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Reviewed, UniProtKB/Swiss-Prot A0JSU9 (GPMA_ARTS2)

Last modified November 3, 2009. Version 21. 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: Arth_0721
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length248 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 – 2482482,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039
PRO_1000064027

Sites

Active site101Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Site611Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JSU9-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 80E2659F5E8C36FA

FASTA24827,832
        10         20         30         40         50         60 
MTYKLILLRH GHSEWNAKNL FTGWVDVDLN DQGREEAARG GELLVENNVL PDVLYTSLLK 

        70         80         90        100        110        120 
RAINTANIAL DKADRGWIPV KRDWRLNERH YGALQGKDKA QTLAEYGEEQ FMEWRRSYDT 

       130        140        150        160        170        180 
PPPPLDDDSE FSQAHDPRYA DLGDALPRTE CLKDVLIRLM PYWESDIKED LKAGKTVLVT 

       190        200        210        220        230        240 
AHGNSLRALV KHLDGISDEA IAGLNIPTGI PLVYDLDENF KPLNPGGTYL DPEAAAESIK 


AVANQGKK 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000454 Genomic DNA. Translation: ABK02119.1.
RefSeqYP_830219.1.

3D structure databases

SMRA0JSU9. Positions 2-236.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0JSU9.

Genome annotation databases

GeneID4446789.
GenomeReviewsGene locus Arth_0721 in contig CP000454_GR.
KEGGart:Arth_0721.
TIGRArth_0721.

Phylogenomic databases

OMAFMLWRRS.

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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPMA_ARTS2
AccessionPrimary (citable) accession number: A0JSU9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 21 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