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Protein

Phosphoenolpyruvate carboxykinase [ATP]

Gene

pckA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA (By similarity).By similarity1 Publication

Catalytic activityi

ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2.UniRule annotation

Cofactori

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

Enzyme regulationi

Allosterically activated by calcium.By similarity

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 sitei52SubstrateUniRule annotation1
Metal bindingi130Calcium; via carbonyl oxygen1
Metal bindingi131Calcium; via carbonyl oxygen1
Metal bindingi133Calcium; via carbonyl oxygen1
Binding sitei191SubstrateUniRule annotation1
Metal bindingi197ManganeseUniRule annotation1
Binding sitei197ATPUniRule annotation1
Binding sitei197SubstrateUniRule annotation1
Metal bindingi216Manganese 2; via tele nitrogenUniRule annotation1
Binding sitei216ATPUniRule annotation1
Metal bindingi253ManganeseUniRule annotation1
Metal bindingi267Calcium; via carbonyl oxygen1
Binding sitei281ATPUniRule annotation1
Binding sitei319ATPUniRule annotation1
Binding sitei319SubstrateUniRule annotation1
Binding sitei439ATP; via carbonyl oxygenUniRule annotation2 Publications1
Binding sitei444ATPUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi232 – 240ATPUniRule annotation2 Publications9
Nucleotide bindingi438 – 439ATP2 Publications2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

ATP-binding, Calcium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.1.1.49. 2305.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxykinase [ATP]UniRule annotation (EC:4.1.1.49UniRule annotation)
Short name:
PCKUniRule annotation
Short name:
PEP carboxykinaseUniRule annotation
Short name:
PEPCKUniRule annotation
Gene namesi
Name:pckAUniRule annotation
Synonyms:tthHB8IM
Ordered Locus Names:TTHA0278
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002369521 – 529Phosphoenolpyruvate carboxykinase [ATP]Add BLAST529

Interactioni

Subunit structurei

Dimer of dimers.2 Publications

Protein-protein interaction databases

STRINGi300852.TTHA0278.

Structurei

Secondary structure

1529
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Beta strandi15 – 18Combined sources4
Helixi21 – 30Combined sources10
Beta strandi42 – 44Combined sources3
Helixi54 – 56Combined sources3
Beta strandi57 – 60Combined sources4
Turni63 – 68Combined sources6
Turni72 – 74Combined sources3
Beta strandi75 – 78Combined sources4
Helixi80 – 95Combined sources16
Beta strandi99 – 106Combined sources8
Turni110 – 112Combined sources3
Beta strandi114 – 121Combined sources8
Helixi123 – 132Combined sources10
Helixi136 – 139Combined sources4
Beta strandi151 – 157Combined sources7
Helixi164 – 167Combined sources4
Beta strandi170 – 172Combined sources3
Beta strandi174 – 178Combined sources5
Turni179 – 182Combined sources4
Beta strandi183 – 188Combined sources6
Helixi193 – 206Combined sources14
Helixi207 – 210Combined sources4
Beta strandi213 – 216Combined sources4
Beta strandi218 – 221Combined sources4
Beta strandi227 – 232Combined sources6
Helixi238 – 241Combined sources4
Beta strandi249 – 257Combined sources9
Beta strandi262 – 265Combined sources4
Beta strandi267 – 272Combined sources6
Turni278 – 280Combined sources3
Helixi282 – 288Combined sources7
Beta strandi294 – 297Combined sources4
Turni302 – 304Combined sources3
Beta strandi319 – 323Combined sources5
Helixi324 – 326Combined sources3
Beta strandi328 – 330Combined sources3
Beta strandi334 – 336Combined sources3
Beta strandi339 – 346Combined sources8
Beta strandi355 – 359Combined sources5
Helixi361 – 370Combined sources10
Beta strandi372 – 375Combined sources4
Beta strandi387 – 390Combined sources4
Helixi392 – 394Combined sources3
Helixi396 – 398Combined sources3
Helixi403 – 417Combined sources15
Beta strandi420 – 425Combined sources6
Beta strandi427 – 432Combined sources6
Turni433 – 435Combined sources3
Beta strandi436 – 438Combined sources3
Helixi441 – 452Combined sources12
Helixi455 – 458Combined sources4
Beta strandi461 – 463Combined sources3
Turni465 – 467Combined sources3
Beta strandi470 – 473Combined sources4
Helixi480 – 483Combined sources4
Helixi485 – 488Combined sources4
Helixi492 – 514Combined sources23
Helixi519 – 523Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J3BX-ray2.00A/B1-529[»]
1XKVX-ray2.20A/B1-529[»]
2PC9X-ray2.40A/B/C/D1-529[»]
ProteinModelPortaliQ5SLL5.
SMRiQ5SLL5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLL5.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DJ1. Bacteria.
COG1866. LUCA.
HOGENOMiHOG000271471.
KOiK01610.
OMAiFILPRRF.
PhylomeDBiQ5SLL5.

