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Protein

Phosphoenolpyruvate carboxykinase [GTP]

Gene

pckG

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the gluconeogenesis, in growth on fatty acids and is important for initiation of infection in the macrophages. Catalyzes the GTP-dependent 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.2 Publications

Catalytic activityi

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.UniRule annotation

Cofactori

Mn2+UniRule annotationNote: Binds 1 Mn2+ ion per subunit.UniRule annotation

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.UniRule annotation
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 sitei81SubstrateUniRule annotation1
Metal bindingi229ManganeseUniRule annotation1
Metal bindingi249Manganese; via tele nitrogenUniRule annotation1
Binding sitei271SubstrateUniRule annotation1
Active sitei273UniRule annotation1
Metal bindingi296ManganeseUniRule annotation1
Binding sitei389GTPUniRule annotation1
Binding sitei420GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi272 – 277GTPUniRule annotation6
Nucleotide bindingi515 – 518GTPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

  • cellular response to iron ion starvation Source: MTBBASE
  • gluconeogenesis Source: UniProtKB-HAMAP
  • response to host immune response Source: MTBBASE
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

BioCyciMTBH37RV:G185E-4331-MONOMER.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxykinase [GTP]1 PublicationUniRule annotation (EC:4.1.1.32UniRule annotation)
Short name:
PEP carboxykinase1 PublicationUniRule annotation
Short name:
PEPCK1 PublicationUniRule annotation
Alternative name(s):
GTP-dependent phosphoenolpyruvate carboxykinaseUniRule annotation
Short name:
GTP-PEPCKUniRule annotation
Gene namesi
Name:pckGUniRule annotation
Synonyms:pck1, pckA
Ordered Locus Names:Rv0211
ORF Names:MTCY08D5.06
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0211.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to grow in the absence of an external carbon source when grown with fatty acids acetate, valerate, or butyrate as the sole carbon source. This mutant also fails to replicate in mouse lungs. PEPCK depletion during the chronic phase of infection results in mycobacterial clearance.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001036112 – 606Phosphoenolpyruvate carboxykinase [GTP]Add BLAST605

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP9WIH3.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi83332.Rv0211.

Structurei

Secondary structure

1606
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni7 – 11Combined sources5
Helixi17 – 30Combined sources14
Beta strandi33 – 37Combined sources5
Helixi42 – 54Combined sources13
Beta strandi57 – 60Combined sources4
Turni63 – 65Combined sources3
Beta strandi66 – 68Combined sources3
Beta strandi70 – 72Combined sources3
Helixi83 – 85Combined sources3
Beta strandi86 – 88Combined sources3
Helixi93 – 95Combined sources3
Helixi105 – 116Combined sources12
Turni117 – 122Combined sources6
Beta strandi123 – 133Combined sources11
Beta strandi137 – 139Combined sources3
Beta strandi141 – 148Combined sources8
Helixi150 – 159Combined sources10
Beta strandi160 – 163Combined sources4
Helixi164 – 170Combined sources7
Turni171 – 173Combined sources3
Beta strandi177 – 182Combined sources6
Beta strandi203 – 207Combined sources5
Turni208 – 211Combined sources4
Beta strandi212 – 217Combined sources6
Helixi221 – 223Combined sources3
Helixi227 – 233Combined sources7
Helixi234 – 243Combined sources10
Beta strandi246 – 249Combined sources4
Beta strandi251 – 256Combined sources6
Beta strandi258 – 260Combined sources3
Beta strandi262 – 268Combined sources7
Helixi275 – 279Combined sources5
Beta strandi289 – 296Combined sources8
Beta strandi298 – 302Combined sources5
Beta strandi304 – 306Combined sources3
Beta strandi308 – 311Combined sources4
Beta strandi315 – 320Combined sources6
Turni326 – 328Combined sources3
Helixi330 – 337Combined sources8
Beta strandi342 – 345Combined sources4
Beta strandi347 – 349Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi364 – 367Combined sources4
Beta strandi373 – 375Combined sources3
Turni376 – 378Combined sources3
Beta strandi389 – 393Combined sources5
Helixi394 – 396Combined sources3
Helixi402 – 405Combined sources4
Beta strandi410 – 418Combined sources9
Beta strandi422 – 425Combined sources4
Beta strandi427 – 430Combined sources4
Helixi434 – 442Combined sources9
Turni451 – 453Combined sources3
Helixi463 – 465Combined sources3
Turni467 – 469Combined sources3
Helixi474 – 486Combined sources13
Helixi490 – 492Combined sources3
Beta strandi495 – 499Combined sources5
Beta strandi510 – 512Combined sources3
Helixi515 – 518Combined sources4
Helixi519 – 529Combined sources11
Beta strandi536 – 538Combined sources3
Beta strandi541 – 543Combined sources3
Helixi546 – 548Combined sources3
Helixi558 – 565Combined sources8
Helixi569 – 586Combined sources18
Helixi587 – 589Combined sources3
Helixi592 – 605Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R43X-ray1.80A1-606[»]
4RCGX-ray2.60A1-606[»]
ProteinModelPortaliP9WIH3.
SMRiP9WIH3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni220 – 222Substrate bindingUniRule annotation3
Regioni387 – 389Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1274. LUCA.
KOiK01596.
OMAiYGENMRV.
PhylomeDBiP9WIH3.

