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Reviewed, UniProtKB/Swiss-Prot Q74L45 (GPMA2_LACJO)

Last modified February 9, 2010. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2
      Short name=Phosphoglyceromutase 2
      Short name=PGAM 2
      Short name=BPG-dependent PGAM 2
      Short name=dPGM 2
    EC=5.4.2.1
Gene names
Name: gpmA2
Ordered Locus Names: LJ_0380
OrganismLactobacillus johnsonii [Complete proteome] [HAMAP]
Taxonomic identifier33959 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

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. HAMAP MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01039

Pathway

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

Sequence similarities

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

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: HAMAP

   Molecular function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2292292,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 HAMAP MF_01039
PRO_0000179884

Sites

Active site131Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Site651Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q74L45-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 11E2135674109A56

FASTA22926,212
        10         20         30         40         50         60 
MKRKLAKLVL VRHGESVANR DNVYTGWNDV PLSKKGIAQA KNAGLKVEKI AEFAPTHIHT 

        70         80         90        100        110        120 
SVLSRAIMTA NIIADVCSFL YLPITKTWRL NERHYGALRG INKDVSKKIF GTNQVLEWRR 

       130        140        150        160        170        180 
GFDSVPPLLT QPVQDRRYQK YDMRLMPQGE SLHQTQERLM PYFWDHIAPE LMAGHDQLVV 

       190        200        210        220 
AHGSSLRALI KKIEDISNED IVKVEVPNAE PIVYTFDTDL HIVKKEILH 

« Hide

References

[1]"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533."
Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.
Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed: 14983040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 533.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017198 Genomic DNA. Translation: AAS08370.1.
RefSeqNP_964404.1.

3D structure databases

SMRQ74L45. Positions 6-228.
ModBaseSearch...

Genome annotation databases

GeneID2741990.
GenomeReviewsGene locus LJ_0380 in contig AE017198_GR.
KEGGljo:LJ0380.
NMPDRfig|257314.1.peg.390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658938.
OMAYTGWSDV.

Enzyme and pathway databases

BioCycLJOH257314:LJ_0380-MONOMER.
BRENDA5.4.2.1. 141476.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
[Tree]
InterProIPR001345. PG/BPGM_mutase_AS.
IPR013078. PG_mutase.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. Phosphogly_mut1. 1 hit.
PfamPF00300. PGAM. 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 nameGPMA2_LACJO
AccessionPrimary (citable) accession number: Q74L45
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 5, 2004
Last modified: February 9, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents