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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Treponema paraluiscuniculi (strain Cuniculi A)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81Tele-phosphohistidine intermediateUniRule annotation
Binding sitei14 – 1412-phospho-D-glycerateUniRule annotation
Binding sitei59 – 5912-phospho-D-glycerateUniRule annotation
Binding sitei97 – 9712-phospho-D-glycerateUniRule annotation
Active sitei185 – 1851UniRule annotation
Binding sitei187 – 18712-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

BioCyciTPAR545776:GJC6-179-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 annotation
Ordered Locus Names:TPCCA_0168Imported
OrganismiTreponema paraluiscuniculi (strain Cuniculi A)Imported
Taxonomic identifieri545776 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
ProteomesiUP000008317 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliF7XS04.
SMRiF7XS04. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 2122-phospho-D-glycerate bindingUniRule annotation
Regioni86 – 8942-phospho-D-glycerate bindingUniRule annotation
Regioni113 – 11422-phospho-D-glycerate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

KOiK01834.

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.

F7XS04-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLVLIRHGE SEWNRLNLFT GWTDVPLTPR GESEAQEGGR VLQEAGFDFD
60 70 80 90 100
LCYTSFLKRA IRTLNFVLQA LDREWLPVHK SWKLNERHYG DLQGLNKTET
110 120 130 140 150
AQKYGEQQVR VWRRSFDVAP PPLTVGDARC PHTQASYRGV CASGRTPVLP
160 170 180 190 200
FTESLKDTVA RVVPYFEEEI KPQMISGQRV LIVAHGNSLR ALMKHIESLD
210 220 230 240 250
ETQIMEVNLP TGVPLVYEFE ADFTLCGKRF LGNEADVAAR AQAVADQGKS

N
Length:251
Mass (Da):28,358
Last modified:September 21, 2011 - v1
Checksum:i8589EE625A80D60B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002103 Genomic DNA. Translation: AEH40123.1.
RefSeqiYP_004672914.1. NC_015714.1.

Genome annotation databases

EnsemblBacteriaiAEH40123; AEH40123; TPCCA_0168.
KEGGitpl:TPCCA_0168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002103 Genomic DNA. Translation: AEH40123.1.
RefSeqiYP_004672914.1. NC_015714.1.

3D structure databases

ProteinModelPortaliF7XS04.
SMRiF7XS04. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEH40123; AEH40123; TPCCA_0168.
KEGGitpl:TPCCA_0168.

Phylogenomic databases

KOiK01834.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciTPAR545776:GJC6-179-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. "Complete genome sequence of Treponema paraluiscuniculi, strain Cuniculi A: the loss of infectivity to humans is associated with genome decay."
    Smajs D., Zobanikova M., Strouhal M., Cejkova D., Dugan-Rocha S., Pospisilova P., Norris S.J., Albert T., Qin X., Hallsworth-Pepin K., Buhay C., Muzny D.M., Chen L., Gibbs R.A., Weinstock G.M.
    PLoS ONE 6:E20415-E20415(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Cuniculi AImported.

Entry informationi

Entry nameiF7XS04_TREPU
AccessioniPrimary (citable) accession number: F7XS04
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: April 29, 2015
This is version 25 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.