Family and domain databases

CDDicd00484. PEPCK_ATP. 1 hit.
Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00453. PEPCK_ATP. 1 hit.
InterProiIPR001272. PEP_carboxykinase_ATP.
IPR013035. PEP_carboxykinase_C.
IPR008210. PEP_carboxykinase_N.
IPR015994. PEPCK_ATP_CS.
[Graphical view]
PfamiPF01293. PEPCK_ATP. 1 hit.
[Graphical view]
PIRSFiPIRSF006294. PEP_crbxkin. 1 hit.
SUPFAMiSSF68923. SSF68923. 1 hit.
TIGRFAMsiTIGR00224. pckA. 1 hit.
PROSITEiPS00532. PEPCK_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SLL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRLEALGIH PKKRVFWNTV SPVLVEHTLL RGEGLLAHHG PLVVDTTPYT
60 70 80 90 100
GRSPKDKFVV REPEVEGEIW WGEVNQPFAP EAFEALYQRV VQYLSERDLY
110 120 130 140 150
VQDLYAGADR RYRLAVRVVT ESPWHALFAR NMFILPRRFG NDDEVEAFVP
160 170 180 190 200
GFTVVHAPYF QAVPERDGTR SEVFVGISFQ RRLVLIVGTK YAGEIKKSIF
210 220 230 240 250
TVMNYLMPKR GVFPMHASAN VGKEGDVAVF FGLSGTGKTT LSTDPERPLI
260 270 280 290 300
GDDEHGWSED GVFNFEGGCY AKVIRLSPEH EPLIYKASNQ FEAILENVVV
310 320 330 340 350
NPESRRVQWD DDSKTENTRS SYPIAHLENV VESGVAGHPR AIFFLSADAY
360 370 380 390 400
GVLPPIARLS PEEAMYYFLS GYTARVAGTE RGVTEPRATF SACFGAPFLP
410 420 430 440 450
MHPGVYARML GEKIRKHAPR VYLVNTGWTG GPYGVGYRFP LPVTRALLKA
460 470 480 490 500
ALSGALENVP YRRDPVFGFE VPLEAPGVPQ ELLNPRETWA DKEAYDQQAR
510 520
KLARLFQENF QKYASGVAKE VAEAGPRTE
Length:529
Mass (Da):59,314
Last modified:December 21, 2004 - v1
Checksum:i62FC60C17D719D70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70101.1.
RefSeqiWP_011227826.1. NC_006461.1.
YP_143544.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70101; BAD70101; BAD70101.
GeneIDi3168667.
KEGGittj:TTHA0278.
PATRICi23955511. VBITheThe93045_0278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70101.1.
RefSeqiWP_011227826.1. NC_006461.1.
YP_143544.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J3BX-ray2.00A/B1-529[»]
1XKVX-ray2.20A/B1-529[»]
2PC9X-ray2.40A/B/C/D1-529[»]
ProteinModelPortaliQ5SLL5.
SMRiQ5SLL5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70101; BAD70101; BAD70101.
GeneIDi3168667.
KEGGittj:TTHA0278.
PATRICi23955511. VBITheThe93045_0278.

Phylogenomic databases

eggNOGiENOG4105DJ1. Bacteria.
COG1866. LUCA.
HOGENOMiHOG000271471.
KOiK01610.
OMAiFILPRRF.
PhylomeDBiQ5SLL5.

Enzyme and pathway databases

UniPathwayiUPA00138.
BRENDAi4.1.1.49. 2305.

Miscellaneous databases

EvolutionaryTraceiQ5SLL5.

Family and domain databases

CDDicd00484. PEPCK_ATP. 1 hit.
Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00453. PEPCK_ATP. 1 hit.
InterProiIPR001272. PEP_carboxykinase_ATP.
IPR013035. PEP_carboxykinase_C.
IPR008210. PEP_carboxykinase_N.
IPR015994. PEPCK_ATP_CS.
[Graphical view]
PfamiPF01293. PEPCK_ATP. 1 hit.
[Graphical view]
PIRSFiPIRSF006294. PEP_crbxkin. 1 hit.
SUPFAMiSSF68923. SSF68923. 1 hit.
TIGRFAMsiTIGR00224. pckA. 1 hit.
PROSITEiPS00532. PEPCK_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPCKA_THET8
AccessioniPrimary (citable) accession number: Q5SLL5
Secondary accession number(s): P84128, Q7SIC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.