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C8U3Y4 (C8U3Y4_ECO10) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039

Short name=BPG-dependent PGAM HAMAP-Rule MF_01039
Short name=PGAM HAMAP-Rule MF_01039
Short name=Phosphoglyceromutase HAMAP-Rule MF_01039
Short name=dPGM HAMAP-Rule MF_01039
EC=5.4.2.11 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039 EMBL BAI29598.1
Ordered Locus Names:ECO103_0743 EMBL BAI29598.1
OrganismEscherichia coli O103:H2 (strain 12009 / EHEC) [Complete proteome] [HAMAP] EMBL BAI29598.1
Taxonomic identifier585395 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length250 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_01039 RuleBase RU004512

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039 RuleBase RU004512 SAAS SAAS001345

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039 RuleBase RU004512

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01039

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Ontologies

Keywords
   Biological processGlycolysis HAMAP-Rule MF_01039 SAAS SAAS001345
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS001345
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region23 – 2422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region89 – 9242-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region116 – 11722-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1841 By similarity HAMAP-Rule MF_01039
Binding site1712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site10012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
C8U3Y4 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: A6E0A49406F8482A

FASTA25028,556
        10         20         30         40         50         60 
MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY SFDFAYTSVL 

        70         80         90        100        110        120 
KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA 

       130        140        150        160        170        180 
VTPPELTKDD ERYPGHDPRY AKLSEKELPL TESLALTIDR VIPYWNETIL PRMKSGERVI 

       190        200        210        220        230        240 
IAAHGNSLRA LVKYLDNMSE EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA 

       250 
AAVANQGKAK 

« Hide

References

[1]"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12009 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010958 Genomic DNA. Translation: BAI29598.1.
RefSeqYP_003220732.1. NC_013353.1.

3D structure databases

ProteinModelPortalC8U3Y4.
SMRC8U3Y4. Positions 2-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING585395.ECO103_0743.

Proteomic databases

PRIDEC8U3Y4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI29598; BAI29598; ECO103_0743.
GeneID8474732.
KEGGeoh:ECO103_0743.
PATRIC32093153. VBIEscCol146794_0786.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMARYATIPP.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycECOL585395:GJA9-771-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC8U3Y4_ECO10
AccessionPrimary (citable) accession number: C8U3Y4
Entry history
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: June 11, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)