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B1YLE1 (PGK_EXIS2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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:Exig_2396
OrganismExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15) [Complete proteome] [HAMAP]
Taxonomic identifier262543 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length394 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 – 394394Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096342

Regions

Nucleotide binding350 – 3534ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1181Substrate By similarity
Binding site1511Substrate By similarity
Binding site2021ATP By similarity
Binding site3241ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YLE1 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: C25D718F669E2A0D

FASTA39442,103
        10         20         30         40         50         60 
MNKKSIRDID VKGKRVFTRV DFNVPLEDGK ITDDTRIRAA LPTIKHLVDG GAKVILASHM 

        70         80         90        100        110        120 
GRPKGEKNPE FSLAPVVARL SELLGKDIKL VEEAYGPVAE EAVSKLEEGD VIVLENVRFY 

       130        140        150        160        170        180 
PGETKNDPEL AEGFAKLADV FVNDAFGAAH RAHASTEGIA HHVETAVAGL LIEKELQVLG 

       190        200        210        220        230        240 
KALSNPDRPF TAIIGGSKVA DKIGVIDHLL DIVDTLIIGG GLSYTFLKAQ GYEVGTSLLE 

       250        260        270        280        290        300 
VDKIEQAKEF MKKAEDKGVK FLMPVDCVIT KEFGEETYVG SRDIDSIPAD HMSLDIGPKT 

       310        320        330        340        350        360 
VELYAEAIKA SKLVVWNGPM GVFELDKYAN GTKGVAQALA DSDAYSIIGG GDSAAAAEKF 

       370        380        390 
GLADKMSHIS TGGGASLEFM EGKALPGVEA LNDK 

« Hide

References

[1]"Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17290 / JCM 13490 / 255-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001022 Genomic DNA. Translation: ACB61846.1.
RefSeqYP_001814863.1. NC_010556.1.

3D structure databases

ProteinModelPortalB1YLE1.
SMRB1YLE1. Positions 1-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262543.Exig_2396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB61846; ACB61846; Exig_2396.
GeneID6173109.
KEGGesi:Exig_2396.
PATRIC32138424. VBIExiSib53410_2434.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAWEALDIG.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycESIB262543:GHBP-2477-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.
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.
ProtoNetSearch...

Entry information

Entry namePGK_EXIS2
AccessionPrimary (citable) accession number: B1YLE1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 37 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