Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P04711 (CAPP1_MAIZE)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Phosphoenolpyruvate carboxylase 1
      Short name=PEPCase 1
      Short name=PEPC 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 › PACCAD clade › Panicoideae › Andropogoneae › Zea

Hide | Top

Protein attributes

Sequence length970 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

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 + CO2.

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.

Hide | Top

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...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P04711-1 [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

« Hide

Hide | Top

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: 3005978] [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: 2731539] [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: 2628434] [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: 2894322] [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: 2268676] [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: 16668168] [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: 12467579] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Hide | Top

Cross-references

Sequence databases

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.
UniGeneZm.94270

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JQOX-ray3.00A/B1-970[»]
ModBaseSearch...

Genome annotation databases

GeneID542372.

Organism-specific databases

GrameneP04711.
MaizeGDB30066.

Enzyme and pathway databases

BRENDA4.1.1.31. 289.

Family and domain databases

InterProIPR001449. PEP_COase.
IPR018129. PEP_COase_AS.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PfamPF00311. PEPcase. 1 hit.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

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: June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents