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

C7TEJ0 (C7TEJ0_LACRG) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 39. 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 CAR88033.1
Ordered Locus Names:LGG_02138 EMBL CAR88033.1, LRHM_2055 EMBL BAI42582.1
OrganismLactobacillus rhamnosus (strain ATCC 53103 / GG) [Complete proteome] [HAMAP]
Taxonomic identifier568703 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

Sequence similarities

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

Ontologies

Keywords
   Biological processGlycolysis SAAS SAAS001345 HAMAP-Rule MF_01039
   Molecular functionIsomerase SAAS SAAS001345 HAMAP-Rule MF_01039
   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

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
C7TEJ0 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 3E36188BACE898CD

FASTA22925,954
        10         20         30         40         50         60 
MAKLVLIRHG QSEWNLSNQF TGWVDVDLSE KGVEEAKHAG ELIKQAGLEF DQAYTSVLTR 

        70         80         90        100        110        120 
AIKTLHYVLE ESGQLWIPEM KTWRLNERHY GALQGLNKKE TADKYGADQV HIWRRSYDVL 

       130        140        150        160        170        180 
PPLLKATDEG SAAKDRRYAD LDPRIIPGGE NLKVTLERVI PFWEDHIAPD LLDGKNVVIA 

       190        200        210        220 
AHGNSLRALT KYIENISDAD IMNLEMATGE PVVYDFDEKL NVNSKTKLD 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the probiotic Lactobacillus rhamnosus ATCC 53103."
Morita H., Toh H., Oshima K., Murakami M., Taylor T.D., Igimi S., Hattori M.
J. Bacteriol. 191:7630-7631(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53103 EMBL BAI42582.1 and ATCC 53103 / GG [Tokyo].
[2]"Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human- mucus binding protein."
Kankainen M., Paulin L., Tynkkynen S., von Ossowski I., Reunanen J., Partanen P., Satokari R., Vesterlund S., Hendrickx A.P., Lebeer S., De Keersmaecker S.C., Vanderleyden J., Hamalainen T., Laukkanen S., Salovuori N., Ritari J., Alatalo E., Korpela R. expand/collapse author list , Mattila-Sandholm T., Lassig A., Hatakka K., Kinnunen K.T., Karjalainen H., Saxelin M., Laakso K., Surakka A., Palva A., Salusjarvi T., Auvinen P., de Vos W.M.
Proc. Natl. Acad. Sci. U.S.A. 106:17193-17198(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53103 / GG [Helsinki].
[3]"Genomic Adaptation of the Lactobacillus casei Group."
Toh H., Oshima K., Nakano A., Takahata M., Murakami M., Takaki T., Nishiyama H., Igimi S., Hattori M., Morita H.
PLoS ONE 8:e75073-e75073(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 53103 EMBL BAI42582.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP011548 Genomic DNA. Translation: BAI42582.1.
FM179322 Genomic DNA. Translation: CAR88033.1.
RefSeqYP_003171884.1. NC_013198.1.
YP_005866547.1. NC_017482.1.

3D structure databases

ProteinModelPortalC7TEJ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING568703.LGG_02138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI42582; BAI42582; LRHM_2055.
CAR88033; CAR88033; LGG_02138.
GeneID12475185.
8421408.
KEGGlrg:LRHM_2055.
lrh:LGG_02138.
PATRIC22265526. VBILacRha2892_2031.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAKDDERFP.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycLRHA568703:GCGS-2110-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 nameC7TEJ0_LACRG
AccessionPrimary (citable) accession number: C7TEJ0
Secondary accession number(s): C8UW28
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: June 11, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)