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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Thermoanaerobacter mathranii (strain DSM 11426 / CIP 108742 / A3)
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 sitei9 – 91Tele-phosphohistidine intermediateUniRule annotation
Binding sitei15 – 1512-phospho-D-glycerateUniRule annotation
Binding sitei60 – 6012-phospho-D-glycerateUniRule annotation
Binding sitei98 – 9812-phospho-D-glycerateUniRule annotation
Active sitei182 – 1821UniRule annotation
Binding sitei184 – 18412-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

BioCyciTMAT583358:GHOX-2148-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:Tmath_2073Imported
OrganismiThermoanaerobacter mathranii (strain DSM 11426 / CIP 108742 / A3)Imported
Taxonomic identifieri583358 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter
ProteomesiUP000002064 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliD7ASV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 2222-phospho-D-glycerate bindingUniRule annotation
Regioni87 – 9042-phospho-D-glycerate bindingUniRule annotation
Regioni114 – 11522-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.

D7ASV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYKVVLLRHG ESLWNMENRF TGWTDIDLSP KGVEEARESG KTLKAEGYIF
60 70 80 90 100
DCAFTSVLKR AIRTLWIVLD ELDLMWIPVY KSWRLNERHY GALQGLNKAE
110 120 130 140 150
TAKKYGEEQV KIWRRSADVR PPALEKDDPR YPGFDPRYAD LSEEEIPLTE
160 170 180 190 200
NLIDTINRVT SYWESTIAPT IKSGKKVLIV AHGNSLRGLV KYLDNLSNEE
210 220 230 240 250
IMELNIPTGI PLVYELDGDL KPIKHYYLAD EEKVKEKKEL VAKQGKVQGN

S
Length:251
Mass (Da):28,885
Last modified:August 10, 2010 - v1
Checksum:i49D483F050664340
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002032 Genomic DNA. Translation: ADH61747.1.
RefSeqiWP_013150903.1. NC_014209.1.
YP_003677758.1. NC_014209.1.

Genome annotation databases

EnsemblBacteriaiADH61747; ADH61747; Tmath_2073.
KEGGitmt:Tmath_2073.
PATRICi38282421. VBITheMat18_2137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002032 Genomic DNA. Translation: ADH61747.1.
RefSeqiWP_013150903.1. NC_014209.1.
YP_003677758.1. NC_014209.1.

3D structure databases

ProteinModelPortaliD7ASV1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADH61747; ADH61747; Tmath_2073.
KEGGitmt:Tmath_2073.
PATRICi38282421. VBITheMat18_2137.

Phylogenomic databases

HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciTMAT583358:GHOX-2148-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 sequence of Thermoanaerobacter mathranii subsp. mathranii mathranii str. A3."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.
    Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 11426 / CIP 108742 / A3Imported.

Entry informationi

Entry nameiD7ASV1_THEM3
AccessioniPrimary (citable) accession number: D7ASV1
Entry historyi
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: May 27, 2015
This is version 37 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.