Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

F4MBH3 (F4MBH3_ECOLX) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595

Short name=PEPC HAMAP-Rule MF_00595
Short name=PEPCase HAMAP-Rule MF_00595
EC=4.1.1.31 HAMAP-Rule MF_00595
Gene names
Name:ppc HAMAP-Rule MF_00595
ORF Names:UMNK88_4794 EMBL AEE59287.1
OrganismEscherichia coli UMNK88 [Complete proteome] EMBL AEE59287.1
Taxonomic identifier696406 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length883 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle By similarity. HAMAP-Rule MF_00595 SAAS SAAS022805

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595 SAAS SAAS021135

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00595 SAAS SAAS021135

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00595

Sequence similarities

Belongs to the PEPCase type 1 family. HAMAP-Rule MF_00595

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1381 By similarity HAMAP-Rule MF_00595
Active site5461 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
F4MBH3 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: C66E18268EB19EFD

FASTA88399,077
        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 
SVISCDLYRG 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

[1]"Genome structure of porcine enterotoxigenic Escherichia coli."
Johnson T.J., Shepard S.M., Isaacson R.E.
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: UMNK88 EMBL AEE59287.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002729 Genomic DNA. Translation: AEE59287.1.
RefSeqYP_006136450.1. NC_017641.1.

3D structure databases

ProteinModelPortalF4MBH3.
SMRF4MBH3. Positions 4-883.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEE59287; AEE59287; UMNK88_4794.
GeneID12688046.
KEGGeun:UMNK88_4794.
PATRIC48577388. VBIEscCol159162_4692.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01595.
OMAAIPWVFG.

Enzyme and pathway databases

BioCycECOL696406:GJE4-4743-MONOMER.

Family and domain databases

HAMAPMF_00595. PEPcase_type1.
InterProIPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF00311. PEPcase. 1 hit.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
SUPFAMSSF51621. SSF51621. 1 hit.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF4MBH3_ECOLX
AccessionPrimary (citable) accession number: F4MBH3
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: February 19, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)