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F4AEP0 (F4AEP0_LACJH) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039

Short name=BPG-dependent PGAM HAMAP-Rule MF_01039
Short name=PGAM HAMAP-Rule MF_01039
Short name=Phosphoglyceromutase HAMAP-Rule MF_01039
Short name=dPGM HAMAP-Rule MF_01039
EC=5.4.2.11 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039
ORF Names:LJP_0351 EMBL AEB92687.1
OrganismLactobacillus johnsonii DPC 6026 [Complete proteome] EMBL AEB92687.1
Taxonomic identifier909954 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP-Rule MF_01039 RuleBase RU004512

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039 RuleBase RU004512 SAAS SAAS001345

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039 RuleBase RU004512

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Ontologies

Keywords
   Biological processGlycolysis HAMAP-Rule MF_01039 SAAS SAAS001345
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS001345
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region28 – 2922-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region95 – 9842-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region122 – 12322-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site161Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1851 By similarity HAMAP-Rule MF_01039
Binding site2212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6812-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site10612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
F4AEP0 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 10048805D1E7E53F

FASTA23226,644
        10         20         30         40         50         60 
MRRVRRKLAK LVLVRHGESI ANRDNVYTGW NDVPLSKKGI EQAKNAGLKV EKIAGFVPTH 

        70         80         90        100        110        120 
IHTSVLSRAI ITANIIADVC SFLYLPITKT WRLNERHYGA LRGINKDVSK KIFGTKQVLE 

       130        140        150        160        170        180 
WRRGFDSVPP LLTQPVQDRR YQKYDMRLMP QGESLHQTQE RLMPYFWDHI APELIAGHDQ 

       190        200        210        220        230 
LVVAHGSSLR ALIKKIEDIS NEDIVKVEVP NAEPIVYTFD TDLHIVKKEV LH 

« Hide

References

[1]"Host Specific Diversity in Lactobacillus johnsonii as Evidenced by a Major Chromosomal Inversion and Phage Resistance Mechanisms."
Guinane C.M., Kent R.M., Norberg S., Hill C., Fitzgerald G.F., Stanton C., Ross R.P.
PLoS ONE 6:E18740-E18740(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DPC 6026 EMBL AEB92687.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002464 Genomic DNA. Translation: AEB92687.1.
RefSeqYP_005861637.1. NC_017477.1.

3D structure databases

ProteinModelPortalF4AEP0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEB92687; AEB92687; LJP_0351.
GeneID12470016.
KEGGljh:LJP_0351.
PATRIC54201554. VBILacJoh171132_0375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.

Enzyme and pathway databases

BioCycLJOH909954:GLFA-358-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF4AEP0_LACJH
AccessionPrimary (citable) accession number: F4AEP0
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 11, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)