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Q7UFG7 (GPMI_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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-independent phosphoglycerate mutase

Short name=BPG-independent PGAM
Short name=Phosphoglyceromutase
Short name=iPGM
EC=5.4.2.12
Gene names
Name:gpmI
Synonyms:pgm
Ordered Locus Names:RB8562
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP-Rule MF_01038

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01038

Cofactor

Binds 2 manganese ions per subunit By similarity. HAMAP-Rule MF_01038

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01038

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01038

Sequence similarities

Belongs to the BPG-independent phosphoglycerate mutase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandManganese
Metal-binding
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular_function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5435432,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038
PRO_0000212195

Sites

Active site731Phosphoserine intermediate By similarity
Metal binding201Manganese 2 By similarity
Metal binding731Manganese 2 By similarity
Metal binding4281Manganese 1 By similarity
Metal binding4321Manganese 1 By similarity
Metal binding4691Manganese 2 By similarity
Metal binding4701Manganese 2 By similarity
Metal binding4881Manganese 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UFG7 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D2AB2967D098CC45

FASTA54359,011
        10         20         30         40         50         60 
MVLTFMTATR RRPVVLIVRD GWGQNPDPKW NESNAVHLAN TPVDDKLTQE YPSVLIHTSG 

        70         80         90        100        110        120 
EDVGLPAGVM GNSEVGHQNI GAGRIVDQEV MRITRAIRDD SFFSNPVVTG AIDHVKKSGG 

       130        140        150        160        170        180 
RLHLLGLMSD GRVHSDLQHG IAVIDLAKRN GLTGDQLAIH AITDGRDTSP RGGLKFVSQL 

       190        200        210        220        230        240 
TDHCEASGVG VVASVIGRFY AMDRDLRWER VEAAYNLMTQ GTGQTFPSAS AAIESYYANP 

       250        260        270        280        290        300 
TESSRDGDEF ITASSIVPEG GSPITVQPGD AVLFMNYRGD RTREITKAFT FDDAAWKDIP 

       310        320        330        340        350        360 
GGGFDRGKKI DNLYFATMTG YETGLPVKVI FEKPAKMPNI LGEYVASKGL HQFRCAETEK 

       370        380        390        400        410        420 
YPHVTFFFND YRDNPFEEEE WGMAPSPRDV STYDQKPEMS AEDITEKVLK QIKSGKCDMI 

       430        440        450        460        470        480 
IVNYANGDMV GHTGVLEAAI KAVEKVDACV GRVVDATLAA GGSLVVTADH GNCEQMIDPE 

       490        500        510        520        530        540 
TGGPHTAHTT YQVPLIVVDP EFVGKPLREG GRLADIAPTV LALMGLEVPP EMTGRPLMET 


QTA 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294147 Genomic DNA. Translation: CAD78715.1.
RefSeqNP_868437.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UFG7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB8562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD78715; CAD78715; RB8562.
GeneID1792126.
KEGGrba:RB8562.
PATRIC23249695. VBIRhoBal59814_4115.

Phylogenomic databases

eggNOGCOG0696.
HOGENOMHOG000223664.
KOK15633.
OMAAIHANEA.
OrthoDBEOG6HJ22X.
ProtClustDBPRK05434.

Enzyme and pathway databases

UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
HAMAPMF_01038. GpmI.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFPIRSF001492. IPGAM. 1 hit.
SUPFAMSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
TIGRFAMsTIGR01307. pgm_bpd_ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGPMI_RHOBA
AccessionPrimary (citable) accession number: Q7UFG7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways