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A6WC55 (PGK_KINRD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Krad_2930
OrganismKineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) [Complete proteome] [HAMAP]
Taxonomic identifier266940 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesKineosporiineaeKineosporiaceaeKineococcus

Protein attributes

Sequence length412 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 – 412412Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000076591

Regions

Nucleotide binding369 – 3724ATP By similarity
Region24 – 263Substrate binding By similarity
Region70 – 734Substrate binding By similarity

Sites

Binding site471Substrate By similarity
Binding site1301Substrate By similarity
Binding site1671Substrate By similarity
Binding site2171ATP By similarity
Binding site3121ATP; via carbonyl oxygen By similarity
Binding site3431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6WC55 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: F351D3DB5ACE7DE2

FASTA41243,035
        10         20         30         40         50         60 
MKTLDDLETQ LGGFAGRRVL VRSDLNVPLD HDRRDGAGQP VITDDGRLRA SVPTLRRLLD 

        70         80         90        100        110        120 
AGARVVVTAH LGRPKGAPEA KYSLAPVHAR LAELLPGVEV GFCPVTVGAQ ATAAVDALAD 

       130        140        150        160        170        180 
GELLLLENIR FNAGETSKDD EEREAFADEL AALADAFVSD GFGAVHRKHA SVYDVALRLP 

       190        200        210        220        230        240 
HAAGGLVATE VEVLQRLTAH PERPYAVVLG GSKVSDKLGV IDNLLGSLLG EGDRLLVGGG 

       250        260        270        280        290        300 
MVFTFLKAQG YEVGKSLLET DQLDRVAGYV RTAREKGVEL VLPTDVVAAT AFAADAEHDV 

       310        320        330        340        350        360 
VAVDAIPADR LGLDIGPDSG AAFAARLADA RTVFWNGPMG VFEMEPYSHG TRAVAQALVD 

       370        380        390        400        410 
GGAFSVVGGG DSAAAVRTLG FADERFGHIS TGGGASLEYL EGKHLPGLDV LS 

« Hide

References

[1]"Complete sequence of chromosome of Kineococcus radiotolerans SRS30216."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J., Fliermans C., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-149 / DSM 14245 / SRS30216.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000750 Genomic DNA. Translation: ABS04394.1.
RefSeqYP_001362658.1. NC_009664.2.

3D structure databases

ProteinModelPortalA6WC55.
SMRA6WC55. Positions 1-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266940.Krad_2930.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS04394; ABS04394; Krad_2930.
GeneID5336659.
KEGGkra:Krad_2930.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMADMIFDIG.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycKRAD266940:GI4N-3870-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_KINRD
AccessionPrimary (citable) accession number: A6WC55
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 45 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