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F0N0U0 (F0N0U0_NEIMO) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 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 EMBL ADZ02418.1
Ordered Locus Names:NMBM04240196_2003 EMBL ADZ02418.1
OrganismNeisseria meningitidis serogroup B (strain M04-240196) [Complete proteome] [HAMAP] EMBL ADZ02418.1
Taxonomic identifier935593 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length900 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 SAAS021135

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595 SAAS SAAS018129

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00595 SAAS SAAS018129

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 site1401 By similarity HAMAP-Rule MF_00595
Active site5681 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
F0N0U0 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: FD2F13E9CB75E5F5

FASTA900100,995
        10         20         30         40         50         60 
MQLHILNNPK DAALAADAEF LKQSLFNLLH EEASPLVVET VKLLSTSDDS AALIEKVLPQ 

        70         80         90        100        110        120 
LDEQQTHDLT LACGLFAQIL NIAEDVHHER RRQIHEEAGR GGAEGSLTET VRRLKAGKAD 

       130        140        150        160        170        180 
GKSVQRQLDN TSVTAVLTAH PTEVQRQTVL SFNRRIRALL PQRERCTNAD ALARLRREID 

       190        200        210        220        230        240 
TILLGLWQTS ETRRHKLSVN DEINNGVSIF PMSFFEALPK LYRNMEHDFQ MVYPGVRVPD 

       250        260        270        280        290        300 
ILKIGGWIGG DRDGNPFVSA ETLRFAFRRH ADAVFRFYRG ELDKLYRELP LSIRRVKVNG 

       310        320        330        340        350        360 
DVTALSDKSP DEEIARAEEP YRRAIAYIMA RAMGKARALG LGMGCKFGFL EPYASAQEFL 

       370        380        390        400        410        420 
DDLKKLQRSL IDNGSRLLAE GRLADLIRSV SVFGFHMMPL DLRQHAGKHA DVVAELFQHA 

       430        440        450        460        470        480 
GLEDYNSLNE EQKQAALLRE LGHQRPLYSP FITYSDHTRH ELAIFNEARK IKDEFGEDAV 

       490        500        510        520        530        540 
TQSIISNCEQ PSDLLALALL LKETGLLVVE NGKPHSRINI VPLFETIEAL ENACPVMETM 

       550        560        570        580        590        600 
FRLDWYDALL ESRGNIQEIM LGYSDSNKDG GYVTSSWCLY QAELGLVELF KKYGVRMRLF 

       610        620        630        640        650        660 
HGRGGSVGRG GGPSYQAILA QPAGSVAGQI RITEQGEVIT AKYADPGNAQ RNLETLVAAT 

       670        680        690        700        710        720 
LEASILPDKK DPDAKLMQAL SDVSFKYYRE LITHPDFIDY FLQTSPIQEI ATLNLGSRPA 

       730        740        750        760        770        780 
SRKTLARIQD LRAIPWVFSW MQNRLMLPAW YGFGSAVETL CEGSPETLAA LREHAQSNPF 

       790        800        810        820        830        840 
FQAMLSNMEQ VMAKTDITLA ENYAGLSESP DKAKIIFGMI KEEYRRSRKA LLDLLQTEEL 

       850        860        870        880        890        900 
LRDNRSLARS LALRIPYLNA LNGLQVAMLK RLRKEPDNPH ALLMVHLTIN GVAQGLRNTG 

« Hide

References

[1]"Neisseria meningitidis is structured in clades associated with restriction modification systems that modulate homologous recombination."
Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.
Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M04-240196 EMBL ADZ02418.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002423 Genomic DNA. Translation: ADZ02418.1.
RefSeqYP_005898657.1. NC_017515.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ02418; ADZ02418; NMBM04240196_2003.
GeneID12489072.
KEGGnmq:NMBM04240196_2003.
PATRIC47171677. VBINeiMen179694_2673.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01595.

Enzyme and pathway databases

BioCycNMEN935593:GLHT-2002-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 nameF0N0U0_NEIMO
AccessionPrimary (citable) accession number: F0N0U0
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: June 11, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)