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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521SubstrateUniRule annotation
Metal bindingi130 – 1301Calcium; via carbonyl oxygen
Metal bindingi131 – 1311Calcium; via carbonyl oxygen
Metal bindingi133 – 1331Calcium; via carbonyl oxygen
Binding sitei191 – 1911SubstrateUniRule annotation
Metal bindingi197 – 1971ManganeseUniRule annotation
Binding sitei197 – 1971ATPUniRule annotation
Binding sitei197 – 1971SubstrateUniRule annotation
Metal bindingi216 – 2161Manganese 2; via tele nitrogenUniRule annotation
Binding sitei216 – 2161ATPUniRule annotation
Metal bindingi253 – 2531ManganeseUniRule annotation
Metal bindingi267 – 2671Calcium; via carbonyl oxygen
Binding sitei281 – 2811ATPUniRule annotation
Binding sitei319 – 3191ATPUniRule annotation
Binding sitei319 – 3191SubstrateUniRule annotation
Binding sitei439 – 4391ATP; via carbonyl oxygenUniRule annotation2 Publications
Binding sitei444 – 4441ATPUniRule annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi232 – 2409ATPUniRule annotation2 Publications
Nucleotide bindingi438 – 4392ATP2 Publications

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

BioCyciTTHE300852:GH8R-292-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Phosphoenolpyruvate carboxykinase [ATP]PRO_0000236952Add
BLAST

Interactioni

Subunit structurei

Dimer of dimers.2 Publications

Protein-protein interaction databases

STRINGi300852.TTHA0278.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Beta strandi15 – 184Combined sources
Helixi21 – 3010Combined sources
Beta strandi42 – 443Combined sources
Helixi54 – 563Combined sources
Beta strandi57 – 604Combined sources
Turni63 – 686Combined sources
Turni72 – 743Combined sources
Beta strandi75 – 784Combined sources
Helixi80 – 9516Combined sources
Beta strandi99 – 1068Combined sources
Turni110 – 1123Combined sources
Beta strandi114 – 1218Combined sources
Helixi123 – 13210Combined sources
Helixi136 – 1394Combined sources
Beta strandi151 – 1577Combined sources
Helixi164 – 1674Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi174 – 1785Combined sources
Turni179 – 1824Combined sources
Beta strandi183 – 1886Combined sources
Helixi193 – 20614Combined sources
Helixi207 – 2104Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi227 – 2326Combined sources
Helixi238 – 2414Combined sources
Beta strandi249 – 2579Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi267 – 2726Combined sources
Turni278 – 2803Combined sources
Helixi282 – 2887Combined sources
Beta strandi294 – 2974Combined sources
Turni302 – 3043Combined sources
Beta strandi319 – 3235Combined sources
Helixi324 – 3263Combined sources
Beta strandi328 – 3303Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi339 – 3468Combined sources
Beta strandi355 – 3595Combined sources
Helixi361 – 37010Combined sources
Beta strandi372 – 3754Combined sources
Beta strandi387 – 3904Combined sources
Helixi392 – 3943Combined sources
Helixi396 – 3983Combined sources
Helixi403 – 41715Combined sources
Beta strandi420 – 4256Combined sources
Beta strandi427 – 4326Combined sources
Turni433 – 4353Combined sources
Beta strandi436 – 4383Combined sources
Helixi441 – 45212Combined sources
Helixi455 – 4584Combined sources
Beta strandi461 – 4633Combined sources
Turni465 – 4673Combined sources
Beta strandi470 – 4734Combined sources
Helixi480 – 4834Combined sources
Helixi485 – 4884Combined sources
Helixi492 – 51423Combined sources
Helixi519 – 5235Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3BX-ray2.00A/B1-529[»]
1XKVX-ray2.20A/B1-529[»]
2PC9X-ray2.40A/B/C/D1-529[»]
ProteinModelPortaliQ5SLL5.
SMRiQ5SLL5. Positions 1-528.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3BX-ray2.00A/B1-529[»]
1XKVX-ray2.20A/B1-529[»]
2PC9X-ray2.40A/B/C/D1-529[»]
ProteinModelPortaliQ5SLL5.
SMRiQ5SLL5. Positions 1-528.
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.
BioCyciTTHE300852:GH8R-292-MONOMER.
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: September 7, 2016
This is version 86 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.