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H0P9V2 (H0P9V2_9SYNC) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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 BAL32734.1
ORF Names:SYNPCCN_1817 EMBL BAL32734.1
OrganismSynechocystis sp. PCC 6803 substr. PCC-N [Complete proteome] EMBL BAL32734.1
Taxonomic identifier1080229 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length1034 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

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 site2031 By similarity HAMAP-Rule MF_00595
Active site6801 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
H0P9V2 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: 76DF6061BAB7235D

FASTA1,034118,940
        10         20         30         40         50         60 
MNLAVPAFGL STNWSGNGNG SNSEEESVLY QRLKMVEELW ERVLQSECGQ ELVDLLTELR 

        70         80         90        100        110        120 
LQGTHEAITS EISEEVIMGI TQRIEHLELN DAIRAARAFA LYFQLINIVE QHYEQNEQQR 

       130        140        150        160        170        180 
NRWEASQETN FYEQAGNEEE MVPPSRLGAS TEPLPVGIDQ NELQASVGTF HWLMRELKRL 

       190        200        210        220        230        240 
NVPPQHIQNL LDHLDIRLVI TAHPTEIVRH TIRRKQRRVD RILRKLDQLQ GSVTGRDWLN 

       250        260        270        280        290        300 
TWDAKTAIAQ LTEEIRFWWR TDELHQFKPT VLDEVDYSLH YFDEVLFDAV PELSKRLGQA 

       310        320        330        340        350        360 
IKETFPHLRA PRANFCYFGS WVGGDRDGNP SVTPEVTWQT ACYQRGLVLG KYLFSLGELV 

       370        380        390        400        410        420 
AILSPSLHWC KVSQELLDSL ERDRIQLPEI YEELSLRYRQ EPYRMKLAYV TKRLENTLRR 

       430        440        450        460        470        480 
NNRLANPEER QTMITMPAEN HYRTGEELLE ELRLIQRNLT ETGLTCLELE NLITQLEVYG 

       490        500        510        520        530        540 
FNLAQLDFRQ ESSRHAEAIA EIAEYMGVLT TPYEEMAEED KLAWLGVELQ TRRPLIPQEM 

       550        560        570        580        590        600 
PFSERTRETI ETLRTLRHLQ MEFGVDICQT YIISMTNDAS DVLEVLLLAK EAGLYDPATA 

       610        620        630        640        650        660 
SNSLRIVPLF ETVEDLKNAP GIMDSLFSLP FYRATLAGSY HSLKELQNQP PDYYQIPTTT 

       670        680        690        700        710        720 
ALLNPGNLQE IMVGYSDSNK DSGFLSSNWE IHKAQKSLQA VAQSHRVILR LFHGRGGSVG 

       730        740        750        760        770        780 
RGGGPAYKAI LAQPAGTVDG RIKITEQGEV LASKYSLPEL ALYNLETLTT AVIQASLLKS 

       790        800        810        820        830        840 
SFDFIEPWNR IMEELACTAR RAYRSLIYEE PDFLDFFLTV TPIPEISELQ ISSRPARRKG 

       850        860        870        880        890        900 
GKADLSSLRA IPWVFSWTQT RFLLPAWYGV GTALKSFVDQ DPVKNMKLLR YFYFKWPFFN 

       910        920        930        940        950        960 
MVISKVEMTL SKVDLTIASH YVQELSKPED RERFDRLFQQ IKQEYQLTRD FAMEITAHPH 

       970        980        990       1000       1010       1020 
LLDGDRSLQR SVLLRNRTIV PLGLLQISLL KRLRQVTQEA ETSGVRYRRY SKEELLRGAL 

      1030 
LTINGIAAGM RNTG 

« Hide

References

[1]"Identification of substrain-specific mutations by massively parallel whole-genome resequencing of Synechocystis sp. PCC 6803."
Kanesaki Y., Shiwa Y., Tajima N., Suzuki M., Watanabe S., Sato N., Ikeuchi M., Yoshikawa H.
DNA Res. 19:67-79(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012277 Genomic DNA. Translation: BAL32734.1.
RefSeqYP_005409456.1. NC_017052.1.

3D structure databases

ProteinModelPortalH0P9V2.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEH0P9V2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAL32734; BAL32734; SYNPCCN_1817.
GeneID12010583.
KEGGsys:SYNPCCN_1817.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01595.

Enzyme and pathway databases

BioCycSSP1080229:GLM2-1838-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. 3 hits.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH0P9V2_9SYNC
AccessionPrimary (citable) accession number: H0P9V2
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: June 11, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)