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E1TRV0 (E1TRV0_LACPS) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 23. 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 EMBL ADN99819.1
Ordered Locus Names:LPST_C2606 EMBL ADN99819.1
OrganismLactobacillus plantarum (strain ST-III) [Complete proteome] [HAMAP] EMBL ADN99819.1
Taxonomic identifier889932 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length230 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_processglycolysis

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

Region21 – 2222-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region87 – 9042-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region114 – 11522-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Binding site1512-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9812-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
E1TRV0 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 48F3904EEB2E142D

FASTA23026,087
        10         20         30         40         50         60 
MAKLVLIRHG QSEWNLSNQF TGWVDVDLSE KGVEEAKAAG QKVKEAGLEF DYAFTSVLTR 

        70         80         90        100        110        120 
AIKTLHYVLE ESDQLWIPET KTWRLNERHY GALQGLNKKE TAEKYGDDQV HIWRRSYDVL 

       130        140        150        160        170        180 
PPLLSADDEG SAVNDRRYAD LDPNIVPGGE NLKVTLERVM PFWEDQIAPK LLDGKNVIIA 

       190        200        210        220        230 
AHGNSLRALS KYIEQISDDD IMDLEMATGE PVVYDFDEKL KVLGKEKLGK 

« Hide

References

[1]"Complete genome sequence of probiotic Lactobacillus plantarum ST-III."
Wang Y., Chen C., Ai L., Zhou F., Zhou Z., Wang L., Zhang H., Guo B., Chen W.
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ST-III.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002222 Genomic DNA. Translation: ADN99819.1.
RefSeqYP_003925913.1. NC_014554.1.

3D structure databases

ProteinModelPortalE1TRV0.
SMRE1TRV0. Positions 1-229.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEE1TRV0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADN99819; ADN99819; LPST_C2606.
GeneID9784536.
KEGGlps:LPST_C2606.
PATRIC42502315. VBILacPla173910_2659.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.

Enzyme and pathway databases

BioCycLPLA889932:GHWQ-2720-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
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]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE1TRV0_LACPS
AccessionPrimary (citable) accession number: E1TRV0
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: February 19, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)