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P04711 (CAPP1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 1
Short name=PEPC 1
Short name=PEPCase 1
EC=4.1.1.31
Gene names
Name:PEP1
Synonyms:PPC
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length970 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.

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.

Cofactor

Magnesium By similarity.

Enzyme regulation

By light-reversible phosphorylation.

Pathway

Photosynthesis; C4 acid pathway.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the PEPCase type 1 family.

Sequence caution

The sequence CAA32722.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbon dioxide fixation
Photosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionLyase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Direct protein sequencing
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 970970Phosphoenolpyruvate carboxylase 1
PRO_0000166667

Sites

Active site1771 Ref.6
Active site6061 Ref.6
Active site6471 Ref.6

Amino acid modifications

Modified residue151Phosphoserine Ref.7

Experimental info

Sequence conflict2391A → D Ref.2
Sequence conflict2391A → D Ref.3
Sequence conflict338 – 3392EL → DV in CAA27270. Ref.2
Sequence conflict4821P → S Ref.2
Sequence conflict4821P → S Ref.3
Sequence conflict5091D → E in CAA33663. Ref.3
Sequence conflict557 – 5593QPL → PAV Ref.2
Sequence conflict557 – 5593QPL → PAV Ref.3
Sequence conflict5701D → S Ref.2
Sequence conflict5701D → S Ref.3
Sequence conflict573 – 5742SA → LR in CAA27270. Ref.2
Sequence conflict6871C → S in CAA27270. Ref.2
Sequence conflict7361A → P in CAA27270. Ref.2
Sequence conflict9631A → R in CAA27270. Ref.2

Secondary structure

1 .......................................................................................................... 970
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04711 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 95B66F96ABCE22F4

FASTA970109,297
        10         20         30         40         50         60 
MASTKAPGPG EKHHSIDAQL RQLVPGKVSE DDKLIEYDAL LVDRFLNILQ DLHGPSLREF 

        70         80         90        100        110        120 
VQECYEVSAD YEGKGDTTKL GELGAKLTGL APADAILVAS SILHMLNLAN LAEEVQIAHR 

       130        140        150        160        170        180 
RRNSKLKKGG FADEGSATTE SDIEETLKRL VSEVGKSPEE VFEALKNQTV DLVFTAHPTQ 

       190        200        210        220        230        240 
SARRSLLQKN ARIRNCLTQL NAKDITDDDK QELDEALQRE IQAAFRTDEI RRAQPTPQAE 

       250        260        270        280        290        300 
MRYGMSYIHE TVWKGVPKFL RRVDTALKNI GINERLPYNV SLIRFSSWMG GDRDGNPRVT 

       310        320        330        340        350        360 
PEVTRDVCLL ARMMAANLYI DQIEELMFEL SMWRCNDELR VRAEELHSSS GSKVTKYYIE 

       370        380        390        400        410        420 
FWKQIPPNEP YRVILGHVRD KLYNTRERAR HLLASGVSEI SAESSFTSIE EFLEPLELCY 

       430        440        450        460        470        480 
KSLCDCGDKA IADGSLLDLL RQVFTFGLSL VKLDIRQESE RHTDVIDAIT THLGIGSYRE 

       490        500        510        520        530        540 
WPEDKRQEWL LSELRGKRPL LPPDLPQTDE IADVIGAFHV LAELPPDSFG PYIISMATAP 

       550        560        570        580        590        600 
SDVLAVELLQ RECGVRQPLP VVPLFERLAD LQSAPASVER LFSVDWYMDR IKGKQQVMVG 

       610        620        630        640        650        660 
YSDSGKDAGR LSAAWQLYRA QEEMAQVAKR YGVKLTLFHG RGGTVGRGGG PTHLAILSQP 

       670        680        690        700        710        720 
PDTINGSIRV TVQGEVIEFC FGEEHLCFQT LQRFTAATLE HGMHPPVSPK PEWRKLMDEM 

       730        740        750        760        770        780 
AVVATEEYRS VVVKEARFVE YFRSATPETE YGRMNIGSRP AKRRPGGGIT TLRAIPWIFS 

