Phosphoenolpyruvate carboxylase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P00864 (CAPP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 130. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphoenolpyruvate carboxylase
Short name=PEPC
Short name=PEPCase
EC=4.1.1.31

Gene names

Name:	ppc
Synonyms:	glu
Ordered Locus Names:	b3956, JW3928

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	883 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. HAMAP-Rule MF_00595
Catalytic activity	Phosphate + oxaloacetate = H₂O + phosphoenolpyruvate + HCO₃^-. HAMAP-Rule MF_00595
Cofactor	Magnesium By similarity.
Enzyme regulation	The enzyme has distinct binding sites for each of the allosteric effectors such as acetyl-CoA, fructose 1,6-bisphosphate, guanosine 3'-diphosphate 5'-diphosphate, long chain fatty acids, and L-aspartate. HAMAP-Rule MF_00595
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the PEPCase type 1 family.

Ontologies

Keywords
Biological process	Carbon dioxide fixation
Ligand	Magnesium
Molecular function	Lyase
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbon fixation Inferred from electronic annotation. Source: HAMAP oxaloacetate metabolic process Inferred from electronic annotation. Source: HAMAP tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphoenolpyruvate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
uvrA	P0A698	1	EBI-1133741,EBI-552091

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 883

883

Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595

PRO_0000166592

Sites

Active site

138

Active site

546

By similarity

Experimental info

Mutagenesis

138

H → N: Loss of activity. Ref.8

Mutagenesis

579

H → N: 29% of wild-type activity. Ref.7

Mutagenesis

579

H → P: 5.4% of wild-type activity. Ref.7

Mutagenesis

587

R → S: Loss of activity. Ref.9

Secondary structure

883

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00864 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 2620A776CF1F2EBC
Show »

FASTA

883

99,063

        10         20         30         40         50         60 
MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILERVETIRK LSKSSRAGND ANRQELLTTL 

        70         80         90        100        110        120 
QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKNQPELSED 

       130        140        150        160        170        180 
TIKKAVESLS LELVLTAHPT EITRRTLIHK MVEVNACLKQ LDNKDIADYE HNQLMRRLRQ 

       190        200        210        220        230        240 
LIAQSWHTDE IRKLRPSPVD EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVEF 

       250        260        270        280        290        300 
VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQVLVSEL SMVEATPELL 

       310        320        330        340        350        360 
ALVGEEGAAE PYRYLMKNLR SRLMATQAWL EARLKGEELP KPEGLLTQNE ELWEPLYACY 

       370        380        390        400        410        420 
QSLQACGMGI IANGDLLDTL RRVKCFGVPL VRIDIRQEST RHTEALGELT RYLGIGDYES 

       430        440        450        460        470        480 
WSEADKQAFL IRELNSKRPL LPRNWQPSAE TREVLDTCQV IAEAPQGSIA AYVISMAKTP 

       490        500        510        520        530        540 
SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNANDVMTQ LLNIDWYRGL IQGKQMVMIG 

       550        560        570        580        590        600 
YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP 

       610        620        630        640        650        660 
PGSLKGGLRV TEQGEMIRFK YGLPEITVSS LSLYTGAILE ANLLPPPEPK ESWRRIMDEL 

       670        680        690        700        710        720 
SVISCDVYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA 

       730        740        750        760        770        780 
WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FAKADLWLAE 

       790        800        810        820        830        840 
YYDQRLVDKA LWPLGKELRN LQEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNIYTDPLN 

       850        860        870        880 
VLQAELLHRS RQAEKEGQEP DPRVEQALMV TIAGIAAGMR NTG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of phosphoenolpyruvate carboxylase of Escherichia coli. Nucleotide sequence of the ppc gene and deduced amino acid sequence." Fujita N., Miwa T., Ishijima S., Izui K., Katsuki H. J. Biochem. 95:909-916(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Structural and biochemical characterization of the Escherichia coli argE gene product." Meinnel T., Schmitt E., Mechulam Y., Blanquet S. J. Bacteriol. 174:2323-2331(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37. Strain: K12.
[6]	"Promoter analysis of the phosphoenolpyruvate carboxylase gene of Escherichia coli." Izui K., Miwa T., Kajitani M., Fujita N., Sabe H., Ishihama I., Katsuki H. Nucleic Acids Res. 13:59-71(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
[7]	"Site-directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli: the role of His579 in the catalytic and regulatory functions." Terada K., Murata T., Izui K. J. Biochem. 109:49-54(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-579.
[8]	"Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction." Terada K., Izui K. Eur. J. Biochem. 202:797-803(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-138.
[9]	"Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase." Yano M., Terada K., Umiji K., Izui K. J. Biochem. 117:1196-1200(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ARG-587.
[10]	"First crystallization of a phosphoenolpyruvate carboxylase from Escherichia coli." Inoue M., Hayashi M., Sugimoto M., Harada S., Kai Y., Kasai N., Terada K., Izui K. J. Mol. Biol. 208:509-510(1989) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION.
[11]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[12]	"Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition." Kai Y., Matsumura H., Inoue T., Terada K., Nagara Y., Yoshinaga T., Kihara A., Tsumura K., Izui K. Proc. Natl. Acad. Sci. U.S.A. 96:823-828(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05903 Genomic DNA. Translation: CAA29332.1.
X55417 Genomic DNA. No translation available.
U00006 Genomic DNA. Translation: AAC43062.1.
U00096 Genomic DNA. Translation: AAC76938.1.
AP009048 Genomic DNA. Translation: BAE77355.1.
X01700 Genomic DNA. Translation: CAA25847.1.

PIR

QYEC. A01083.

RefSeq

NP_418391.1. NC_000913.2.
YP_491496.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FIY	X-ray	2.80	A	1-883	[»]
1JQN	X-ray	2.35	A	1-883	[»]
1QB4	X-ray	2.60	A	1-883	[»]

ProteinModelPortal

P00864.

SMR

P00864. Positions 4-883.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10538N.

IntAct

P00864. 3 interactions.

STRING

511145.b3956.

Proteomic databases

PaxDb

P00864.

PRIDE

P00864.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76938; AAC76938; b3956.
BAE77355; BAE77355; BAE77355.

GeneID

12933655.
948457.

KEGG

ecj:Y75_p3232.
eco:b3956.

PATRIC

32123433. VBIEscCol129921_4077.

Organism-specific databases

EchoBASE

EB0749.

EcoGene

EG10756. ppc.

Phylogenomic databases

eggNOG

COG2352.

HOGENOM

HOG000238648.

K01595.

OMA

AIPWVFG.

ProtClustDB

PRK00009.

Enzyme and pathway databases

BioCyc

EcoCyc:PEPCARBOX-MONOMER.
ECOL316407:JW3928-MONOMER.
MetaCyc:PEPCARBOX-MONOMER.

Gene expression databases

Genevestigator

P00864.

Family and domain databases

HAMAP

MF_00595. PEPcase_type1.

InterPro

IPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]

Pfam

PF00311. PEPcase. 1 hit.
[Graphical view]

PRINTS

PR00150. PEPCARBXLASE.

SUPFAM

SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

PROSITE

PS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00864.

Entry information

Entry name

CAPP_ECOLI

Accession

Primary (citable) accession number: P00864
Secondary accession number(s): Q2M8Q1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents