Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q88YY8 (GPMA1_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1

Short name=BPG-dependent PGAM 1
Short name=PGAM 1
Short name=Phosphoglyceromutase 1
Short name=dPGM 1
EC=5.4.2.1
Gene names
Name:gpmA1
Synonyms:pgm2
Ordered Locus Names:lp_0597
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length225 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
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphosphoglycerate mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2252252,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1 HAMAP MF_01039
PRO_0000179886

Sites

Active site91Tele-phosphohistidine intermediate By similarity
Active site1791 By similarity
Site601Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88YY8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 209F01523D298432

FASTA22525,625
        10         20         30         40         50         60 
MTELVLVRHG ESTANRDNTY TGWSDVPLTA VGIAQAHQAG KRLRATGLQF GAVHTSVLKR 

        70         80         90        100        110        120 
AIVTANIMLS EIDQLWLPEY KTWRLNERHY GALRGQNKDV TRQEYGKAQV QQWRRSFYTV 

       130        140        150        160        170        180 
PPLLTPAELD HDRRYTKYGA AVEPRGESLK MAYDRIMPYW IDEIAPRLLD GQNQLVVAHG 

       190        200        210        220 
STLRAMIKYL EHISDTGIDG VEVANGVPIC YHLDRQLHVI GKEEY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL935263 Genomic DNA. Translation: CCC78081.1.
RefSeqNP_784369.1. NC_004567.1.

3D structure databases

ProteinModelPortalQ88YY8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1061573.
GenomeReviewsGene locus lp_0597 in contig AL935263_GR.
KEGGlpl:lp_0597.
NMPDRfig|220668.1.peg.503.
PATRIC22247647. VBILacPla27411_0500.

Phylogenomic databases

HOGENOMHBG658938.
OMAESTANRD.
ProtClustDBCLSK581144.

Enzyme and pathway databases

BioCycLPLA220668:LP_0597-MONOMER.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
[Tree]
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
KOK01834.
PANTHERPTHR11931. Phosphogly_mut1. 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 nameGPMA1_LACPL
AccessionPrimary (citable) accession number: Q88YY8
Secondary accession number(s): F9UL66
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families