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Protein

Phosphoenolpyruvate carboxylase

Gene

PPCA1

Organism
Flaveria pringlei
Status
Reviewed-Annotation score: Annotation score: 4 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: C3 acid pathway

This protein is involved in the pathway C3 acid pathway, which is part of Photosynthesis.
View all proteins of this organism that are known to be involved in the pathway C3 acid pathway and in Photosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei172By similarity1
Active sitei601By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbon dioxide fixation, Photosynthesis

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BRENDAi4.1.1.31. 2269.
UniPathwayiUPA00321.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxylase (EC:4.1.1.31)
Short name:
PEPC
Short name:
PEPCase
Gene namesi
Name:PPCA1
OrganismiFlaveria pringlei
Taxonomic identifieri4226 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001666641 – 967Phosphoenolpyruvate carboxylaseAdd BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ01647.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1967
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 19Combined sources11
Helixi30 – 49Combined sources20
Helixi51 – 70Combined sources20
Helixi74 – 83Combined sources10
Helixi88 – 115Combined sources28
Helixi126 – 130Combined sources5
Turni132 – 134Combined sources3
Helixi138 – 148Combined sources11
Helixi153 – 161Combined sources9
Beta strandi164 – 169Combined sources6
Helixi179 – 195Combined sources17
Helixi202 – 220Combined sources19
Helixi232 – 239Combined sources8
Helixi242 – 245Combined sources4
Helixi247 – 264Combined sources18
Beta strandi278 – 282Combined sources5
Turni284 – 286Combined sources3
Helixi297 – 325Combined sources29
Helixi333 – 344Combined sources12
Helixi365 – 390Combined sources26
Helixi397 – 399Combined sources3
Helixi404 – 420Combined sources17
Helixi424 – 427Combined sources4
Helixi430 – 441Combined sources12
Beta strandi444 – 453Combined sources10
Helixi454 – 467Combined sources14
Turni473 – 475Combined sources3
Helixi478 – 489Combined sources12
Helixi504 – 518Combined sources15
Helixi521 – 523Combined sources3
Beta strandi524 – 530Combined sources7
Helixi535 – 547Combined sources13
Beta strandi555 – 560Combined sources6
Helixi563 – 577Combined sources15
Helixi580 – 586Combined sources7
Beta strandi589 – 594Combined sources6
Helixi596 – 603Combined sources8
Helixi605 – 626Combined sources22
Beta strandi629 – 634Combined sources6
Helixi639 – 641Combined sources3
Helixi645 – 652Combined sources8
Beta strandi662 – 667Combined sources6
Turni669 – 671Combined sources3
Helixi672 – 676Combined sources5
Helixi679 – 698Combined sources20
Helixi706 – 727Combined sources22
Helixi733 – 740Combined sources8
Helixi743 – 748Combined sources6
Beta strandi751 – 753Combined sources3
Turni764 – 766Combined sources3
Helixi769 – 777Combined sources9
Turni778 – 780Combined sources3
Helixi783 – 786Combined sources4
Helixi789 – 799Combined sources11
Helixi802 – 813Combined sources12
Helixi815 – 829Combined sources15
Helixi833 – 843Combined sources11
Helixi846 – 848Combined sources3
Helixi849 – 870Combined sources22
Turni875 – 878Combined sources4
Helixi880 – 908Combined sources29
Helixi948 – 963Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZGBX-ray2.71A/B6-967[»]
ProteinModelPortaliQ01647.
SMRiQ01647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PEPCase type 1 family.Curated

Family and domain databases

HAMAPiMF_00595. PEPcase_type1. 1 hit.
InterProiIPR021135. PEP_COase.
IPR022805. PEP_COase_bac/pln-type.
IPR018129. PEP_COase_Lys_AS.
IPR033129. PEPCASE_His_AS.
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.

Q01647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANRNLEKLA SIDAQLRLLV PGKVSEDDKL IEYDALLLDK FLDILQDLHG
60 70 80 90 100
EDLKEAVQEC YELSAEYEGK HDPKKLEELG SVLTSLDPGD SIVIAKAFSH
110 120 130 140 150
MLNLANLAEE VQIAYRRRIK LKRGDFADEA NATTESDIEE TFKKLVLKLN
160 170 180 190 200
KSPEEVFDAL KNQTVDLVLT AHPTQSVRRS LLQKHGRIRN CLAQLYAKDI
210 220 230 240 250
TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM SYFHETIWKG
260 270 280 290 300
VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG KHPRVTPEVT
310 320 330 340 350
RDVCLLARMM ASNMYFSQIE DLMFEMSMWR CNSELRVRAE ELYRTARRDV
360 370 380 390 400
KHYIEFWKQV PPTEPYRVIL GDVRDKLYNT RERSRHLLAH GISDIPEEAV
410 420 430 440 450
YTNVEQFLEP LELCYRSLCD CGDRVIADGS LLDFLRQVST FGLSLVKLDI
460 470 480 490 500
RQESDRHTDV LDAITQHLEI GSYREWSEEK RQEWLLAELS GKRPLFGSDL
510 520 530 540 550
PKTEEVKDVL DTFNVLAELP SDCFGAYIIS MATSPSDVLA VELLQRECHV
560 570 580 590 600
KHPLRVVPLF EKLADLEAAP AAMARLFSID WYRNRIDGKQ EVMIGYSDSG
610 620 630 640 650
KDAGRFSAAW QLYKAQEEII KVAKEFGVKL VIFHGRGGTV GRGGGPTHLA
660 670 680 690 700
ILSQPPDTIH GSLRVTVQGE VIEQSFGEEH LCFRTLQRFC AATLEHGMNP
710 720 730 740 750
PISPRPEWRE LMDQMAVVAT EEYRSIVFKE PRFVEYFRLA TPELEYGRMN
760 770 780 790 800
IGSRPSKRKP SGGIESLRAI PWIFAWTQTR FHLPVWLGFG AAFKHAIKKD
810 820 830 840 850
SKNLQMLQEM YKTWPFFRVT IDLVEMVFAK GDPGIAALND KLLVSEDLWP
860 870 880 890 900
FGESLRANYE ETKDYLLKIA GHRDLLEGDP YLKQRIRLRD SYITTLNVCQ
910 920 930 940 950
AYTLKRIRDP NYHVTLRPHI SKEYAAEPSK PADELIHLNP TSEYAPGLED
960
TLILTMKGIA AGMQNTG
Length:967
Mass (Da):110,629
Last modified:April 1, 1993 - v1
Checksum:i8317EA8078C038C0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti291 – 292KH → N in CAA88829 (Ref. 2) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64144 Genomic DNA. Translation: CAA45505.1.
Z48966 mRNA. Translation: CAA88829.1.
PIRiS25081.
S52853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64144 Genomic DNA. Translation: CAA45505.1.
Z48966 mRNA. Translation: CAA88829.1.
PIRiS25081.
S52853.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZGBX-ray2.71A/B6-967[»]
ProteinModelPortaliQ01647.
SMRiQ01647.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ01647.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00321.
BRENDAi4.1.1.31. 2269.

Family and domain databases

HAMAPiMF_00595. PEPcase_type1. 1 hit.
InterProiIPR021135. PEP_COase.
IPR022805. PEP_COase_bac/pln-type.
IPR018129. PEP_COase_Lys_AS.
IPR033129. PEPCASE_His_AS.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiCAPP1_FLAPR
AccessioniPrimary (citable) accession number: Q01647
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 30, 2016
This is version 90 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

3D-structure, Allosteric enzyme

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

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 one 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.