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P75167 (GPMI_MYCPN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MPN_628
ORF Names:MP214
OrganismMycoplasma pneumoniae (strain ATCC 29342 / M129) [Reference proteome] [HAMAP]
Taxonomic identifier272634 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length508 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_processglucose catabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

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 – 5085082,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038
PRO_0000212175

Sites

Active site611Phosphoserine intermediate By similarity
Metal binding111Manganese 2 By similarity
Metal binding611Manganese 2 By similarity
Metal binding3971Manganese 1 By similarity
Metal binding4011Manganese 1 By similarity
Metal binding4381Manganese 2 By similarity
Metal binding4391Manganese 2 By similarity
Metal binding4561Manganese 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
P75167 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: A856375375B09F5E

FASTA50856,375
        10         20         30         40         50         60 
MHKKVLLAIL DGYGISNKQH GNAVYHAKTP ALDSLIKDYP CVMLEASGEA VGLPQGQIGN 

        70         80         90        100        110        120 
SEVGHLNIGA GRIVYTGLSL INQNIKTGAF HHNQVLLEAI ARAKANNAKL HLIGLFSHGG 

       130        140        150        160        170        180 
VHSHMDHLYA LIKLAAPQVK MVLHLFGDGR DVAPCTMKSD LEAFMVFLKD YHNVIIGTLG 

       190        200        210        220        230        240 
GRYYGMDRDQ RWDREEIAYN AILGNSKASF TDPVAYVQSA YDQKVTDEFL YPAVNGNVDK 

       250        260        270        280        290        300 
EQFALKDHDS VIFFNFRPDR ARQMSHMLFQ TDYYDYTPKA GRKYNLFFVT MMNYEGIKPS 

       310        320        330        340        350        360 
AVVFPPETIP NTFGEVIAHN KLKQLRIAET EKYAHVTFFF DGGVEVDLPN ETKCMVPSLK 

       370        380        390        400        410        420 
VATYDLAPEM ACKGITDQLL NQINQFDLTV LNFANPDMVG HTGNYAACVQ GLEALDVQIQ 

       430        440        450        460        470        480 
RIIDFCKANH ITLFLTADHG NAEEMIDSNN NPVTKHTVNK VPFVCTDTNI DLQQDSASLA 

       490        500 
NIAPTILAYL GLKQPAEMTA NSLLISKK 

« Hide

References

[1]"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29342 / M129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00089 Genomic DNA. Translation: AAB95862.1.
PIRS73540.
RefSeqNP_110317.1. NC_000912.1.

3D structure databases

ProteinModelPortalP75167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP75167. 4 interactions.
STRING272634.MPN628.

Proteomic databases

PaxDbP75167.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB95862; AAB95862; MPN_628.
GeneID877355.
KEGGmpn:MPN628.
PATRIC20022739. VBIMycPne110_0692.

Phylogenomic databases

eggNOGCOG0696.
KOK15633.
OMADACIGRV.
OrthoDBEOG6HJ22X.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-550.
MPNE272634:GJ6Z-674-MONOMER.
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_MYCPN
AccessionPrimary (citable) accession number: P75167
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 11, 2014
This is version 95 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

Mycoplasma pneumoniae

Mycoplasma pneumoniae (strain M129): entries and gene names