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Protein

Phosphoenolpyruvate carboxykinase [GTP], mitochondrial

Gene

PCK2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. Facilitates the recycling of lactate carbon in the liver.

Catalytic activityi

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

Cofactori

Mn2+1 PublicationNote: Binds 1 Mn2+ ion per subunit.1 Publication

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei105Substrate1 Publication1
Metal bindingi263Manganese1 Publication1
Metal bindingi283Manganese; via tele nitrogen1 Publication1
Binding sitei305SubstrateBy similarity1
Active sitei3071 Publication1
Metal bindingi330Manganese1 Publication1
Binding sitei424GTPBy similarity1
Binding sitei455GTP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi306 – 311GTP1 Publication6
Nucleotide bindingi549 – 552GTP1 Publication4

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • inosine kinase activity Source: AgBase
  • lactate dehydrogenase activity Source: AgBase
  • manganese ion binding Source: AgBase
  • mRNA binding Source: AgBase
  • phosphoenolpyruvate carboxykinase (GTP) activity Source: AgBase
  • protein-disulfide reductase activity Source: AgBase

GO - Biological processi

  • cellular response to dexamethasone stimulus Source: AgBase
  • cellular response to ethanol Source: AgBase
  • cellular response to insulin stimulus Source: AgBase
  • eggshell formation Source: AgBase
  • embryo development ending in birth or egg hatching Source: AgBase
  • embryonic organ morphogenesis Source: AgBase
  • gluconeogenesis Source: AgBase
  • glucose catabolic process to lactate via pyruvate Source: AgBase
  • glycerol catabolic process Source: AgBase
  • hepatocyte differentiation Source: AgBase
  • kidney interstitial fibroblast differentiation Source: AgBase
  • lactate metabolic process Source: AgBase
  • lactate oxidation Source: AgBase
  • lipid catabolic process Source: AgBase
  • NADH regeneration Source: AgBase
  • oviposition Source: AgBase
  • positive regulation of cAMP-mediated signaling Source: AgBase
  • post-translational protein modification Source: AgBase
  • propionate catabolic process Source: AgBase
  • pyruvate metabolic process Source: AgBase
  • regulation of gluconeogenesis Source: AgBase
  • regulation of viral process Source: AgBase
  • response to cAMP Source: AgBase
  • response to starvation Source: AgBase
  • vitellogenesis Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

GTP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.1.1.32. 1306.
ReactomeiR-GGA-352875. Gluconeogenesis.
SABIO-RKP21642.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxykinase [GTP], mitochondrial (EC:4.1.1.32)
Short name:
PEPCK-M
Gene namesi
Name:PCK2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 33MitochondrionAdd BLAST33
ChainiPRO_000002357034 – 641Phosphoenolpyruvate carboxykinase [GTP], mitochondrialAdd BLAST608

Expressioni

Tissue specificityi

Present in liver and kidney.1 Publication

Inductioni

Appears to be constitutively expressed.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1641
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 56Combined sources14
Beta strandi59 – 63Combined sources5
Helixi68 – 80Combined sources13
Beta strandi83 – 86Combined sources4
Beta strandi90 – 92Combined sources3
Beta strandi94 – 96Combined sources3
Beta strandi102 – 104Combined sources3
Helixi107 – 109Combined sources3
Beta strandi110 – 113Combined sources4
Helixi117 – 119Combined sources3
Beta strandi121 – 123Combined sources3
Helixi139 – 149Combined sources11
Turni151 – 156Combined sources6
Beta strandi157 – 167Combined sources11
Beta strandi171 – 173Combined sources3
Beta strandi175 – 182Combined sources8
Helixi184 – 193Combined sources10
Beta strandi194 – 197Combined sources4
Helixi198 – 201Combined sources4
Beta strandi209 – 214Combined sources6
Helixi233 – 235Combined sources3
Beta strandi237 – 241Combined sources5
Helixi242 – 244Combined sources3
Beta strandi246 – 251Combined sources6
Helixi255 – 258Combined sources4
Helixi261 – 267Combined sources7
Helixi268 – 277Combined sources10
Beta strandi280 – 283Combined sources4
Beta strandi285 – 290Combined sources6
Beta strandi296 – 302Combined sources7
Helixi312 – 314Combined sources3
Beta strandi323 – 330Combined sources8
Beta strandi332 – 336Combined sources5
Beta strandi340 – 345Combined sources6
Beta strandi349 – 354Combined sources6
Turni360 – 362Combined sources3
Helixi364 – 369Combined sources6
Beta strandi371 – 373Combined sources3
Beta strandi375 – 378Combined sources4
Beta strandi380 – 382Combined sources3
Beta strandi407 – 410Combined sources4
Beta strandi424 – 428Combined sources5
Helixi429 – 431Combined sources3
Turni437 – 440Combined sources4
Beta strandi445 – 454Combined sources10
Beta strandi457 – 460Combined sources4
Beta strandi462 – 465Combined sources4
Helixi469 – 477Combined sources9
Beta strandi480 – 482Combined sources3
Beta strandi487 – 489Combined sources3
Beta strandi494 – 496Combined sources3
Helixi498 – 500Combined sources3
Helixi502 – 504Combined sources3
Helixi509 – 519Combined sources11
Beta strandi529 – 535Combined sources7
Beta strandi542 – 546Combined sources5
Helixi549 – 551Combined sources3
Helixi552 – 563Combined sources12
Beta strandi569 – 572Combined sources4
Beta strandi575 – 578Combined sources4
Turni580 – 582Combined sources3
Helixi593 – 596Combined sources4
Helixi601 – 618Combined sources18
Helixi620 – 622Combined sources3
Helixi625 – 639Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FAFX-ray1.70A/B34-641[»]
2FAHX-ray2.09A/B/C/D34-641[»]
2QZYX-ray1.90A/B34-641[»]
SMRiP21642.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21642.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni254 – 256Substrate binding1 Publication3
Regioni422 – 424Substrate bindingBy similarity3

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG053651.
InParanoidiP21642.
KOiK01596.
PhylomeDBiP21642.

