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Protein

Phosphoenolpyruvate carboxylase, housekeeping isozyme

Gene
N/A
Organism
Saccharum hybrid (Sugarcane)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.

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

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxylase, housekeeping isozyme (EC:4.1.1.31)
Short name:
PEPC
Short name:
PEPCase
OrganismiSaccharum hybrid (Sugarcane)
Taxonomic identifieri15819 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeSaccharum

Organism-specific databases

GrameneiP29193.

Subcellular locationi

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 – 966966Phosphoenolpyruvate carboxylase, housekeeping isozymePRO_0000166675Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP29193.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

SMRiP29193. Positions 31-966.
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.

P29193-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARNAVDKAT SIDAQLRLLA PQKLSDDDKL VEYDALLLDR FLDILQDLHG
60 70 80 90 100
EDIRETVQEC YELAAEYENK LDPKMLDEIG NVLTSLDPGD SIVITKSFSH
110 120 130 140 150
MLILANLAEE VQIAYRRRIK LKKGDFVDEN SATTESDIEE TLKRLMHQLK
160 170 180 190 200
KSPLEVFDAL KNQTVDLVLT AHPTQSVRRS LLQKHGRIRN CLTQLYAKDI
210 220 230 240 250
TPDEKQELDE ALQREIQAAF RTDEIRRAPP TPQDEMRAGM SYFHETIWKG
260 270 280 290 300
VPKFLRRVDT ALKNIGINER LPYNAPIIQF SSWMGGDRDG NPRVTPEITR
310 320 330 340 350
DVCLLARMMA ANLYNAQIED LMFELSMWRC SDELRVKVDE LHRSSKKDTT
360 370 380 390 400
KHYIEFWKQV PPSEPYRVIL SDVRDKLYNT RERARHLLAS GFSEIPEEAT
410 420 430 440 450
FTDVEQFLEP LELCYRSLCA CGDRSVADGS LLDFLRQVST FGLSLVRLDI
460 470 480 490 500
RQESDRHTDV MDAITEYLGI GSYRKWTEEK RQEWLLSELN GKRPLFGPDL
510 520 530 540 550
PKSDEIADVL DTFHVLAELP SDSFGAYVIS MATAPSDVLA VELLQRECHV
560 570 580 590 600
KKPLRVVPLF EKLADLEAAP AALARLFSVE WYRNRINGKQ EVMIGYSDSG
610 620 630 640 650
KDAGRFSAAW QLYKAQEELI NVAKLYGVKL TMFHGRGGTV GRGGGPTHLA
660 670 680 690 700
ILSQPPETIH GSLRVTVQGE VIEQSFGEEH LCFRTLQRFT AATLEHGMHP
710 720 730 740 750
PISPKPEWRA LMDEMAIVAT KEYRSIVFEE PRFVEYFRLA TPEMEYGRMN
760 770 780 790 800
IGSRPSKRKP SAGIESLRAI PWIFAWTQTR FHLPVWLGFG AAFKHVLDKD
810 820 830 840 850
IRNLQTLQEM YNQWPFFRVT IDLVEMVFAK GDPGIAALYD KLLVSEDLWS
860 870 880 890 900
FGKRLRANYE ETKQLLLQVA GHKDLLEGDP YLKQRLRIRD SYITALNVCQ
910 920 930 940 950
AYMLKRIRDP GFQVNPGPHL SKDIMDMGKP ASELVKLNTT SEYAPGLEDT
960
LILTMKGIAA GMQNTG
Length:966
Mass (Da):110,219
Last modified:November 30, 1992 - v1
Checksum:iFD84762318FED073
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86661 Genomic DNA. Translation: AAC33164.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86661 Genomic DNA. Translation: AAC33164.1.

3D structure databases

SMRiP29193. Positions 31-966.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP29193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP29193.

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. "Structure and expression of a sugarcane gene encoding a housekeeping phosphoenolpyruvate carboxylase."
    Albert H.A., Martin T., Sun S.S.
    Plant Mol. Biol. 20:663-671(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCAPP1_SACHY
AccessioniPrimary (citable) accession number: P29193
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 1992
Last sequence update: November 30, 1992
Last modified: March 31, 2015
This is version 78 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

Documents

  1. 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.