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P04711

- CAPP1_MAIZE

UniProt

P04711 - CAPP1_MAIZE

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Protein

Phosphoenolpyruvate carboxylase 1

Gene

PEP1

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.

Catalytic activityi

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.

Cofactori

Mg2+By similarity

Enzyme regulationi

By light-reversible phosphorylation.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei177 – 17711 Publication
Active sitei606 – 60611 Publication
Active sitei647 – 64711 Publication

GO - Molecular functioni

  1. phosphoenolpyruvate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbon fixation Source: UniProtKB-KW
  2. photosynthesis Source: UniProtKB-KW
  3. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbon dioxide fixation, Photosynthesis

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

SABIO-RKP04711.
UniPathwayiUPA00322.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxylase 1 (EC:4.1.1.31)
Short name:
PEPC 1
Short name:
PEPCase 1
Gene namesi
Name:PEP1
Synonyms:PPC
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiP04711.
MaizeGDBi30066.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 970970Phosphoenolpyruvate carboxylase 1PRO_0000166667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP04711.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
970
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 5318Combined sources
Helixi55 – 7218Combined sources
Helixi78 – 8912Combined sources
Helixi92 – 12231Combined sources
Helixi143 – 1519Combined sources
Helixi158 – 1669Combined sources
Beta strandi169 – 1757Combined sources
Helixi184 – 19916Combined sources
Helixi207 – 22620Combined sources
Helixi237 – 24812Combined sources
Turni249 – 2557Combined sources
Helixi256 – 26813Combined sources
Turni269 – 2713Combined sources
Beta strandi282 – 2876Combined sources
Turni289 – 2913Combined sources
Helixi301 – 32929Combined sources
Helixi337 – 35014Combined sources
Beta strandi359 – 3613Combined sources
Helixi370 – 39425Combined sources
Helixi409 – 42517Combined sources
Turni430 – 4345Combined sources
Helixi435 – 44612Combined sources
Beta strandi449 – 4568Combined sources
Helixi459 – 47315Combined sources
Helixi483 – 49513Combined sources
Helixi509 – 52315Combined sources
Beta strandi529 – 5346Combined sources
Helixi541 – 55212Combined sources
Beta strandi561 – 5655Combined sources
Helixi568 – 5725Combined sources
Helixi574 – 5829Combined sources
Helixi585 – 5917Combined sources
Beta strandi593 – 6019Combined sources
Helixi604 – 6074Combined sources
Helixi610 – 62920Combined sources
Turni630 – 6323Combined sources
Beta strandi634 – 6407Combined sources
Helixi645 – 6473Combined sources
Helixi652 – 6576Combined sources
Beta strandi667 – 6737Combined sources
Helixi674 – 6818Combined sources
Helixi684 – 70320Combined sources
Helixi711 – 73222Combined sources
Helixi738 – 7458Combined sources
Helixi749 – 7546Combined sources
Helixi775 – 7839Combined sources
Helixi788 – 7914Combined sources
Helixi794 – 80411Combined sources
Helixi808 – 81811Combined sources
Helixi820 – 83314Combined sources
Helixi838 – 84710Combined sources
Helixi854 – 87522Combined sources
Helixi885 – 91329Combined sources
Turni937 – 9415Combined sources
Beta strandi942 – 9443Combined sources
Helixi951 – 96616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQOX-ray3.00A/B1-970[»]
ProteinModelPortaliP04711.
SMRiP04711. Positions 35-970.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04711.

Family & Domainsi

Sequence similaritiesi

Belongs to the PEPCase type 1 family.Curated

Phylogenomic databases

HOGENOMiHOG000238648.
KOiK01595.

