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B1VDQ4 (PGK_CORU7) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 40. 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:cu0992
OrganismCorynebacterium urealyticum (strain ATCC 43042 / DSM 7109) [Complete proteome] [HAMAP]
Taxonomic identifier504474 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length402 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 – 402402Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096335

Regions

Nucleotide binding359 – 3624ATP By similarity
Region24 – 263Substrate binding By similarity
Region62 – 654Substrate binding By similarity

Sites

Binding site391Substrate By similarity
Binding site1211Substrate By similarity
Binding site1611Substrate By similarity
Binding site2111ATP By similarity
Binding site2991ATP; via carbonyl oxygen By similarity
Binding site3301ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1VDQ4 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: ED5475AF21023709

FASTA40241,721
        10         20         30         40         50         60 
MAVKTLKDLL AEGVEGRHVL VRSDLNVPLA DGEITDPGRI DASIPTLRAL LDEGARVIVA 

        70         80         90        100        110        120 
AHLGRPKGEV DPELSLAPVA EALAERLDQW VPLAGDVTGE DAHERANGLD DGDILLLENV 

       130        140        150        160        170        180 
RFDPRETSKD ASERAEFAAE LAELTADNGA FVSDGFGVVH REQASVYDVA KKLPSYAGGL 

       190        200        210        220        230        240 
VSAELEVLEK VSGAPEAPYA VVLGGSKVSD KLGVIEALAP KVDRLIIGGG MCFTFLAAQG 

       250        260        270        280        290        300 
HDVGGSLLQE DMIDTCKDLL ERYGDVIVLP TDVVAAENFS KDAEHKAVGL SEIPSGWMGL 

       310        320        330        340        350        360 
DIGPESADAF AAVLGEAKTV FWNGPMGVFE FPAFAAGTKA VAEAIIKATD AGAFSVVGGG 

       370        380        390        400 
DSAAAVRTLG LDEKGFSHIS TGGGASLEFL EGKTLPGVEV LG 

« Hide

References

[1]"The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing."
Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., Puehler A.
J. Biotechnol. 136:11-21(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43042 / DSM 7109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942444 Genomic DNA. Translation: CAQ04952.1.
RefSeqYP_001800386.1. NC_010545.1.

3D structure databases

ProteinModelPortalB1VDQ4.
SMRB1VDQ4. Positions 3-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING504474.cur_0992.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ04952; CAQ04952; cu0992.
GeneID6186331.
KEGGcur:cur_0992.
PATRIC21521720. VBICorUre58120_0989.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycCURE504474:GJ8Y-1015-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_CORU7
AccessionPrimary (citable) accession number: B1VDQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 40 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