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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Substrate
Binding sitei200 – 2001SubstrateUniRule annotation
Metal bindingi206 – 2061ManganeseUniRule annotation1 Publication
Binding sitei206 – 2061ATPUniRule annotation
Binding sitei206 – 2061SubstrateUniRule annotation
Metal bindingi225 – 2251Manganese; via tele nitrogenUniRule annotation1 Publication
Binding sitei225 – 2251ATPUniRule annotation
Binding sitei244 – 2441Substrate
Metal bindingi263 – 2631ManganeseUniRule annotation1 Publication
Binding sitei291 – 2911ATPUniRule annotation
Binding sitei327 – 3271ATPUniRule annotation1 Publication
Binding sitei327 – 3271SubstrateUniRule annotation
Binding sitei449 – 4491ATPUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi242 – 2509ATP1 Publication
Nucleotide bindingi443 – 4442ATPUniRule annotation1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 532531Phosphoenolpyruvate carboxykinase [ATP]PRO_0000203801Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation2 Publications

Structurei

Secondary structure

1
532
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97Combined sources
Beta strandi16 – 216Combined sources
Helixi24 – 318Combined sources
Helixi38 – 403Combined sources
Beta strandi42 – 443Combined sources
Beta strandi48 – 525Combined sources
Helixi62 – 643Combined sources
Beta strandi65 – 684Combined sources
Helixi71 – 733Combined sources
Beta strandi81 – 833Combined sources
Beta strandi88 – 903Combined sources
Helixi92 – 10615Combined sources
Beta strandi107 – 12014Combined sources
Turni122 – 1243Combined sources
Beta strandi126 – 1338Combined sources
Helixi135 – 14410Combined sources
Helixi150 – 1534Combined sources
Beta strandi159 – 1657Combined sources
Turni171 – 1777Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi183 – 1875Combined sources
Turni188 – 1914Combined sources
Beta strandi192 – 1976Combined sources
Helixi203 – 21513Combined sources
Helixi217 – 2193Combined sources
Beta strandi222 – 23110Combined sources
Beta strandi236 – 2416Combined sources
Helixi248 – 2525Combined sources
Beta strandi257 – 26711Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi277 – 2826Combined sources
Turni288 – 2903Combined sources
Helixi292 – 2976Combined sources
Beta strandi303 – 3064Combined sources
Beta strandi327 – 3315Combined sources
Helixi332 – 3343Combined sources
Beta strandi335 – 3384Combined sources
Beta strandi341 – 3466Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi364 – 3674Combined sources
Helixi370 – 37910Combined sources
Beta strandi381 – 3844Combined sources
Beta strandi396 – 3994Combined sources
Helixi401 – 4033Combined sources
Helixi405 – 4073Combined sources
Helixi412 – 42615Combined sources
Beta strandi429 – 4346Combined sources
Beta strandi441 – 4433Combined sources
Helixi446 – 45712Combined sources
Helixi460 – 4634Combined sources
Beta strandi466 – 4694Combined sources
Turni470 – 4734Combined sources
Beta strandi474 – 4785Combined sources
Helixi486 – 4883Combined sources
Helixi490 – 4934Combined sources
Beta strandi494 – 4963Combined sources
Helixi497 – 51519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YTMX-ray2.20A/B1-532[»]
1YVYX-ray2.35A/B1-532[»]
ProteinModelPortaliO09460.
SMRiO09460. Positions 2-518.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1YTMX-ray2.20A/B1-532[»]
1YVYX-ray2.35A/B1-532[»]
ProteinModelPortaliO09460.
SMRiO09460. Positions 2-518.
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: September 7, 2016
This is version 87 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.