Family and domain databases

HAMAPiMF_00595. PEPcase_type1.
InterProiIPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF00311. PEPcase. 1 hit.
[Graphical view]
PRINTSiPR00150. PEPCARBXLASE.
SUPFAMiSSF51621. SSF51621. 1 hit.
PROSITEiPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04711-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASTKAPGPG EKHHSIDAQL RQLVPGKVSE DDKLIEYDAL LVDRFLNILQ
60 70 80 90 100
DLHGPSLREF VQECYEVSAD YEGKGDTTKL GELGAKLTGL APADAILVAS
110 120 130 140 150
SILHMLNLAN LAEEVQIAHR RRNSKLKKGG FADEGSATTE SDIEETLKRL
160 170 180 190 200
VSEVGKSPEE VFEALKNQTV DLVFTAHPTQ SARRSLLQKN ARIRNCLTQL
210 220 230 240 250
NAKDITDDDK QELDEALQRE IQAAFRTDEI RRAQPTPQAE MRYGMSYIHE
260 270 280 290 300
TVWKGVPKFL RRVDTALKNI GINERLPYNV SLIRFSSWMG GDRDGNPRVT
310 320 330 340 350
PEVTRDVCLL ARMMAANLYI DQIEELMFEL SMWRCNDELR VRAEELHSSS
360 370 380 390 400
GSKVTKYYIE FWKQIPPNEP YRVILGHVRD KLYNTRERAR HLLASGVSEI
410 420 430 440 450
SAESSFTSIE EFLEPLELCY KSLCDCGDKA IADGSLLDLL RQVFTFGLSL
460 470 480 490 500
VKLDIRQESE RHTDVIDAIT THLGIGSYRE WPEDKRQEWL LSELRGKRPL
510 520 530 540 550
LPPDLPQTDE IADVIGAFHV LAELPPDSFG PYIISMATAP SDVLAVELLQ
560 570 580 590 600
RECGVRQPLP VVPLFERLAD LQSAPASVER LFSVDWYMDR IKGKQQVMVG
610 620 630 640 650
YSDSGKDAGR LSAAWQLYRA QEEMAQVAKR YGVKLTLFHG RGGTVGRGGG
660 670 680 690 700
PTHLAILSQP PDTINGSIRV TVQGEVIEFC FGEEHLCFQT LQRFTAATLE
710 720 730 740 750
HGMHPPVSPK PEWRKLMDEM AVVATEEYRS VVVKEARFVE YFRSATPETE
760 770 780 790 800
YGRMNIGSRP AKRRPGGGIT TLRAIPWIFS WTQTRFHLPV WLGVGAAFKF
810 820 830 840 850
AIDKDVRNFQ VLKEMYNEWP FFRVTLDLLE MVFAKGDPGI AGLYDELLVA
860 870 880 890 900
EELKPFGKQL RDKYVETQQL LLQIAGHKDI LEGDPFLKQG LVLRNPYITT
910 920 930 940 950
LNVFQAYTLK RIRDPNFKVT PQPPLSKEFA DENKPAGLVK LNPASEYPPG
960 970
LEDTLILTMK GIAAGMQNTG
Length:970
Mass (Da):109,297
Last modified:October 1, 1989 - v2
Checksum:i95B66F96ABCE22F4
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391A → D(PubMed:3005978)Curated
Sequence conflicti239 – 2391A → D(PubMed:2731539)Curated
Sequence conflicti338 – 3392EL → DV in CAA27270. (PubMed:3005978)Curated
Sequence conflicti482 – 4821P → S(PubMed:3005978)Curated
Sequence conflicti482 – 4821P → S(PubMed:2731539)Curated
Sequence conflicti509 – 5091D → E in CAA33663. (PubMed:2731539)Curated
Sequence conflicti557 – 5593QPL → PAV(PubMed:3005978)Curated
Sequence conflicti557 – 5593QPL → PAV(PubMed:2731539)Curated
Sequence conflicti570 – 5701D → S(PubMed:3005978)Curated
Sequence conflicti570 – 5701D → S(PubMed:2731539)Curated
Sequence conflicti573 – 5742SA → LR in CAA27270. (PubMed:3005978)Curated
Sequence conflicti687 – 6871C → S in CAA27270. (PubMed:3005978)Curated
Sequence conflicti736 – 7361A → P in CAA27270. (PubMed:3005978)Curated
Sequence conflicti963 – 9631A → R in CAA27270. (PubMed:3005978)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001105418.1. NM_001111948.1.
UniGeneiZm.2433.

Genome annotation databases

GeneIDi542372.
KEGGizma:542372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
RefSeqi NP_001105418.1. NM_001111948.1.
UniGenei Zm.2433.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JQO X-ray 3.00 A/B 1-970 [» ]
ProteinModelPortali P04711.
SMRi P04711. Positions 35-970.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P04711.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 542372.
KEGGi zma:542372.

Organism-specific databases

Gramenei P04711.
MaizeGDBi 30066.

Phylogenomic databases

HOGENOMi HOG000238648.
KOi K01595.

Enzyme and pathway databases

UniPathwayi UPA00322 .
SABIO-RK P04711.

Miscellaneous databases

EvolutionaryTracei P04711.

Family and domain databases

HAMAPi MF_00595. PEPcase_type1.
InterProi IPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
Pfami PF00311. PEPcase. 1 hit.
[Graphical view ]
PRINTSi PR00150. PEPCARBXLASE.
SUPFAMi SSF51621. SSF51621. 1 hit.
PROSITEi PS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiCAPP1_MAIZE
AccessioniPrimary (citable) accession number: P04711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1989
Last modified: November 26, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3