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P47669 (GPMI_MYCGE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. 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:MG430
OrganismMycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) [Complete proteome] [HAMAP]
Taxonomic identifier243273 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length507 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
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 – 5075072,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038
PRO_0000212167

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
P47669 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 9BD9F5007C9CBEB5

FASTA50756,867
        10         20         30         40         50         60 
MHKKVLLAIL DGYGISNAIY GNAVQNANTP MLDELINSYP CVLLDASGEA VGLPMGQIGN 

        70         80         90        100        110        120 
SEVGHLNIGA GRVVYTGLSL INQHIKDRSF FANKAFLKTI EHVEKNHSKI HLIGLFSNGG 

       130        140        150        160        170        180 
VHSHNEHLLA LIELFSKHAK VVLHLFGDGR DVAPCSLKQD LEKLMIFLKN YPNVVIGTIG 

       190        200        210        220        230        240 
GRYYGMDRDQ RWDREMIAYK ALLGVSKNKF NDPIGYIETQ YQNQITDEFI YPAINANLNS 

       250        260        270        280        290        300 
DQFALNNNDG VISFNFRPDR ARQMSHLIFN SNYYNYQPEL KRKENLFFVT MMNYEGIVPS 

       310        320        330        340        350        360 
EFAFPPQTIK NSLGEVIANN NLKQLRIAET EKYAHVTFFF DGGFEVNLSN ETKTLIPSLK 

       370        380        390        400        410        420 
VATYDLAPEM SCKAITDALL EKLNNFDFTV LNFANPDMVG HTGNYQACIK ALEALDVQIK 

       430        440        450        460        470        480 
RIVDFCKANQ ITMFLTADHG NAEVMIDNNN NPVTKHTINP VPFVCTDKNV NFNQTGILAN 

       490        500 
IAPTILEYLN LSKPKEMTAK SLLKNNN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43967 Genomic DNA. Translation: AAC72451.1.
PIRE64247.
RefSeqNP_073101.2. NC_000908.2.

3D structure databases

ProteinModelPortalP47669.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243273.MG_430.

Proteomic databases

PRIDEP47669.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC72451; AAC72451; MG_430.
GeneID875625.
KEGGmge:MG_430.
PATRIC20010446. VBIMycGen98045_0496.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0696.
KOK15633.
OrthoDBEOG6HJ22X.

Enzyme and pathway databases

BioCycMGEN243273:GH2R-484-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_MYCGE
AccessionPrimary (citable) accession number: P47669
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 94 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 genitalium

Mycoplasma genitalium (strain G-37): entries and gene names