVRSSA TAEDMPDASF AGQQETFLNV QGFDAVLVAV KHVFASLFND RAISYRVHQG
YDHRGVALSA GVQRMVRSDL ASSGVMFSID TESGFDQVVF ITSAWGLGEM VVQGAVNPDE
FYVHKPTLAA NRPAIVRRTM GSKKIRMVYA PTQEHGKQVK IEDVPQEQRD IFSLTNEEVQ
ELAKQAVQIE KHYGRPMDIE WAKDGHTGKL FIVQARPETV RSRGQVMERY TLHSQGKIIA
EGRAIGHRIG AGPVKVIHDI SEMNRIEPGD VLVTDMTDPD WEPIMKKASA IVTNRGGRTC
HAAIIARELG IPAVVGCGDA TERMKDGENV TVSCAEGDTG YVYAELLEFS VKSSSVETMP
DLPLKVMMNV GNPDRAFDFA CLPNEGVGLA RLEFIINRMI GVHPRALLEF DDQEPQLQNE
IREMMKGFDS PREFYVGRLT EGIATLGAAF YPKRVIVRLS DFKSNEYANL VGGERYEPDE
ENPMLGFRGA GRYVSDSFRD CFALECEAVK RVRNDMGLTN VEIMIPFVRT VDQAKAVVEE
LARQGLKRGE NGLKIIMMCE IPSNALLAEQ FLEYFDGFSI GSNDMTQLAL GLDRDSGVVS
ELFDERNDAV KALLSMAIRA AKKQGKYVGI CGQGPSDHED FAAWLMEEGI DSLSLNPDTV
VQTWLSLAEL KK
Length

792

Mol. Wt

87.434 kDa

pI

4.8 (calculated)

Extinction coefficient

65,320 - 66,320 (calc based on 18 Y, 7 W, and 8 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Initiator Methionine

1

Removed

UniProt:P23538

Modification Site

419

phosphorylation site at T419

probability greater than 75%

PMID:17938405[9]

Domain

379..460

PF00391 PEP-utilising enzyme, mobile domain

PMID:19920124[10]

Domain

468..792

PF02896 PEP-utilising enzyme, TIM barrel domain

PMID:19920124[10]

Domain

18..361

PF01326 Pyruvate phosphate dikinase, PEP/pyruvate binding domain

PMID:19920124[10]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=pps taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16129658

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946209

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P23538

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946209

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 Cooper, RA & Kornberg, HL (1967) The direct synthesis of phosphoenolpyruvate from pyruvate by Escherichia coli. Proc. R. Soc. Lond., B, Biol. Sci. 168 263-80 PubMed
  6. ↑ 6.0 6.1 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  7. ↑ Brice, CB & Kornberg, HL (1967) Location of a gene specifying phosphopyruvate synthase activity on the genome of Escherichia coli, K12. Proc. R. Soc. Lond., B, Biol. Sci. 168 281-92 PubMed
  8. ↑ 8.0 8.1 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  9. ↑ Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed
  10. ↑ 10.0 10.1 10.2 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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