Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A9WT63 (PGK_RENSM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 44. 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:RSal33209_2270
OrganismRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP]
Taxonomic identifier288705 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeRenibacterium

Protein attributes

Sequence length417 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 – 417417Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000076600

Regions

Nucleotide binding373 – 3764ATP By similarity
Region24 – 263Substrate binding By similarity
Region67 – 704Substrate binding By similarity

Sites

Binding site441Substrate By similarity
Binding site1261Substrate By similarity
Binding site1701Substrate By similarity
Binding site2201ATP By similarity
Binding site3161ATP; via carbonyl oxygen By similarity
Binding site3471ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9WT63 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: D2057C164948CC3B

FASTA41743,040
        10         20         30         40         50         60 
MTLHTLDELL ADGVQGRYVL VRSDLNVPLS GAEDTNLTVT DDGRIRASLP VIEKLAAAGA 

        70         80         90        100        110        120 
RVLVLAHLGR PKGAPEAKYS LRPAADRLAE LASVPVSLAA DTSGESAQKA AAELADGQVL 

       130        140        150        160        170        180 
VLENVRFDPR ETSKDDAERA AFAAELAELA ASGADKEAAY VDDAFGAVHR KHASVFDLAL 

       190        200        210        220        230        240 
KLPSFHGDLV RTELDVLRKL TDSPERPYVV VLGGSKVSDK LAVIENLIGK ADSILVGGGM 

       250        260        270        280        290        300 
LFTFLAAQGH EVGASLLESD QIDTVKDYLA RAEAAGTSFV LPTDVVVASK FAADAAHELV 

       310        320        330        340        350        360 
AAQAIESSSF GAAGIGLDIG PETSQAFAEQ ISAAKTVFWN GPMGVFEFAA FASGTRAVAQ 

       370        380        390        400        410 
ALADSAAFSV VGGGDSAAAV RTLGFADNAF GHISTGGGAS LEFLEGKELP GLTALDR 

« Hide

References

[1]"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
J. Bacteriol. 190:6970-6982(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000910 Genomic DNA. Translation: ABY24001.1.
RefSeqYP_001625415.1. NC_010168.1.

3D structure databases

ProteinModelPortalA9WT63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288705.RSal33209_2270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY24001; ABY24001; RSal33209_2270.
GeneID5823871.
KEGGrsa:RSal33209_2270.
PATRIC23077901. VBIRenSal21953_2365.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAHASVYDI.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycRSAL288705:GHX1-2270-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_RENSM
AccessionPrimary (citable) accession number: A9WT63
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: June 11, 2014
This is version 44 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