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Q3SMD2 (PGK_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:Tbd_0161
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

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_1000058087

Regions

Nucleotide binding346 – 3494ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1141Substrate By similarity
Binding site1471Substrate By similarity
Binding site1981ATP By similarity
Binding site3201ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SMD2 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: FBEE52D9B10061AE

FASTA39341,556
        10         20         30         40         50         60 
MAFIRVTDLD LAGKRVFIRA DMNVPVKDGK VTSDARITAS MRTIEHCMRA GAKVMVTSHL 

        70         80         90        100        110        120 
GRPTEGEFKE EDSLKPVVDV IAQKLGKNVR LIREWTEGGF DVANGELVVL ENCRVNKGEK 

       130        140        150        160        170        180 
KNVDETAKKY AALCDVFVMD AFGTAHRAEA STHGIAKFAP TAAAGILLTE ELDALAKALA 

       190        200        210        220        230        240 
NPARPMVAIV GGSKVSTKLT VLEALSEKVD QLVVGGGIAN TFLAAMGKNV GKSLCEHDLI 

       250        260        270        280        290        300 
PTAKTLIEKM AARGASIPIA VDVVCGKKFD ANEPAVLKSA DEVADDDMIF DIGPKSAQEL 

       310        320        330        340        350        360 
ADIIAKAGTI VWNGPVGVFE FDQFGEGTKT VSMAIANAPG FSLAGGGDTI AAIQKYDIYD 

       370        380        390 
KVSYISTAGG AFLEYLEGKV LPAVAILEER AQG 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ96114.1.
RefSeqYP_313919.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SMD2.
SMRQ3SMD2. Positions 2-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_0161.

Proteomic databases

PRIDEQ3SMD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ96114; AAZ96114; Tbd_0161.
GeneID3673607.
KEGGtbd:Tbd_0161.
PATRIC23966467. VBIThiDen82923_0165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycTDEN292415:GHWG-164-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_THIDA
AccessionPrimary (citable) accession number: Q3SMD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 11, 2005
Last modified: February 19, 2014
This is version 57 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