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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Escherichia coli O103:H2 (strain 12009 / EHEC)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.UniRule annotationSAAS annotation

Pathway: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
  3. Probable phosphoglycerate mutase GpmB (ytjC), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (pykA), Pyruvate kinase (pykF)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Tele-phosphohistidine intermediateUniRule annotation
Binding sitei17 – 1712-phospho-D-glycerateUniRule annotation
Binding sitei62 – 6212-phospho-D-glycerateUniRule annotation
Binding sitei100 – 10012-phospho-D-glycerateUniRule annotation
Active sitei184 – 1841UniRule annotation
Binding sitei186 – 18612-phospho-D-glycerateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

IsomeraseUniRule annotationSAAS annotation

Keywords - Biological processi

GlycolysisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciECOL585395:GJA9-771-MONOMER.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutaseUniRule annotation (EC:5.4.2.11UniRule annotation)
Short name:
BPG-dependent PGAMUniRule annotation
Short name:
PGAMUniRule annotation
Short name:
PhosphoglyceromutaseUniRule annotation
Short name:
dPGMUniRule annotation
Gene namesi
Name:gpmAUniRule annotationImported
Ordered Locus Names:ECO103_0743Imported
OrganismiEscherichia coli O103:H2 (strain 12009 / EHEC)Imported
Taxonomic identifieri585395 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000959 Componenti: Chromosome

PTM / Processingi

Proteomic databases

PRIDEiC8U3Y4.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliC8U3Y4.
SMRiC8U3Y4. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 2422-phospho-D-glycerate bindingUniRule annotation
Regioni89 – 9242-phospho-D-glycerate bindingUniRule annotation
Regioni116 – 11722-phospho-D-glycerate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C8U3Y4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY
60 70 80 90 100
SFDFAYTSVL KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK
110 120 130 140 150
AETAEKYGDE QVKQWRRGFA VTPPELTKDD ERYPGHDPRY AKLSEKELPL
160 170 180 190 200
TESLALTIDR VIPYWNETIL PRMKSGERVI IAAHGNSLRA LVKYLDNMSE
210 220 230 240 250
EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA AAVANQGKAK
Length:250
Mass (Da):28,556
Last modified:November 3, 2009 - v1
Checksum:iA6E0A49406F8482A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010958 Genomic DNA. Translation: BAI29598.1.
RefSeqiWP_001295305.1. NC_013353.1.
YP_003220732.1. NC_013353.1.

Genome annotation databases

EnsemblBacteriaiBAI29598; BAI29598; ECO103_0743.
KEGGieoh:ECO103_0743.
PATRICi32093153. VBIEscCol146794_0786.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010958 Genomic DNA. Translation: BAI29598.1.
RefSeqiWP_001295305.1. NC_013353.1.
YP_003220732.1. NC_013353.1.

3D structure databases

ProteinModelPortaliC8U3Y4.
SMRiC8U3Y4. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiC8U3Y4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAI29598; BAI29598; ECO103_0743.
KEGGieoh:ECO103_0743.
PATRICi32093153. VBIEscCol146794_0786.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciECOL585395:GJA9-771-MONOMER.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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 / EHECImported.

Entry informationi

Entry nameiC8U3Y4_ECO10
AccessioniPrimary (citable) accession number: C8U3Y4
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: June 24, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.