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Reviewed, UniProtKB/Swiss-Prot Q81DD2 (GPMA_BACCR)

Last modified November 3, 2009. Version 37. 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
      Short name=Phosphoglyceromutase
      Short name=PGAM
      Short name=BPG-dependent PGAM
      Short name=dPGM
    EC=5.4.2.1
Gene names
Name: gpmA
Ordered Locus Names: BC_2435
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length245 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 – 2452452,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039
PRO_0000179845

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q81DD2-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 49DAD0089DADFA12

FASTA24528,228
        10         20         30         40         50         60 
MIKLVLIRHG QSLWNLENRF TGWTDVDLSE NGLSEAREAG AILKKNGYTF DVAYTSVLKR 

        70         80         90        100        110        120 
AIRTLWIVLH EMDLTWVPIH KSWKLNERHY GALQGLNKDE TAQKYGEEQV HIWRRSVDVR 

       130        140        150        160        170        180 
PPALTEDDPR YEATDPRYKT LKKGEFPLTE CLEDTEKRVL AYWHSEIAPT LKSGNKVIIS 

       190        200        210        220        230        240 
SHGNTIRSLV KYLDNLSSDG VVSLNIPTSI PLVYELDENL RPIRHYYLSM DGEVPEGEIP 


KHISF 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE016877 Genomic DNA. Translation: AAP09398.1.
RefSeqNP_832197.1.

3D structure databases

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

Protein-protein interaction databases

STRINGQ81DD2.

Genome annotation databases

GeneID1204784.
GenomeReviewsGene locus BC_2435 in contig AE016877_GR.
KEGGbce:BC2435.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ81DD2.
OMAFMLWRRS.

Enzyme and pathway databases

BioCycBCER226900:BC_2435-MON.

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 nameGPMA_BACCR
AccessionPrimary (citable) accession number: Q81DD2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 37 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