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D2NWV8 (D2NWV8_LISM1) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 29. 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
Ordered Locus Names:LM5578_2408 EMBL ADB69155.1
OrganismListeria monocytogenes serotype 1/2a (strain 08-5578) [Complete proteome] [HAMAP] EMBL ADB69155.1
Taxonomic identifier653938 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

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

Region20 – 2122-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region86 – 8942-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region113 – 11422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site81Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1811 By similarity HAMAP-Rule MF_01039
Binding site1412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site5912-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18312-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
D2NWV8 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 3073F6E8CAEDEFE9

FASTA22926,461
        10         20         30         40         50         60 
MKLVLIRHGQ SEWNKLNLFT GWHDVDLSQE GVVEAMTAGK RIKEAGLEFD VAFTSVLTRA 

        70         80         90        100        110        120 
IKTLNYVLEE SDQMWVPVHK SWRLNERHYG ALQGLNKQET AEKYGADQVQ KWRRSYDTLP 

       130        140        150        160        170        180 
PLLEENDERQ AKNDRRYQLL DTHAIPSGEN LKVTLERVIP YWMDTIAPEI KEGRRVVIAA 

       190        200        210        220 
HGNSLRALVK FLEGISDDEI MDLEIPTGVP LVYELNDDLK PVNKYYLDK 

« Hide

References

[1]"High-throughput genome sequencing of two Listeria monocytogenes clinical isolates during a large foodborne outbreak."
Gilmour M.W., Graham M., Van Domselaar G., Tyler S., Kent H., Trout-Yakel K.M., Larios O., Allen V., Lee B., Nadon C.
BMC Genomics 11:120-120(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 08-5578 EMBL ADB69155.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001602 Genomic DNA. Translation: ADB69155.1.
RefSeqYP_003414517.1. NC_013766.1.

3D structure databases

ProteinModelPortalD2NWV8.
SMRD2NWV8. Positions 2-227.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB69155; ADB69155; LM5578_2408.
GeneID8749391.
KEGGlmn:LM5578_2408.
PATRIC35279350. VBILisMon159512_2425.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221682.
KOK01834.

Enzyme and pathway databases

BioCycLMON653938:GJ8G-2444-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
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]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD2NWV8_LISM1
AccessionPrimary (citable) accession number: D2NWV8
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: June 11, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)