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Q65EM9 (PGK_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:BLi03664, BL03465
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

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
   PTMPhosphoprotein
   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 – 394394Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000057966

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 site2011ATP By similarity
Binding site3231ATP By similarity

Amino acid modifications

Modified residue1831Phosphoserine By similarity
Modified residue2991Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65EM9 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 8E7C195741A960EC

FASTA39442,382
        10         20         30         40         50         60 
MNKKSVKDID VKGRVVFCRV DFNVPMKDGK VTDDTRIRAA LPTIQYLTEQ GAKVLLASHL 

        70         80         90        100        110        120 
GRPKGQVSEE LRLTPVAARL GELIGKEVKK ADEAYGDAVK AQISEMKDGD ILVLENVRFY 

       130        140        150        160        170        180 
PGEEKNDPEL SKAFADLADV YVNDAFGAAH RAHASTAGIA EHLPAVAGFL MEKELEVLGK 

       190        200        210        220        230        240 
ALSNPERPFT AIIGGAKVKD KIGVIESLLE KVDNLIIGGG LAYTFVKALG HEVGKSLLEE 

       250        260        270        280        290        300 
DKIELAKSFM DRAKEKGVNF YMPTDVLVAD DFSNDANTKI VPVSEIPSDW EALDIGEETR 

       310        320        330        340        350        360 
KTYADVIKNS KLVVWNGPMG VFEIDAFAKG TRAVAEALAE ANDTYSVIGG GDSAAAVEKF 

       370        380        390 
GLADKMSHIS TGGGASLEFM EGKELPGVKA LNDK 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU25114.1.
AE017333 Genomic DNA. Translation: AAU42485.1.
RefSeqYP_006714948.1. NC_006322.1.
YP_080752.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65EM9.
SMRQ65EM9. Positions 1-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL03465.

Proteomic databases

PRIDEQ65EM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU25114; AAU25114; BL03465.
AAU42485; AAU42485; BLi03664.
GeneID3029334.
3100633.
KEGGbld:BLi03664.
bli:BL03465.
PATRIC18953114. VBIBacLic203714_3733.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAFGLADKM.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-3623-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_BACLD
AccessionPrimary (citable) accession number: Q65EM9
Secondary accession number(s): Q62Q46
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 25, 2004
Last modified: February 19, 2014
This is version 71 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