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Q898R3 (PGK_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:CTC_00379
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length401 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 – 401401Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000145934

Regions

Nucleotide binding357 – 3604ATP By similarity
Region26 – 283Substrate binding By similarity
Region64 – 674Substrate binding By similarity

Sites

Binding site411Substrate By similarity
Binding site1251Substrate By similarity
Binding site1581Substrate By similarity
Binding site2091ATP By similarity
Binding site3001ATP; via carbonyl oxygen By similarity
Binding site3311ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q898R3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 68BD1895E77F3C49

FASTA40143,578
        10         20         30         40         50         60 
MVYVAFNKKT IEDIDVKGRK VLVRCDFNVP LKDGKITDEN RLMGALPTIK YIMEKGGKVI 

        70         80         90        100        110        120 
LCSHLGKPKG EPKQELSLAP VAKRLSELLN KEVLFPADNE VVGENAKKAV ENMKDGDVIL 

       130        140        150        160        170        180 
LQNTRYRKEE TKNEETFSKE LASLADIFVN DAFGTAHRAH CSTVGVTEFV ATSVCGYLIQ 

       190        200        210        220        230        240 
KELKFLGNAV ENPQRPFISI LGGAKVSDKI NVINNLLEKV DTLIIGGGMS YTFQKAQGYT 

       250        260        270        280        290        300 
IGSSLLEEDK IDYAKEMIEK AKEKGVKLLL PVDNVAAEKF AEDAEAIITE DQNIKEGYMG 

       310        320        330        340        350        360 
LDIGPKTSKL YSQEVQSAKT VVWNGPMGVF EFEKFAKGTI EVAKAMAESQ ATTIIGGGDS 

       370        380        390        400 
AAAVNQLGFG DKMTHISTGG GASLEFLEGK ELPGIAALND K 

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015927 Genomic DNA. Translation: AAO35016.1.
RefSeqNP_781079.1. NC_004557.1.

3D structure databases

ProteinModelPortalQ898R3.
SMRQ898R3. Positions 8-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING212717.CTC00379.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO35016; AAO35016; CTC_00379.
GeneID1059957.
KEGGctc:CTC00379.
PATRIC19508582. VBICloTet101274_0347.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
KOK00927.
OMAFGLADKM.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycCTET212717:GJAM-336-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_CLOTE
AccessionPrimary (citable) accession number: Q898R3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 64 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