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Q01647

- CAPP1_FLAPR

UniProt

Q01647 - CAPP1_FLAPR

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Protein

Phosphoenolpyruvate carboxylase

Gene

PPCA1

Organism
Flaveria pringlei
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei172 – 1721By similarity
Active sitei601 – 6011By 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

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

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 967967Phosphoenolpyruvate carboxylasePRO_0000166664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ01647.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
967
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911Combined sources
Helixi30 – 4920Combined sources
Helixi51 – 7020Combined sources
Helixi74 – 8310Combined sources
Helixi88 – 11528Combined sources
Helixi126 – 1305Combined sources
Turni132 – 1343Combined sources
Helixi138 – 14811Combined sources
Helixi153 – 1619Combined sources
Beta strandi164 – 1696Combined sources
Helixi179 – 19517Combined sources
Helixi202 – 22019Combined sources
Helixi232 – 2398Combined sources
Helixi242 – 2454Combined sources
Helixi247 – 26418Combined sources
Beta strandi278 – 2825Combined sources
Turni284 – 2863Combined sources
Helixi297 – 32529Combined sources
Helixi333 – 34412Combined sources
Helixi365 – 39026Combined sources
Helixi397 – 3993Combined sources
Helixi404 – 42017Combined sources
Helixi424 – 4274Combined sources
Helixi430 – 44112Combined sources
Beta strandi444 – 45310Combined sources
Helixi454 – 46714Combined sources
Turni473 – 4753Combined sources
Helixi478 – 48912Combined sources
Helixi504 – 51815Combined sources
Helixi521 – 5233Combined sources
Beta strandi524 – 5307Combined sources
Helixi535 – 54713Combined sources
Beta strandi555 – 5606Combined sources
Helixi563 – 57715Combined sources
Helixi580 – 5867Combined sources
Beta strandi589 – 5946Combined sources
Helixi596 – 6038Combined sources
Helixi605 – 62622Combined sources
Beta strandi629 – 6346Combined sources
Helixi639 – 6413Combined sources
Helixi645 – 6528Combined sources
Beta strandi662 – 6676Combined sources
Turni669 – 6713Combined sources
Helixi672 – 6765Combined sources
Helixi679 – 69820Combined sources
Helixi706 – 72722Combined sources
Helixi733 – 7408Combined sources
Helixi743 – 7486Combined sources
Beta strandi751 – 7533Combined sources
Turni764 – 7663Combined sources
Helixi769 – 7779Combined sources
Turni778 – 7803Combined sources
Helixi783 – 7864Combined sources
Helixi789 – 79911Combined sources
Helixi802 – 81312Combined sources
Helixi815 – 82915Combined sources
Helixi833 – 84311Combined sources
Helixi846 – 8483Combined sources
Helixi849 – 87022Combined sources
Turni875 – 8784Combined sources
Helixi880 – 90829Combined sources
Helixi948 – 96316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZGBX-ray2.71A/B6-967[»]
ProteinModelPortaliQ01647.
SMRiQ01647. Positions 31-967.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PEPCase type 1 family.Curated

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti291 – 2922KH → N in CAA88829. 1 PublicationCurated

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 .
PIRi S25081.
S52853.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZGB X-ray 2.71 A/B 6-967 [» ]
ProteinModelPortali Q01647.
SMRi Q01647. Positions 31-967.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q01647.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00321 .

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. 2 hits.
PROSITEi PS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Homologous genes for the C4 isoform of phosphoenolpyruvate carboxylase in a C3 and a C4 Flaveria species."
    Hermans J., Westhoff P.
    Mol. Gen. Genet. 234:275-284(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Svensson P., Blaesing O.E., Westhoff P.
    Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leaf.

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 26, 2014
This is version 82 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

External Data

Dasty 3