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Protein

Phosphoenolpyruvate carboxylase 1

Gene

PEP1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: 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: C4 acid pathway

This protein is involved in the pathway C4 acid pathway, which is part of Photosynthesis.
View all proteins of this organism that are known to be involved in the pathway C4 acid pathway and in Photosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1771 Publication1
Active sitei6061 Publication1
Active sitei6471 Publication1

GO - Molecular functioni

  • phosphoenolpyruvate carboxylase activity Source: CACAO

GO - Biological processi

  • carbon fixation Source: UniProtKB-KW
  • photosynthesis Source: UniProtKB-KW
  • response to ammonium ion Source: AgBase
  • response to cytokinin Source: AgBase
  • response to nitrate Source: AgBase
  • 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

BRENDAi4.1.1.31. 6752.
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 cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi30066.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001666671 – 970Phosphoenolpyruvate carboxylase 1Add BLAST970

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP04711.
PRIDEiP04711.

PTM databases

iPTMnetiP04711.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi4577.GRMZM2G083841_P01.

Structurei

Secondary structure

1970
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 53Combined sources18
Helixi55 – 72Combined sources18
Helixi78 – 89Combined sources12
Helixi92 – 122Combined sources31
Helixi143 – 151Combined sources9
Helixi158 – 166Combined sources9
Beta strandi169 – 175Combined sources7
Helixi184 – 199Combined sources16
Helixi207 – 226Combined sources20
Helixi237 – 248Combined sources12
Turni249 – 255Combined sources7
Helixi256 – 268Combined sources13
Turni269 – 271Combined sources3
Beta strandi282 – 287Combined sources6
Turni289 – 291Combined sources3
Helixi301 – 329Combined sources29
Helixi337 – 350Combined sources14
Beta strandi359 – 361Combined sources3
Helixi370 – 394Combined sources25
Helixi402 – 404Combined sources3
Helixi409 – 425Combined sources17
Turni430 – 434Combined sources5
Helixi435 – 446Combined sources12
Beta strandi449 – 456Combined sources8
Helixi459 – 473Combined sources15
Helixi478 – 480Combined sources3
Helixi483 – 495Combined sources13
Helixi509 – 523Combined sources15
Helixi526 – 528Combined sources3
Beta strandi529 – 534Combined sources6
Helixi541 – 552Combined sources12
Beta strandi561 – 565Combined sources5
Helixi568 – 572Combined sources5
Helixi574 – 582Combined sources9
Helixi585 – 591Combined sources7
Beta strandi593 – 601Combined sources9
Helixi604 – 607Combined sources4
Helixi610 – 629Combined sources20
Turni630 – 632Combined sources3
Beta strandi634 – 640Combined sources7
Helixi645 – 647Combined sources3
Helixi652 – 657Combined sources6
Beta strandi667 – 673Combined sources7
Helixi674 – 681Combined sources8
Helixi684 – 703Combined sources20
Helixi711 – 732Combined sources22
Helixi738 – 745Combined sources8
Helixi749 – 754Combined sources6
Beta strandi761 – 765Combined sources5
Helixi768 – 771Combined sources4
Helixi775 – 783Combined sources9
Helixi788 – 791Combined sources4
Helixi794 – 804Combined sources11
Helixi808 – 818Combined sources11
Helixi820 – 833Combined sources14
Helixi838 – 847Combined sources10
Turni851 – 853Combined sources3
Helixi854 – 875Combined sources22
Helixi885 – 913Combined sources29
Turni937 – 941Combined sources5
Beta strandi942 – 944Combined sources3
Beta strandi946 – 948Combined sources3
Helixi951 – 966Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQOX-ray3.00A/B1-970[»]
4UOLX-ray3.30A/B/C/D35-970[»]
ProteinModelPortaliP04711.
SMRiP04711.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04711.

Family & Domainsi

Sequence similaritiesi

Belongs to the PEPCase type 1 family.Curated

Phylogenomic databases

eggNOGiENOG410JW91. Eukaryota.
COG2352. LUCA.
HOGENOMiHOG000238648.

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.

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti239A → D (PubMed:3005978).Curated1
Sequence conflicti239A → D (PubMed:2731539).Curated1
Sequence conflicti338 – 339EL → DV in CAA27270 (PubMed:3005978).Curated2
Sequence conflicti482P → S (PubMed:3005978).Curated1
Sequence conflicti482P → S (PubMed:2731539).Curated1
Sequence conflicti509D → E in CAA33663 (PubMed:2731539).Curated1
Sequence conflicti557 – 559QPL → PAV (PubMed:3005978).Curated3
Sequence conflicti557 – 559QPL → PAV (PubMed:2731539).Curated3
Sequence conflicti570D → S (PubMed:3005978).Curated1
Sequence conflicti570D → S (PubMed:2731539).Curated1
Sequence conflicti573 – 574SA → LR in CAA27270 (PubMed:3005978).Curated2
Sequence conflicti687C → S in CAA27270 (PubMed:3005978).Curated1
Sequence conflicti736A → P in CAA27270 (PubMed:3005978).Curated1
Sequence conflicti963A → R in CAA27270 (PubMed:3005978).Curated1

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.
UniGeneiZm.137741.
Zm.2433.
Zm.94462.

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.
UniGeneiZm.137741.
Zm.2433.
Zm.94462.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQOX-ray3.00A/B1-970[»]
4UOLX-ray3.30A/B/C/D35-970[»]
ProteinModelPortaliP04711.
SMRiP04711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G083841_P01.

PTM databases

iPTMnetiP04711.

Proteomic databases

PaxDbiP04711.
PRIDEiP04711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MaizeGDBi30066.

Phylogenomic databases

eggNOGiENOG410JW91. Eukaryota.
COG2352. LUCA.
HOGENOMiHOG000238648.

Enzyme and pathway databases

UniPathwayiUPA00322.
BRENDAi4.1.1.31. 6752.
SABIO-RKP04711.

Miscellaneous databases

EvolutionaryTraceiP04711.

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_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 2, 2016
This is version 137 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, Complete proteome, Direct protein sequencing, Reference proteome

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.