       790        800        810        820        830        840 
WTQTRFHLPV WLGVGAAFKF AIDKDVRNFQ VLKEMYNEWP FFRVTLDLLE MVFAKGDPGI 

       850        860        870        880        890        900 
AGLYDELLVA EELKPFGKQL RDKYVETQQL LLQIAGHKDI LEGDPFLKQG LVLRNPYITT 

       910        920        930        940        950        960 
LNVFQAYTLK RIRDPNFKVT PQPPLSKEFA DENKPAGLVK LNPASEYPPG LEDTLILTMK 

       970 
GIAAGMQNTG

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References

[1]"Structure and expression of the maize gene encoding the phosphoenolpyruvate carboxylase isozyme involved in C4 photosynthesis."
Hudspeth R.L., Grula J.W.
Plant Mol. Biol. 12:579-589(1989)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. B73.
Tissue: Leaf.
[2]"Cloning and sequence analysis of cDNA encoding active phosphoenolpyruvate carboxylase of the C4-pathway from maize."
Izui K., Ishijima S., Yamaguchi Y., Katagiri F., Murata T., Shigesada K., Sugiyama T., Katsuki H.
Nucleic Acids Res. 14:1615-1628(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 39-970.
[3]"Complete structure of the gene for phosphoenolpyruvate carboxylase from maize."
Matsuoka M., Minami E.
Eur. J. Biochem. 181:593-598(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Golden cross Bantam.
[4]"Maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis: nucleotide sequence analysis of the 5' flanking region of the gene."
Yanagisawa S., Izui K.
J. Biochem. 106:982-987(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
Strain: cv. H84.
Tissue: Leaf.
[5]"Further analysis of cDNA clones for maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis. Nucleotide sequence of entire open reading frame and evidence for polyadenylation of mRNA at multiple sites in vivo."
Yanagisawa S., Izui K., Yamaguchi Y., Shigesada K., Katsuki H.
FEBS Lett. 229:107-110(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-82.
[6]"Isolation and sequence of an active-site peptide from maize leaf phosphoenolpyruvate carboxylase inactivated by pyridoxal 5'-phosphate."
Jiao J.-A., Podesta F.E., Chollet R., O'Leary M.H., Andreo C.S.
Biochim. Biophys. Acta 1041:291-295(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, PROTEIN SEQUENCE OF 599-610.
[7]"In vivo regulatory phosphorylation site in C4-leaf phosphoenolpyruvate carboxylase from maize and sorghum."
Jiao J.-A., Vidal J., Echevarria C., Chollet R.
Plant Physiol. 96:297-301(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-15.
[8]"Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases."
Matsumura H., Xie Y., Shirakata S., Inoue T., Yoshinaga T., Ueno Y., Izui K., Kai Y.
Structure 10:1721-1730(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X15238 mRNA. Translation: CAA33316.1.
X03613 mRNA. Translation: CAA27270.1.
X14581 Genomic DNA. Translation: CAA32724.1.
X14579 Genomic DNA. Translation: CAA32722.1. Different initiation.
X14580 Genomic DNA. Translation: CAA32723.1.
X15642 Genomic DNA. Translation: CAA33663.1.
X07168 mRNA. Translation: CAA30158.1.
RefSeqNP_001105418.1. NM_001111948.1.
UniGeneZm.2433.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQOX-ray3.00A/B1-970[»]
ProteinModelPortalP04711.
SMRP04711. Positions 35-970.
ModBaseSearch...

Proteomic databases

PRIDEP04711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542372.
KEGGzma:542372.

Organism-specific databases

GrameneP04711.
MaizeGDB30066.

Phylogenomic databases

HOGENOMHOG000238648.
KOK01595.

Enzyme and pathway databases

UniPathwayUPA00322.

Family and domain databases

InterProIPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
PfamPF00311. PEPcase. 1 hit.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04711.

Entry information

Entry nameCAPP1_MAIZE
AccessionPrimary (citable) accession number: P04711
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1989
Last modified: May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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