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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280)
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

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

  1. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

IsomeraseUniRule annotationSAAS annotation

Keywords - Biological processi

GlycolysisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciCROD637910:GJIG-771-MONOMER.

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:ROD_07471Imported
OrganismiCitrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280)Imported
Taxonomic identifieri637910 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter
ProteomesiUP000001889: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliD2TPF5.
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

HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.

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.

D2TPF5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVTKLVLVR HGESQWNNEN RFTGWYDVDL SEKGVGEAKA AGKLLKEEGY
60 70 80 90 100
SFDFAYTSVL KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK
110 120 130 140 150
AETAEKYGDE QVKQWRRGFA VTPPELTKDD ERYPGHDPRY AKLTEKELPL
160 170 180 190 200
TESLALTIDR VIPYWNETIL PRMKSGERVI IAAHGNSLRA LVKYLDNMSE
210 220 230 240 250
DEILELNIPT GVPLVYEFDE NFKPIKHYYL GNADEIAAKA AAVANQGKAK
Length:250
Mass (Da):28,493
Last modified:March 2, 2010 - v1
Checksum:i1814C950DA5843FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN543502 Genomic DNA. Translation: CBG87524.1.
RefSeqiWP_012905076.1. NC_013716.1.
YP_003364371.1. NC_013716.1.

Genome annotation databases

EnsemblBacteriaiCBG87524; CBG87524; ROD_07471.
GeneIDi8710392.
KEGGicro:ROD_07471.
PATRICi32025397. VBICitRod33214_0733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN543502 Genomic DNA. Translation: CBG87524.1.
RefSeqiWP_012905076.1. NC_013716.1.
YP_003364371.1. NC_013716.1.

3D structure databases

ProteinModelPortaliD2TPF5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBG87524; CBG87524; ROD_07471.
GeneIDi8710392.
KEGGicro:ROD_07471.
PATRICi32025397. VBICitRod33214_0733.

Phylogenomic databases

HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.

Enzyme and pathway databases

BioCyciCROD637910:GJIG-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. "The Citrobacter rodentium genome sequence reveals convergent evolution with human pathogenic Escherichia coli."
    Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G., Thomson N.R.
    J. Bacteriol. 192:525-538(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ICC168Imported.

Entry informationi

Entry nameiD2TPF5_CITRI
AccessioniPrimary (citable) accession number: D2TPF5
Entry historyi
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: February 4, 2015
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.