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.

P9WIH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSATIPGLD TAPTNHQGLL SWVEEVAELT QPDRVVFTDG SEEEFQRLCD
60 70 80 90 100
QLVEAGTFIR LNPEKHKNSY LALSDPSDVA RVESRTYICS AKEIDAGPTN
110 120 130 140 150
NWMDPGEMRS IMKDLYRGCM RGRTMYVVPF CMGPLGAEDP KLGVEITDSE
160 170 180 190 200
YVVVSMRTMT RMGKAALEKM GDDGFFVKAL HSVGAPLEPG QKDVAWPCSE
210 220 230 240 250
TKYITHFPET REIWSYGSGY GGNALLGKKC YSLRIASAMA HDEGWLAEHM
260 270 280 290 300
LILKLISPEN KAYYFAAAFP SACGKTNLAM LQPTIPGWRA ETLGDDIAWM
310 320 330 340 350
RFGKDGRLYA VNPEFGFFGV APGTNWKSNP NAMRTIAAGN TVFTNVALTD
360 370 380 390 400
DGDVWWEGLE GDPQHLIDWK GNDWYFRETE TNAAHPNSRY CTPMSQCPIL
410 420 430 440 450
APEWDDPQGV PISGILFGGR RKTTVPLVTE ARDWQHGVFI GATLGSEQTA
460 470 480 490 500
AAEGKVGNVR RDPMAMLPFL GYNVGDYFQH WINLGKHADE SKLPKVFFVN
510 520 530 540 550
WFRRGDDGRF LWPGFGENSR VLKWIVDRIE HKAGGATTPI GTVPAVEDLD
560 570 580 590 600
LDGLDVDAAD VAAALAVDAD EWRQELPLIE EWLQFVGEKL PTGVKDEFDA

LKERLG
Length:606
Mass (Da):67,253
Last modified:April 16, 2014 - v1
Checksum:iAEE29412E6BCCAE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP42939.1.
PIRiA70960.
RefSeqiNP_214725.1. NC_000962.3.
WP_003401212.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP42939; CCP42939; Rv0211.
GeneIDi886744.
KEGGimtu:Rv0211.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP42939.1.
PIRiA70960.
RefSeqiNP_214725.1. NC_000962.3.
WP_003401212.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R43X-ray1.80A1-606[»]
4RCGX-ray2.60A1-606[»]
ProteinModelPortaliP9WIH3.
SMRiP9WIH3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0211.

Proteomic databases

PaxDbiP9WIH3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP42939; CCP42939; Rv0211.
GeneIDi886744.
KEGGimtu:Rv0211.

Organism-specific databases

TubercuListiRv0211.

Phylogenomic databases

eggNOGiCOG1274. LUCA.
KOiK01596.
OMAiYGENMRV.
PhylomeDBiP9WIH3.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciMTBH37RV:G185E-4331-MONOMER.

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 nameiPCKG_MYCTU
AccessioniPrimary (citable) accession number: P9WIH3
Secondary accession number(s): L0T2U6, P65686, P96393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The number of CD4 T-cells is increased in the PEPCK immunized mice although the change of the number of CD8 T-cells is not significant. The cytokines IFN-gamma (IFNG), IL-12 (IL12A or IL12B) and TNF-alpha (TNF) are increased significantly in the mice immunized with PEPCK relative to those immunized with incomplete adjuvant.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.