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Q01647 (CAPP1_FLAPR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:PPCA1
OrganismFlaveria pringlei
Taxonomic identifier4226 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

Protein attributes

Sequence length967 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Through the carboxylation of phosphoenolpyruvate (PEP) it 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. HAMAP-Rule MF_00595

Enzyme regulation

By light-reversible phosphorylation. HAMAP-Rule MF_00595

Pathway

Photosynthesis; C3 acid pathway. HAMAP-Rule MF_00595

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00595.

Sequence similarities

Belongs to the PEPCase type 1 family.

Ontologies

Keywords
   Biological processCarbon dioxide fixation
Photosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionLyase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from electronic annotation. Source: UniProtKB-KW

photosynthesis

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphoenolpyruvate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 967967Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595
PRO_0000166664

Sites

Active site1721 By similarity
Active site6011 By similarity

Amino acid modifications

Modified residue111Phosphoserine By similarity

Experimental info

Sequence conflict291 – 2922KH → N in CAA88829. Ref.2

Secondary structure

........................................................................................................................ 967
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01647 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 8317EA8078C038C0

FASTA967110,629
        10         20         30         40         50         60 
MANRNLEKLA SIDAQLRLLV PGKVSEDDKL IEYDALLLDK FLDILQDLHG EDLKEAVQEC 

        70         80         90        100        110        120 
YELSAEYEGK HDPKKLEELG SVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRIK 

       130        140        150        160        170        180 
LKRGDFADEA NATTESDIEE TFKKLVLKLN KSPEEVFDAL KNQTVDLVLT AHPTQSVRRS 

       190        200        210        220        230        240 
LLQKHGRIRN CLAQLYAKDI TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM 

       250        260        270        280        290        300 
SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG KHPRVTPEVT 

       310        320        330        340        350        360 
RDVCLLARMM ASNMYFSQIE DLMFEMSMWR CNSELRVRAE ELYRTARRDV KHYIEFWKQV 

       370        380        390        400        410        420 
PPTEPYRVIL GDVRDKLYNT RERSRHLLAH GISDIPEEAV YTNVEQFLEP LELCYRSLCD 

       430        440        450        460        470        480 
CGDRVIADGS LLDFLRQVST FGLSLVKLDI RQESDRHTDV LDAITQHLEI GSYREWSEEK 

       490        500        510        520        530        540 
RQEWLLAELS GKRPLFGSDL PKTEEVKDVL DTFNVLAELP SDCFGAYIIS MATSPSDVLA 

       550        560        570        580        590        600 
VELLQRECHV KHPLRVVPLF EKLADLEAAP AAMARLFSID WYRNRIDGKQ EVMIGYSDSG 

       610        620        630        640        650        660 
KDAGRFSAAW QLYKAQEEII KVAKEFGVKL VIFHGRGGTV GRGGGPTHLA ILSQPPDTIH 

       670        680        690        700        710        720 
GSLRVTVQGE VIEQSFGEEH LCFRTLQRFC AATLEHGMNP PISPRPEWRE LMDQMAVVAT 

       730        740        750        760        770        780 
EEYRSIVFKE PRFVEYFRLA TPELEYGRMN IGSRPSKRKP SGGIESLRAI PWIFAWTQTR 

       790        800        810        820        830        840 
FHLPVWLGFG AAFKHAIKKD SKNLQMLQEM YKTWPFFRVT IDLVEMVFAK GDPGIAALND 

       850        860        870        880        890        900 
KLLVSEDLWP FGESLRANYE ETKDYLLKIA GHRDLLEGDP YLKQRIRLRD SYITTLNVCQ 

       910        920        930        940        950        960 
AYTLKRIRDP NYHVTLRPHI SKEYAAEPSK PADELIHLNP TSEYAPGLED TLILTMKGIA 


AGMQNTG 

« Hide

References

[1]"Homologous genes for the C4 isoform of phosphoenolpyruvate carboxylase in a C3 and a C4 Flaveria species."
Hermans J., Westhoff P.
Mol. Gen. Genet. 234:275-284(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Svensson P., Blaesing O.E., Westhoff P.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64144 Genomic DNA. Translation: CAA45505.1.
Z48966 mRNA. Translation: CAA88829.1.
PIRS25081.
S52853.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZGBX-ray2.71A/B6-967[»]
ProteinModelPortalQ01647.
SMRQ01647. Positions 31-967.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ01647.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00321.

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. 2 hits.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAPP1_FLAPR
AccessionPrimary (citable) accession number: Q01647
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: February 19, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways