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

Q9RNU9 (CAPP_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate carboxylase

Short name=PEPC
Short name=PEPCase
EC=4.1.1.31
Gene names
Name:ppc
Ordered Locus Names:SCO3127
ORF Names:SCE66.06c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00595

Sequence similarities

Belongs to the PEPCase type 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 911911Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595
PRO_0000166628

Sites

Active site1371 By similarity
Active site5691 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RNU9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5192E0BB96881273

FASTA911101,297
        10         20         30         40         50         60 
MSSADDQTTT TTSSELRADI RRLGDLLGET LVRQEGPELL ELVEKVRRLT REDGEAAAEL 

        70         80         90        100        110        120 
LRGTELETAA KLVRAFSTYF HLANVTEQVH RGRELGAKRA AEGGLLARTA DRLKDADPEH 

       130        140        150        160        170        180 
LRETVRNLNV RPVFTAHPTE AARRSVLNKL RRIAALLDTP VNESDRRRLD TRLAENIDLV 

       190        200        210        220        230        240 
WQTDELRVVR PEPADEARNA IYYLDELHLG AVGDVLEDLT AELERAGVKL PDDTRPLTFG 

       250        260        270        280        290        300 
TWIGGDRDGN PNVTPQVTWD VLILQHEHGI NDALEMIDEL RGFLSNSIRY AGATEELLAS 

       310        320        330        340        350        360 
LQADLERLPE ISPRYKRLNA EEPYRLKATC IRQKLENTKQ RLAKGTPHED GRDYLGTAQL 

       370        380        390        400        410        420 
IDDLRIVQTS LREHRGGLFA DGRLARTIRT LAAFGLQLAT MDVREHADAH HHALGQLFDR 

       430        440        450        460        470        480 
LGEESWRYAD MPREYRTKLL AKELRSRRPL APSPAPVDAP GEKTLGVFQT VRRALEVFGP 

       490        500        510        520        530        540 
EVIESYIISM CQGADDVFAA AVLAREAGLI DLHAGWAKIG IVPLLETTDE LKAADTILED 

       550        560        570        580        590        600 
LLADPSYRRL VALRGDVQEV MLGYSDSSKF GGITTSQWEI HRAQRRLRDV AHRYGVRLRL 

       610        620        630        640        650        660 
FHGRGGTVGR GGGPTHDAIL AQPWGTLEGE IKVTEQGEVI SDKYLIPALA RENLELTVAA 

       670        680        690        700        710        720 
TLQASALHTA PRQSDEALAR WDAAMDVVSD AAHTAYRHLV EDPDLPTYFL ASTPVDQLAD 

       730        740        750        760        770        780 
LHLGSRPSRR PGSGVSLDGL RAIPWVFGWT QSRQIVPGWY GVGSGLKALR EAGLDTVLDE 

       790        800        810        820        830        840 
MHQQWHFFRN FISNVEMTLA KTDLRIAQHY VDTLVPDELK HVFDTIKAEH ELTVAEVLRV 

       850        860        870        880        890        900 
TGESELLDAD PVLKQTFTIR DAYLDPISYL QVALLGRQRE AAAANEDPDP LLARALLLTV 

       910 
NGVAAGLRNT G 

« Hide

References

« Hide 'large scale' references
[1]"Phosphoenolpyruvate carboxylase from Streptomyces coelicolor A3(2): purification of the enzyme, cloning of the ppc gene and over-expression of the protein in a streptomycete."
Bramwell H., Nimmo H.G., Hunter I.S., Coggins J.R.
Biochem. J. 293:131-136(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: A3(2) / NRRL B-16638.
[2]"The ppc gene of Streptomyces coelicolor A3(2)."
Ricketts A.D.J., Hunter I.S.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3(2) / NRRL B-16638.
[3]"Characterization of the phosphoenolpyruvate carboxylase gene from Streptomyces coelicolor A3(2) and a ppc gene disruption mutant."
Alves A.M.C.R., te Poele E., White J., Bibb M.J., Dijkhuizen L.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3(2) / NRRL B-16638.
[4]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF177946 Genomic DNA. Translation: AAD53311.1.
AF160253 Genomic DNA. Translation: AAM54458.1.
AL939115 Genomic DNA. Translation: CAB95920.1.
RefSeqNP_627344.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9RNU9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO3127.

Proteomic databases

PRIDEQ9RNU9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB95920; CAB95920; CAB95920.
GeneID1098561.
KEGGsco:SCO3127.
PATRIC23736002. VBIStrCoe124346_3191.

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238647.
KOK01595.
OMAAIPWVFG.
OrthoDBEOG6TJ7T8.
PhylomeDBQ9RNU9.
ProtClustDBCLSK902480.

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 nameCAPP_STRCO
AccessionPrimary (citable) accession number: Q9RNU9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families