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P51059 (CAPP2_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2

Short name=PEPC 2
Short name=PEPCase 2
EC=4.1.1.31
Gene names
Name:PEP4
Synonyms:PEP
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length967 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity. HAMAP-Rule MF_00595

Pathway

Photosynthesis; C3 acid pathway. HAMAP-Rule MF_00595

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00595

Subcellular location

Cytoplasm By similarity 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 termAllosteric enzyme
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to phosphate starvation

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

photosynthesis

Inferred from electronic annotation. Source: UniProtKB-KW

protein tetramerization

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapoplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cytosol

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   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 2 HAMAP-Rule MF_00595
PRO_0000166668

Sites

Active site1741 By similarity
Active site6021 By similarity

Amino acid modifications

Modified residue131Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P51059 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 7034A2AD5521645B

FASTA967109,999
        10         20         30         40         50         60 
MAALGPKMER LSSIDAQLRM LVPGKVSEDD KLIEYDALLL DRFLDILQDL HGDDLKEMVQ 

        70         80         90        100        110        120 
ECYEVAAEYE TKHDLQKLDE LGKMITSLDP GDSIVIAKSL SHMLNLANLA EEVQIAYRRR 

       130        140        150        160        170        180 
IKLKKGDFAD ENSAITESDI EETLKRLVVD LKKSPAEVFD ALKSQTVDLV LTAHPTQSVR 

       190        200        210        220        230        240 
RSLLQKHSRI RNCLVQLYSK DITPDDKQEL DEALQREIQA AFRTDEIRRT QPTPQDEMRA 

       250        260        270        280        290        300 
GMSYFHETIW KGVPKFLRRV DTALKNIGIN ERVPYNAPLI QFSSWMGGDR DGNPRVTPEV 

       310        320        330        340        350        360 
TRDVCLLARM MASNLYCSQI EDLMFELSMW RCSDELRMRA DVLHLSTKKD AKHYIEFWKK 

       370        380        390        400        410        420 
VPPNEPYRVI LSDVRDKLYN TRERSRELLS SGHSDIPEEA TLTNVEQLLE PLELCYRSLC 

       430        440        450        460        470        480 
ACGDSVIADG TLLDFLRQVS TFGLSLVRLD IRQESDRHTD VLDAITTYLG IGSYREWTEE 

       490        500        510        520        530        540 
RRQEWLLSEL NGKRPLFGSD LPKTEEISDV LDTFHVIAEL PSDNFGAYII SMATAPSDVL 

       550        560        570        580        590        600 
AVELLQRECH VKTPLRVVPL FEKLADLEAA PAALARLFSI DWYRQRINGK QEVMIGYSDS 

       610        620        630        640        650        660 
GKDAGRLSAA WQLYKAQEEL IKVAKDFGVK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI 

       670        680        690        700        710        720 
HGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMH PPNAPKPEWR ALLDEMAVVA 

       730        740        750        760        770        780 
TEEYRSIVFK EPRFVEYFRL ATPETEYGRM NIGSRPSKRK PSGGIDSLRA IPWIFAWTQT 

       790        800        810        820        830        840 
RFHLPVWLGF GAAFKNVLQK DIRNLHMLQE MYNEWPFFRV TIDLVEMVFA KGNPGIAALY 

       850        860        870        880        890        900 
DKLLVSEELH PLGEKLRANY EETQKLLLQV AGHRDLLEGD LYLKQRLRLR DAYITTLNVC 

       910        920        930        940        950        960 
QAYTLKRIRD PDYHVALRPH LSKEIMDSTK AAADVVKLNP GSEYAPGLED TLILTMKGIA 


AGLQNTG 

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References

[1]"Molecular evolution of phosphoenolpyruvate carboxylase for C4 photosynthesis in maize: comparison of its cDNA sequence with a newly isolated cDNA encoding an isozyme involved in the anaplerotic function."
Kawamura T., Shigesada K., Toh H., Okumura S., Yanagisawa S., Izui K.
J. Biochem. 112:147-154(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. H84.
Tissue: Root.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61489 mRNA. Translation: CAA43709.1.
PIRJH0667.
RefSeqNP_001105438.1. NM_001111968.1.
UniGeneZm.163236.

3D structure databases

ProteinModelPortalP51059.
SMRP51059. Positions 33-967.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP51059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542393.
KEGGzma:542393.

Organism-specific databases

GrameneP51059.
MaizeGDB30066.

Phylogenomic databases

HOGENOMHOG000238648.
KOK01595.

Enzyme and pathway databases

SABIO-RKP51059.
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 nameCAPP2_MAIZE
AccessionPrimary (citable) accession number: P51059
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 84 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

PATHWAY comments

Index of metabolic and biosynthesis pathways