Family and domain databases

Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00452. PEPCK_GTP. 1 hit.
InterProiIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PANTHERiPTHR11561. PTHR11561. 1 hit.
PfamiPF00821. PEPCK. 1 hit.
[Graphical view]
PIRSFiPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMiSSF68923. SSF68923. 1 hit.
PROSITEiPS00505. PEPCK_GTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21642-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFWLRGGAQS CRGGETEDRM QRGMWGVGLA RRRLSTSLSA LPAAARDFVE
60 70 80 90 100
EAVRLCRPRE VLLCDGSEEE GKELLRGLQD DGVLHPLPKY DNCWLARTDP
110 120 130 140 150
RDVARVESKT VLVTPEQSDA VPPPPPSGGP PQLGNWMSPN AFQAAVQERF
160 170 180 190 200
PGCMAGRPLY VIPFSMGPPT SPLAKLGVQV TDSPYVVLSM RIMTRVGPAV
210 220 230 240 250
LQRLDDDFVR CLHSVGRPLP LTEPLVSSWP CDRSPVLVAH IPSERRIVSF
260 270 280 290 300
GSGYGGNSLL GKKCFALRIA SRMAQQQGWL AEHMLILGVT SPSGEKRYMA
310 320 330 340 350
AAFPSACGKT NLAMMTPSLP GWRIHCVGDD IAWMKFDDEG RLRAINPERG
360 370 380 390 400
FFGVAPGTSS RTNPNAMATI ARNTIFTNVG LRSDGGVYWD GLDEPTEPGV
410 420 430 440 450
TYTSWLGKPW KHGDPEPCAH PNSRFCAPAD QCPIMDPRWD DPEGVPIDAI
460 470 480 490 500
IFGGRRPRGV PLVVEAFGWR HGVFMGSAMR SEATAAAEHK GGRLMHDPFA
510 520 530 540 550
MRPFFGYNAG RYLEHWLSTG LRSNARLPRL FHVNWFLRDN EGRFVWPGFG
560 570 580 590 600
HNARVLAWIF GRIQGRDTAR PTPIGWVPKE GDLDLGGLPG VDYSQLFPME
610 620 630 640
KGFWEEECRQ LREYYGENFG ADLPRDVMAE LEGLEERVRK M
Length:641
Mass (Da):71,106
Last modified:March 24, 2009 - v2
Checksum:iA5C2BA63C659E633
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti107E → Q in AAA49006 (PubMed:2110163).Curated1
Sequence conflicti129 – 130GP → S in AAA49006 (PubMed:2110163).Curated2
Sequence conflicti235P → R in AAA49006 (PubMed:2110163).Curated1
Sequence conflicti268R → A in AAA49006 (PubMed:2110163).Curated1
Sequence conflicti339E → R in AAA49006 (PubMed:2110163).Curated1
Sequence conflicti502R → S in AAA49006 (PubMed:2110163).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05419 mRNA. Translation: AAA49006.1.
PIRiA35191. QYCHGM.
RefSeqiNP_990801.1. NM_205470.1.
UniGeneiGga.979.

Genome annotation databases

GeneIDi396457.
KEGGigga:396457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05419 mRNA. Translation: AAA49006.1.
PIRiA35191. QYCHGM.
RefSeqiNP_990801.1. NM_205470.1.
UniGeneiGga.979.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FAFX-ray1.70A/B34-641[»]
2FAHX-ray2.09A/B/C/D34-641[»]
2QZYX-ray1.90A/B34-641[»]
SMRiP21642.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396457.
KEGGigga:396457.

Organism-specific databases

CTDi5106.

Phylogenomic databases

HOVERGENiHBG053651.
InParanoidiP21642.
KOiK01596.
PhylomeDBiP21642.

Enzyme and pathway databases

UniPathwayiUPA00138.
BRENDAi4.1.1.32. 1306.
ReactomeiR-GGA-352875. Gluconeogenesis.
SABIO-RKP21642.

Miscellaneous databases

EvolutionaryTraceiP21642.
PROiP21642.

Family and domain databases

Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00452. PEPCK_GTP. 1 hit.
InterProiIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PANTHERiPTHR11561. PTHR11561. 1 hit.
PfamiPF00821. PEPCK. 1 hit.
[Graphical view]
PIRSFiPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMiSSF68923. SSF68923. 1 hit.
PROSITEiPS00505. PEPCK_GTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPCKGM_CHICK
AccessioniPrimary (citable) accession number: P21642
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: March 24, 2009
Last modified: November 2, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are two isozymes: a cytoplasmic one and a mitochondrial one. In birds, PEPCK-M is the sole form of hepatic PEPCK, but it constitutes 60% of the enzyme in the kidney.

Keywords - Technical termi

3D-structure, 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.