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Reviewed, UniProtKB/Swiss-Prot Q88T35 (GPMA2_LACPL)

Last modified November 3, 2009. Version 34. 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
Synonyms: pmg9
Ordered Locus Names: lp_3170
OrganismLactobacillus plantarum [Complete proteome] [HAMAP]
Taxonomic identifier1590 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity.

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 – 2302302,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 HAMAP MF_01039
PRO_0000179887

Sites

Active site91Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Site601Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88T35-1 [UniParc].

Last modified June 1, 2003. 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

Cross-references

Sequence databases

AL935261 Genomic DNA. Translation: CAD65323.1.
RefSeqNP_786452.1.

3D structure databases

HSSPHSSP built from PDB template 1E58 based on UniProtKB P31217.
ModBaseSearch...

Genome annotation databases

GeneID1063992.
GenomeReviewsGene locus lp_3170 in contig AL935263_GR.
KEGGlpl:lp_3170.
NMPDRfig|220668.1.peg.2586.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ88T35.
OMAFMLWRRS.

Enzyme and pathway databases

BioCycLPLA220668:LP_3170-MON.
BRENDA5.4.2.1. 593.

Family and domain databases

HAMAPMF_01039.
[Tree]
InterProIPR001345. PG/BPGM_mutase_AC.
IPR013078. PG_mutase.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. Phosphogly_mut1. 1 hit.
PfamPF00300. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPMA2_LACPL
AccessionPrimary (citable) accession number: Q88T35
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 34 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