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I6S344 (I6S344_ENTCL) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039

Short name=BPG-dependent PGAM HAMAP-Rule MF_01039
Short name=PGAM HAMAP-Rule MF_01039
Short name=Phosphoglyceromutase HAMAP-Rule MF_01039
Short name=dPGM HAMAP-Rule MF_01039
EC=5.4.2.11 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039 EMBL AFM59064.1
ORF Names:A3UG_06615 EMBL AFM59064.1
OrganismEnterobacter cloacae subsp. dissolvens SDM [Complete proteome] EMBL AFM59064.1
Taxonomic identifier1104326 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. RuleBase RU004512 HAMAP-Rule MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. RuleBase RU004512 HAMAP-Rule MF_01039 SAAS SAAS001345

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. RuleBase RU004512 HAMAP-Rule MF_01039

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01039

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Ontologies

Keywords
   Biological processGlycolysis HAMAP-Rule MF_01039 SAAS SAAS001345
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS001345 EMBL AFM59064.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region23 – 2422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region89 – 9242-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region116 – 11722-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1841 By similarity HAMAP-Rule MF_01039
Binding site1712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site10012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
I6S344 [UniParc].

Last modified October 3, 2012. Version 1.
Checksum: 0644DB92912B008D

FASTA25028,376
        10         20         30         40         50         60 
MAITKLVLVR HGESQWNNEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGF SFDFAYTSVL 

        70         80         90        100        110        120 
KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA 

       130        140        150        160        170        180 
VTPPELTKDD ERYPGHDPRY AKLTDAELPT TESLALTIDR VVPYWNETIL PRLKSGERVI 

       190        200        210        220        230        240 
IAAHGNSLRA LVKYLDNMGE DEILELNIPT GVPLVYEFDE NFKPIKHYYL GNADEIAAKA 

       250 
AAVANQGKAK 

« Hide

References

[1]"Genome sequence of Enterobacter cloacae subsp. dissolvens SDM, an efficient biomass-utilizing producer of platform chemical 2,3-butanediol."
Xu Y., Wang A., Tao F., Su F., Tang H., Ma C., Xu P.
J. Bacteriol. 194:897-898(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SDM EMBL AFM59064.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003678 Genomic DNA. Translation: AFM59064.1.
RefSeqYP_006476766.1. NC_018079.1.

3D structure databases

ProteinModelPortalI6S344.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFM59064; AFM59064; A3UG_06615.
GeneID13169105.
KEGGenl:A3UG_06615.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.

Enzyme and pathway databases

UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameI6S344_ENTCL
AccessionPrimary (citable) accession number: I6S344
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2012
Last sequence update: October 3, 2012
Last modified: February 19, 2014
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)