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Q47A08 (PGK_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:Daro_3594
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length393 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_processglycolysis

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 – 393393Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000057980

Regions

Nucleotide binding347 – 3504ATP By similarity
Region21 – 233Substrate binding By similarity
Region60 – 634Substrate binding By similarity

Sites

Binding site371Substrate By similarity
Binding site1151Substrate By similarity
Binding site1481Substrate By similarity
Binding site1991ATP By similarity
Binding site3211ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47A08 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 5EFB11B17A7DB77B

FASTA39341,599
        10         20         30         40         50         60 
MNVIKLTDLD VSGKRVFIRA DLNVPQDEAG NITEDTRIRA SLPSIKYCLE KGAAVMVTSH 

        70         80         90        100        110        120 
LGRPTEGELN HEDSLMPVAV RLGQMLHTSV RLITDWVDGG FEVKPGEVVL LENCRVNKGE 

       130        140        150        160        170        180 
KKNNDELAQK MAKLCDIYVN DAFGTAHRAE ATTHGIAKYA PVACAGMLMG AEIDALSKAL 

       190        200        210        220        230        240 
HEPKRPLVAI VGGSKVSSKL TILKSLASKV DQLIVGGGIA NTFLLADGKR IGHSLAEPDL 

       250        260        270        280        290        300 
VKEAHTIMDI MKERGAEVPL PTDVVVADEV SALARANKIS VDDVHANDRI LDVGPKTAAK 

       310        320        330        340        350        360 
FAEIIANAGT IVWNGPVGVF ELPQFAGGTK MMASAIAHSE AFSIAGGGDT LAAIAKFHIA 

       370        380        390 
DDVGYISTGG GAFLEFLEGK TLPAIAILEE RAA 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ48323.1.
RefSeqYP_286793.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47A08.
SMRQ47A08. Positions 2-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_3594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ48323; AAZ48323; Daro_3594.
GeneID3568258.
KEGGdar:Daro_3594.
PATRIC21605868. VBIDecAro89105_3576.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMADMIFDIG.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycDARO159087:GI5B-3670-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_DECAR
AccessionPrimary (citable) accession number: Q47A08
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 58 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