Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A9WLX7 (A9WLX7_RENSM) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 41. 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:RSal33209_0404 EMBL ABY22158.1
OrganismRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP] EMBL ABY22158.1
Taxonomic identifier288705 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeRenibacterium

Protein attributes

Sequence length253 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 SAAS SAAS013078

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039 SAAS SAAS013078

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039 SAAS SAAS013078

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 SAAS013078
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS013078 EMBL ABY22158.1
   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

Region28 – 2922-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region94 – 9742-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region121 – 12222-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site161Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1881 By similarity HAMAP-Rule MF_01039
Binding site2212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site10512-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site19012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
A9WLX7 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 5CC534C4CFBF5643

FASTA25328,113
        10         20         30         40         50         60 
MDRLLDMTYT LILLRHGHSE WNAKNLFTGW VDVDLNDQGR AEAVRGGQLL VENDLLPDVL 

        70         80         90        100        110        120 
YTSRQKRAIN TANLTLAEAD RGWIDVKRSW RLNERHYGAL QGKDKAQTLA EFGEAQFMEW 

       130        140        150        160        170        180 
RRSYDVPPPP LPDDSEFSQV GDPRYADLGD AIPRTECLKD VLERLLSYWE SDIKADLCAG 

       190        200        210        220        230        240 
KTVLVTAHGN SLRSLVKHLD GISDEAIAGL NIPTGIPLVY ELDENFAPIT AGGRYLDPAA 

       250 
AAAIQAVANQ GKK 

« Hide

References

[1]"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
J. Bacteriol. 190:6970-6982(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000910 Genomic DNA. Translation: ABY22158.1.
RefSeqYP_001623572.1. NC_010168.1.

3D structure databases

ProteinModelPortalA9WLX7.
SMRA9WLX7. Positions 8-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288705.RSal33209_0404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY22158; ABY22158; RSal33209_0404.
GeneID5822556.
KEGGrsa:RSal33209_0404.
PATRIC23073960. VBIRenSal21953_0417.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK14120.

Enzyme and pathway databases

BioCycRSAL288705:GHX1-404-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
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.
ProtoNetSearch...

Entry information

Entry nameA9WLX7_RENSM
AccessionPrimary (citable) accession number: A9WLX7
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)