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Protein

Phosphoenolpyruvate carboxylase 2

Gene

PEP4

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei174 – 1741By similarity
Active sitei602 – 6021By similarity

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-RKP51059.
UniPathwayiUPA00321.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxylase 2 (EC:4.1.1.31)
Short name:
PEPC 2
Short name:
PEPCase 2
Gene namesi
Name:PEP4
Synonyms:PEP
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305 Componenti: Unplaced

Organism-specific databases

GrameneiP51059.
MaizeGDBi30066.

Subcellular locationi

  1. Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 967967Phosphoenolpyruvate carboxylase 2PRO_0000166668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP51059.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP51059.
SMRiP51059. Positions 33-967.
ModBaseiSearch...
MobiDBiSearch...

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. 2 hits.
PROSITEiPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51059-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALGPKMER LSSIDAQLRM LVPGKVSEDD KLIEYDALLL DRFLDILQDL
60 70 80 90 100
HGDDLKEMVQ ECYEVAAEYE TKHDLQKLDE LGKMITSLDP GDSIVIAKSL
110 120 130 140 150
SHMLNLANLA EEVQIAYRRR IKLKKGDFAD ENSAITESDI EETLKRLVVD
160 170 180 190 200
LKKSPAEVFD ALKSQTVDLV LTAHPTQSVR RSLLQKHSRI RNCLVQLYSK
210 220 230 240 250
DITPDDKQEL DEALQREIQA AFRTDEIRRT QPTPQDEMRA GMSYFHETIW
260 270 280 290 300
KGVPKFLRRV DTALKNIGIN ERVPYNAPLI QFSSWMGGDR DGNPRVTPEV
310 320 330 340 350
TRDVCLLARM MASNLYCSQI EDLMFELSMW RCSDELRMRA DVLHLSTKKD
360 370 380 390 400
AKHYIEFWKK VPPNEPYRVI LSDVRDKLYN TRERSRELLS SGHSDIPEEA
410 420 430 440 450
TLTNVEQLLE PLELCYRSLC ACGDSVIADG TLLDFLRQVS TFGLSLVRLD
460 470 480 490 500
IRQESDRHTD VLDAITTYLG IGSYREWTEE RRQEWLLSEL NGKRPLFGSD
510 520 530 540 550
LPKTEEISDV LDTFHVIAEL PSDNFGAYII SMATAPSDVL AVELLQRECH
560 570 580 590 600
VKTPLRVVPL FEKLADLEAA PAALARLFSI DWYRQRINGK QEVMIGYSDS
610 620 630 640 650
GKDAGRLSAA WQLYKAQEEL IKVAKDFGVK LTMFHGRGGT VGRGGGPTHL
660 670 680 690 700
AILSQPPDTI HGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMH
710 720 730 740 750
PPNAPKPEWR ALLDEMAVVA TEEYRSIVFK EPRFVEYFRL ATPETEYGRM
760 770 780 790 800
NIGSRPSKRK PSGGIDSLRA IPWIFAWTQT RFHLPVWLGF GAAFKNVLQK
810 820 830 840 850
DIRNLHMLQE MYNEWPFFRV TIDLVEMVFA KGNPGIAALY DKLLVSEELH
860 870 880 890 900
PLGEKLRANY EETQKLLLQV AGHRDLLEGD LYLKQRLRLR DAYITTLNVC
910 920 930 940 950
QAYTLKRIRD PDYHVALRPH LSKEIMDSTK AAADVVKLNP GSEYAPGLED
960
TLILTMKGIA AGLQNTG
Length:967
Mass (Da):109,999
Last modified:October 1, 1996 - v1
Checksum:i7034A2AD5521645B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61489 mRNA. Translation: CAA43709.1.
PIRiJH0667.
RefSeqiNP_001105438.1. NM_001111968.1.
UniGeneiZm.163236.

Genome annotation databases

GeneIDi542393.
KEGGizma:542393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61489 mRNA. Translation: CAA43709.1.
PIRiJH0667.
RefSeqiNP_001105438.1. NM_001111968.1.
UniGeneiZm.163236.

3D structure databases

ProteinModelPortaliP51059.
SMRiP51059. Positions 33-967.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP51059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi542393.
KEGGizma:542393.

Organism-specific databases

GrameneiP51059.
MaizeGDBi30066.

Phylogenomic databases

HOGENOMiHOG000238648.
KOiK01595.

Enzyme and pathway databases

UniPathwayiUPA00321.
SABIO-RKP51059.

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. 2 hits.
PROSITEiPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCAPP2_MAIZE
AccessioniPrimary (citable) accession number: P51059
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.