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

Q12QA3 (PGK_SHEDO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:Sden_1085
OrganismShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [Complete proteome] [HAMAP]
Taxonomic identifier318161 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length391 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 – 391391Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000058056

Regions

Nucleotide binding345 – 3484ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1131Substrate By similarity
Binding site1461Substrate By similarity
Binding site1971ATP By similarity
Binding site3191ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12QA3 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 00882533CF33123E

FASTA39140,966
        10         20         30         40         50         60 
MAIINMTDLD LTNKRVLIRQ DLNVPVSDGM VTSDARLRAS LPTIQLALDK GAAVMVMSHL 

        70         80         90        100        110        120 
GRPTEGEFNN EFSLQPVVDY LAKALKSPVR LATDYLDGVE ANVGEVVVFE NVRFNQGEGK 

       130        140        150        160        170        180 
NDEALSKKMA ALCDVYVMDA FGTAHRAQAS THGVGMFAPI ACAGPLLAQE LDALGKALDN 

       190        200        210        220        230        240 
PARPMVAIVG GSKVSTKLTV LESLSGIVDQ LVVGGGIANT FIAAAGFNVG KSLYEADLVD 

       250        260        270        280        290        300 
EAKRLVANAR SRGGDIPVPT DVVVASEFSP TAAAKLVDVS QVSDTDMIFD IGPDSAEALA 

       310        320        330        340        350        360 
KIIETAGTIV WNGPVGVFEF DQFGKGTERI ARAIADSKAF SIAGGGDTLA AVDKYNIADK 

       370        380        390 
VSYISTGGGA FLEFLEGKEL PAVAMLEKRG A 

« Hide

References

[1]"Complete sequence of Shewanella denitrificans OS217."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS217 / ATCC BAA-1090 / DSM 15013.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000302 Genomic DNA. Translation: ABE54373.1.
RefSeqYP_562096.1. NC_007954.1.

3D structure databases

ProteinModelPortalQ12QA3.
SMRQ12QA3. Positions 2-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318161.Sden_1085.

Proteomic databases

PRIDEQ12QA3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE54373; ABE54373; Sden_1085.
GeneID4017368.
KEGGsdn:Sden_1085.
PATRIC23487910. VBISheDen79529_1153.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycSDEN318161:GHKQ-1120-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_SHEDO
AccessionPrimary (citable) accession number: Q12QA3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 22, 2006
Last modified: June 11, 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