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Protein

Phosphoenolpyruvate carboxykinase [ATP]

Gene

pckA

Organism
Anaerobiospirillum succiniciproducens
Status
Reviewed-Annotation score: Annotation score: 5 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 similarity2 Publications

Catalytic activityi

ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2.UniRule annotation2 Publications

Cofactori

Mn2+UniRule annotation1 PublicationNote: Binds 1 Mn2+ ion per subunit.UniRule annotation1 Publication

Enzyme regulationi

Inhibited by p-chloromercuribenzoate.1 Publication

Kineticsi

  1. KM=0.42 mM for ADP (at 37 degrees Celsius and at pH 6.2)2 Publications
  2. KM=0.54 mM for PEP (at 37 degrees Celsius and at pH 6.2)2 Publications
  3. KM=1.2 mM for OAA (at 37 degrees Celsius and at pH 6.2)2 Publications
  4. KM=2.3 mM for ATP (at 37 degrees Celsius and at pH 6.2)2 Publications
  5. KM=17 mM for bicarbonate (at 37 degrees Celsius and at pH 6.2)2 Publications
  1. Vmax=10 µmol/min/mg enzyme (at 37 degrees Celsius and at pH 6.2)2 Publications

pH dependencei

Optimum pH is between 6.7 and 7.1. The enzyme is stable from pH 5.0 to 9.0. It completely losing activity at pH values lower than 4.5 and retaining some activity in the pH range 9-12.2 Publications

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 sitei60Substrate1
Binding sitei200SubstrateUniRule annotation1
Metal bindingi206ManganeseUniRule annotation1 Publication1
Binding sitei206ATPUniRule annotation1
Binding sitei206SubstrateUniRule annotation1
Metal bindingi225Manganese; via tele nitrogenUniRule annotation1 Publication1
Binding sitei225ATPUniRule annotation1
Binding sitei244Substrate1
Metal bindingi263ManganeseUniRule annotation1 Publication1
Binding sitei291ATPUniRule annotation1
Binding sitei327ATPUniRule annotation1 Publication1
Binding sitei327SubstrateUniRule annotation1
Binding sitei449ATPUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi242 – 250ATP1 Publication9
Nucleotide bindingi443 – 444ATPUniRule annotation1 Publication2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi4.1.1.49. 330.
SABIO-RKO09460.
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
OrganismiAnaerobiospirillum succiniciproducens
Taxonomic identifieri13335 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesSuccinivibrionaceaeAnaerobiospirillum

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002038012 – 532Phosphoenolpyruvate carboxykinase [ATP]Add BLAST531

Interactioni

Subunit structurei

Monomer.UniRule annotation2 Publications

Structurei

Secondary structure

1532
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 9Combined sources7
Beta strandi16 – 21Combined sources6
Helixi24 – 31Combined sources8
Helixi38 – 40Combined sources3
Beta strandi42 – 44Combined sources3
Beta strandi48 – 52Combined sources5
Helixi62 – 64Combined sources3
Beta strandi65 – 68Combined sources4
Helixi71 – 73Combined sources3
Beta strandi81 – 83Combined sources3
Beta strandi88 – 90Combined sources3
Helixi92 – 106Combined sources15
Beta strandi107 – 120Combined sources14
Turni122 – 124Combined sources3
Beta strandi126 – 133Combined sources8
Helixi135 – 144Combined sources10
Helixi150 – 153Combined sources4
Beta strandi159 – 165Combined sources7
Turni171 – 177Combined sources7
Beta strandi179 – 181Combined sources3
Beta strandi183 – 187Combined sources5
Turni188 – 191Combined sources4
Beta strandi192 – 197Combined sources6
Helixi203 – 215Combined sources13
Helixi217 – 219Combined sources3
Beta strandi222 – 231Combined sources10
Beta strandi236 – 241Combined sources6
Helixi248 – 252Combined sources5
Beta strandi257 – 267Combined sources11
Beta strandi272 – 275Combined sources4
Beta strandi277 – 282Combined sources6
Turni288 – 290Combined sources3
Helixi292 – 297Combined sources6
Beta strandi303 – 306Combined sources4
Beta strandi327 – 331Combined sources5
Helixi332 – 334Combined sources3
Beta strandi335 – 338Combined sources4
Beta strandi341 – 346Combined sources6
Beta strandi348 – 355Combined sources8
Beta strandi364 – 367Combined sources4
Helixi370 – 379Combined sources10
Beta strandi381 – 384Combined sources4
Beta strandi396 – 399Combined sources4
Helixi401 – 403Combined sources3
Helixi405 – 407Combined sources3
Helixi412 – 426Combined sources15
Beta strandi429 – 434Combined sources6
Beta strandi441 – 443Combined sources3
Helixi446 – 457Combined sources12
Helixi460 – 463Combined sources4
Beta strandi466 – 469Combined sources4
Turni470 – 473Combined sources4
Beta strandi474 – 478Combined sources5
Helixi486 – 488Combined sources3
Helixi490 – 493Combined sources4
Beta strandi494 – 496Combined sources3
Helixi497 – 515Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YTMX-ray2.20A/B1-532[»]
1YVYX-ray2.35A/B1-532[»]
ProteinModelPortaliO09460.
SMRiO09460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO09460.

Family & Domainsi

Sequence similaritiesi

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

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.

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

O09460-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSESLAKY GITGATNIVH NPSHEELFAA ETQASLEGFE KGTVTEMGAV
60 70 80 90 100
NVMTGVYTGR SPKDKFIVKN EASKEIWWTS DEFKNDNKPV TEEAWAQLKA
110 120 130 140 150
LAGKELSNKP LYVVDLFCGA NENTRLKIRF VMEVAWQAHF VTNMFIRPTE
160 170 180 190 200
EELKGFEPDF VVLNASKAKV ENFKELGLNS ETAVVFNLAE KMQIILNTWY
210 220 230 240 250
GGEMKKGMFS MMNFYLPLQG IAAMHCSANT DLEGKNTAIF FGLSGTGKTT
260 270 280 290 300
LSTDPKRLLI GDDEHGWDDD GVFNFEGGCY AKVINLSKEN EPDIWGAIKR
310 320 330 340 350
NALLENVTVD ANGKVDFADK SVTENTRVSY PIFHIKNIVK PVSKAPAAKR
360 370 380 390 400
VIFLSADAFG VLPPVSILSK EQTKYYFLSG FTAKLAGTER GITEPTPTFS
410 420 430 440 450
SCFGAAFLTL PPTKYAEVLV KRMEASGAKA YLVNTGWNGT GKRISIKDTR
460 470 480 490 500
GIIDAILDGS IDTANTATIP YFNFTVPTEL KGVDTKILDP RNTYADASEW
510 520 530
EVKAKDLAER FQKNFKKFES LGGDLVKAGP QL
Length:532
Mass (Da):58,643
Last modified:July 1, 1997 - v1
Checksum:i983ABC71930F9E44
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U95960 Genomic DNA. Translation: AAC45394.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U95960 Genomic DNA. Translation: AAC45394.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YTMX-ray2.20A/B1-532[»]
1YVYX-ray2.35A/B1-532[»]
ProteinModelPortaliO09460.
SMRiO09460.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00138.
BRENDAi4.1.1.49. 330.
SABIO-RKO09460.

Miscellaneous databases

EvolutionaryTraceiO09460.

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_ANASU
AccessioniPrimary (citable) accession number: O09460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 89 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, Direct protein sequencing

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.