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Q08262 (PCKG_CHLLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 69. 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
Synonyms:pckA
OrganismChlorobium limicola
Taxonomic identifier1092 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Chlorobium

Protein attributes

Sequence length618 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 MF_00452

Catalytic activity

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

Cofactor

Binds 1 manganese ion per subunit By similarity. HAMAP MF_00452

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00452

Subunit structure

Monomer By similarity. HAMAP MF_00452

Subcellular location

Cytoplasm By similarity HAMAP MF_00452.

Sequence similarities

Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.

Sequence caution

The sequence AAB25776.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentCytoplasm
   LigandGTP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionDecarboxylase
Lyase
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoenolpyruvate carboxykinase (GTP) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 618618Phosphoenolpyruvate carboxykinase [GTP] HAMAP MF_00452
PRO_0000103595

Regions

Nucleotide binding270 – 2756GTP By similarity
Nucleotide binding510 – 5134GTP By similarity
Region386 – 3883Substrate binding By similarity

Sites

Active site2711 By similarity
Metal binding2271Manganese By similarity
Metal binding2471Manganese By similarity
Metal binding2961Manganese By similarity
Binding site791Substrate By similarity
Binding site2201Substrate; via amide nitrogen By similarity
Binding site2271Substrate By similarity
Binding site2691Substrate By similarity
Binding site3881GTP By similarity
Binding site4191GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08262 [UniParc].

Last modified November 25, 2002. Version 2.
Checksum: 274A1FA8D0612C29

FASTA61869,531
        10         20         30         40         50         60 
MEPIPINAPD YVKNLKLLQW VKETVALCQP DSVCWCDGST EEYDRLCEEM VNSGTFIKLS 

        70         80         90        100        110        120 
EQKRPNSYLC RSDPSDVARV EDRTFICSIR RQDAGPTNNW VAPKEMKATL NKLFTGCMKG 

       130        140        150        160        170        180 
RTMYVIPFSM GPLGSHIAHI GVEITDSPYV VTNMRIMTRM GRQVLELLDE EAEFVPCLHS 

       190        200        210        220        230        240 
VGAPLEPGQA DVPWPCNDTK YIVHFPEEHA IVSYSSGYNG NTLLGKKCFA LRIASSMARD 

       250        260        270        280        290        300 
EGWLAEHMLI LGVESPAGEK DYVAAAFPSA CGKTNFAMII PPGEMEGWKI TTVGDDIRLD 

       310        320        330        340        350        360 
QQGKDGRLHA INPEYGFFGV APGTSDKSNP NAMATLHANC IFTNVALTPD GDVWWEDMTD 

       370        380        390        400        410        420 
TPPEYLIDWQ GKPWVPGCDR PAAHPNSRFT APASQCPVID PAWENPRVLP ISAFIFAGRR 

       430        440        450        460        470        480 
GDTIPLVYQS SNWYYGVYMA ATMGSEKTAA AARSATCVDP FAMLPFCGYH MGDYFNHWLH 

       490        500        510        520        530        540 
VGRTVSDPPR IFIVNWFRKT RTGKFLWPGF GDNMRVLKWM MGRVHGRSGA VESPLGWMPR 

       550        560        570        580        590        600 
YESLDWRGLD GFTSNKFSKL MSVDREGKQE LFSHEELLEK LYDRLPKEFT HIRELLLSTL 

       610 
WMSPEHWELA PELYSAES

« Hide

References

[1]"The atp2 operon of the green bacterium Chlorobium limicola."
Xie D.L., Lill H., Hauska G., Maeda M., Futai M., Nelson N.
Biochim. Biophys. Acta 1172:267-273(1993) [PubMed: 8448205] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S56812 Genomic DNA. Translation: AAB25776.1. Different initiation.

3D structure databases

ProteinModelPortalQ08262.
SMRQ08262. Positions 11-599.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00452. PEPCK_GTP.
[Tree]
InterProIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
Gene3DG3DSA:3.90.228.20. PEP_carboxykinase_C. 2 hits.
G3DSA:3.40.449.10. PEP_carboxykinase_N. 1 hit.
PANTHERPTHR11561. PEP_carboxykin. 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_CHLLI
AccessionPrimary (citable) accession number: Q08262
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 25, 2002
Last modified: May 31, 2011
This is version 69 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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