Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Escherichia coli O103:H2 (strain 12009 / EHEC)
Status
Unreviewed-Annotation score: -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

Pathwayi: 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)
  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)DescriptionActionsGraphical viewLength
Active sitei11Tele-phosphohistidine intermediateUniRule annotation1
Binding sitei62SubstrateUniRule annotation1
Active sitei89Proton donor/acceptorUniRule annotation1
Binding sitei100SubstrateUniRule annotation1
Sitei184Transition state stabilizerUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomeraseUniRule annotationSAAS annotation
Biological processGluconeogenesisUniRule annotation, GlycolysisUniRule annotationSAAS annotation

Enzyme and pathway databases

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000959 Componenti: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliC8U3Y4
SMRiC8U3Y4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 17Substrate bindingUniRule annotation8
Regioni23 – 24Substrate bindingUniRule annotation2
Regioni89 – 92Substrate bindingUniRule annotation4
Regioni116 – 117Substrate bindingUniRule annotation2
Regioni185 – 186Substrate bindingUniRule annotation2

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000221682
KOiK01834
OMAiRMLPYWY

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
HAMAPiMF_01039 PGAM_GpmA, 1 hit
InterProiView protein in InterPro
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR001345 PG/BPGM_mutase_AS
IPR005952 Phosphogly_mut1
PANTHERiPTHR11931 PTHR11931, 1 hit
PfamiView protein in Pfam
PF00300 His_Phos_1, 1 hit
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF53254 SSF53254, 1 hit
TIGRFAMsiTIGR01258 pgm_1, 1 hit
PROSITEiView protein in PROSITE
PS00175 PG_MUTASE, 1 hit

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

Genome annotation databases

EnsemblBacteriaiBAI29598; BAI29598; ECO103_0743
KEGGieoh:ECO103_0743

Entry informationi

Entry nameiC8U3Y4_ECO10
AccessioniPrimary (citable) accession number: C8U3Y4
Entry historyiIntegrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: March 28, 2018
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health