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B2GAL8 (PGK_LACF3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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:LAF_0364
OrganismLactobacillus fermentum (strain NBRC 3956 / LMG 18251) [Complete proteome] [HAMAP]
Taxonomic identifier334390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length401 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_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 – 401401Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096351

Regions

Nucleotide binding357 – 3604ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1191Substrate By similarity
Binding site1601Substrate By similarity
Binding site2121ATP By similarity
Binding site3301ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2GAL8 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 32F5CEDA69A1C640

FASTA40142,697
        10         20         30         40         50         60 
MAKLTVEDLD LAGKKVLMRV DFNVPIKDGV VGDDNRIVAA LPTIKYVLDH QGKAILFSHL 

        70         80         90        100        110        120 
GRIKKEDDKP GLSMRPVAER LSNLLNMPVT FVPVTEGPQL EDAIAKMEDG QVLVVQNTRY 

       130        140        150        160        170        180 
EDVKDGEYVK RESGNDPELG KYWASLGDLF INDAFGTAHR KHASNVGIAS NMPGKAAAGF 

       190        200        210        220        230        240 
LMEKEIKFLG DAVTNPVRPF VAILGGAKVS DKIGVINNLL DKADKVIVGG GMTYTFYAAK 

       250        260        270        280        290        300 
GIKIGNSLVE EDKIDVAKEI LEKAGDKLVL PVDNVVADKF ANDANTKVVE GDIDDGWMAL 

       310        320        330        340        350        360 
DIGPKSIEEF KKVLADAKTV VWNGPMGVFE MSNFAKGTLE VGQFLGTLEG ATTIVGGGDS 

       370        380        390        400 
TAAAKQLGIS DKLTHISTGG GASLAYLEGD VLPGIAAISD K 

« Hide

References

[1]"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 3956 / LMG 18251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008937 Genomic DNA. Translation: BAG26700.1.
RefSeqYP_001843180.1. NC_010610.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334390.LAF_0364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG26700; BAG26700; LAF_0364.
GeneID6232415.
KEGGlfe:LAF_0364.
PATRIC22224772. VBILacFer15497_0397.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAFGLADKM.
OrthoDBEOG64N9Z0.
ProtClustDBCLSK2337251.

Enzyme and pathway databases

BioCycLFER334390:GJ2S-386-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_LACF3
AccessionPrimary (citable) accession number: B2GAL8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 35 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