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A3M840 (PCKG_ACIBT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate carboxykinase [GTP]
Short name=PEP carboxykinase
Short name=PEPCK
EC=4.1.1.32
Alternative name(s):
Phosphoenolpyruvate carboxylase
Gene names
Name:pckG
Ordered Locus Names:A1S_2668
OrganismAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]
Taxonomic identifier400667 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex ›

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the 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 By similarity. HAMAP-Rule MF_00452

Catalytic activity

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2. HAMAP-Rule MF_00452

Cofactor

Binds 1 manganese ion per subunit By similarity.

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_00452

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentCytoplasm
   LigandGTP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: HAMAP

manganese ion binding

Inferred from electronic annotation. Source: HAMAP

phosphoenolpyruvate carboxykinase (GTP) activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Phosphoenolpyruvate carboxykinase [GTP] HAMAP-Rule MF_00452
PRO_1000125041

Regions

Nucleotide binding268 – 2736GTP By similarity
Nucleotide binding516 – 5194GTP By similarity
Region382 – 3843Substrate binding By similarity

Sites

Active site2691 By similarity
Metal binding2251Manganese By similarity
Metal binding2451Manganese By similarity
Metal binding2941Manganese By similarity
Binding site771Substrate By similarity
Binding site2181Substrate; via amide nitrogen By similarity
Binding site2251Substrate By similarity
Binding site2671Substrate By similarity
Binding site3841GTP By similarity
Binding site4151GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3M840 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 35BAC9B5834E03C9

FASTA61167,530
        10         20         30         40         50         60 
MTTVNAPEFV RHPKLIAWVE EIANLTKPAK IEWCDGSEEE YQRLIDLMIA NGTMQKLNQE 

        70         80         90        100        110        120 
KHPGSYLANS DPSDVARVED RTYICSQNKE DAGATNNWED PAVMREKLNG LFEGSMKGRT 

       130        140        150        160        170        180 
MYVVPFSMGP LGSHIAHIGI ELTDSPYVAV SMRKMARMGK AVYDVLGTDG EFVPCVHTVG 

       190        200        210        220        230        240 
TPLAEGQKDV AWPCNPEKYI VHYPETREIW SFGSGYGGNA LLGKKCLALR IASVMGREQG 

       250        260        270        280        290        300 
WLAEHMLILG VTNPQGEKHY IAAAFPSACG KTNFAMLIPP AGYEGWKIET VGDDIAWIKP 

       310        320        330        340        350        360 
GEDGRLYAIN PEAGFFGVAP GTNTKTNPNC MATLHKDVIY TNVAVTDDGQ VWWEGLSKEV 

       370        380        390        400        410        420 
PANLTNWKGQ PHVNGEKAAH PNARFTVAAG QCPSIDADWE NPAGVPISAF IFGGRRADTV 

       430        440        450        460        470        480 
PLVSEAFDWV DGVYKAATMG SETTAAAVGQ QGIVRRDPFA MLPFAGYNMA DYFDHWLNLG 

       490        500        510        520        530        540 
AKVSEKAEAS GNKLPKIFNV NWFRRDAEGN FVWPGFGQNM RVLEWIIDRC EGRANAVETP 

       550        560        570        580        590        600 
IGFVPTYEDL NWEGTEFTKE QFDLITNQDK DQWVTEIESH TELFNKLGER LPKALKERQA 

       610 
ALLEAVKLAS N

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References

[1]"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17978 / NCDC KC 755.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000521 Genomic DNA. Translation: ABO13084.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING400667.A1S_2668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC20721647. VBIAciBau103176_2718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1274.
HOGENOMHOG000191700.
ProtClustDBPRK04210.

Enzyme and pathway databases

BioCycABAU400667:GI0Q-2675-MONOMER.
UniPathwayUPA00138.

Family and domain databases

Gene3D3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPMF_00452. PEPCK_GTP.
InterProIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PANTHERPTHR11561. PTHR11561. 1 hit.
PfamPF00821. PEPCK. 1 hit.
[Graphical view]
PIRSFPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMSSF68923. PEP_carboxykinase_N. 1 hit.
PROSITEPS00505. PEPCK_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCKG_ACIBT
AccessionPrimary (citable) accession number: A3M840
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: May 1, 2013
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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