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Q2II25 (PGK_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase

EC=2.7.2.3
Gene names
Name:pgk
Ordered Locus Names:Adeh_1531
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP-Rule MF_00145

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP-Rule MF_00145

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00145

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000057957

Regions

Nucleotide binding353 – 3564ATP By similarity
Region21 – 233Substrate binding By similarity
Region60 – 634Substrate binding By similarity

Sites

Binding site371Substrate By similarity
Binding site1211Substrate By similarity
Binding site1541Substrate By similarity
Binding site2051ATP By similarity
Binding site2961ATP; via carbonyl oxygen By similarity
Binding site3271ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2II25 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 24E3DBC7842AF1D3

FASTA39642,409
        10         20         30         40         50         60 
MALRTIDALD LAGKRVFIRV DFNVPLDPQG KVTDDARIRA ALPTIRHAIQ AKAKVILASH 

        70         80         90        100        110        120 
LGRPKGKPDD RTKLTLEPAA VRLSELLSQD VILADDCVGD GVKKLVRDLK DGHVLLLENL 

       130        140        150        160        170        180 
RFHPEEEKND EAFARELASL ADVWVNDAFG TAHRAHASTA GMAKFVKEKA AGFLVQKEVE 

       190        200        210        220        230        240 
YLGKALGSPA RPFVAIVGGA KVSDKIKVLE NLIAKADAVC VGGAMAYTFL KAQGVPVGRS 

       250        260        270        280        290        300 
LVEEDKLELA RQILERAEAR KVDLLLPVDH VCGAEPKETA ERVVVNDRAI PDGLMGLDIG 

       310        320        330        340        350        360 
PKTLDRYRQR IAGAKTVFWN GPMGLFEQKP WSEGTFGVAK AMAASPAVTV VGGGDSAAAV 

       370        380        390 
EQAGLVDKMK HVSTGGGASL EFIEGRELPG VKACEE 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC81304.1.
RefSeqYP_464741.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2II25.
SMRQ2II25. Positions 4-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290397.Adeh_1531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC81304; ABC81304; Adeh_1531.
GeneID3887941.
KEGGade:Adeh_1531.
PATRIC20919181. VBIAnaDeh31384_1580.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAMSIRYID.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycADEH290397:GI2Z-1548-MONOMER.
UniPathwayUPA00109; UER00185.

Family and domain databases

Gene3D3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPMF_00145. Phosphoglyc_kinase.
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGK_ANADE
AccessionPrimary (citable) accession number: Q2II25
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 7, 2006
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways