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

F9VH34 (F9VH34_LACGL) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 14. 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:LCGL_0207 EMBL BAK59667.1
OrganismLactococcus garvieae (strain Lg2) (Enterococcus seriolicida) [Complete proteome] [HAMAP] EMBL BAK59667.1
Taxonomic identifier420890 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length233 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
   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

Region21 – 2222-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region87 – 9042-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region114 – 11522-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Binding site1512-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9812-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
F9VH34 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 739CC5D6A0C01D9E

FASTA23326,393
        10         20         30         40         50         60 
MVKLVFARHG ESEWNLANLF TGWADVDLSE NGTQQAIDAG KLIKAAGIEF DIAYTSVLKR 

        70         80         90        100        110        120 
AIKTTNYALE YSDQLWVPVV KTWRLNERHY GGLTGLNKAD AAAKHGDEQV HIWRRSYDVL 

       130        140        150        160        170        180 
PPAMPRDDEY SAHADRRYAN LEDSLIPDAE NLKVTLERSL PFWEDQIAPA LKDGKNVFVG 

       190        200        210        220        230 
AHGNSIRALV KHIKQLSDDE IMDVEIPNFP PLVFEFDDNL NLVKEYYLAP KQA 

« Hide

References

[1]"Complete genome sequence and comparative analysis of the fish pathogen Lactococcus garvieae."
Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K., Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.
PLoS ONE 6:E23184-E23184(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lg2 EMBL BAK59667.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009333 Genomic DNA. Translation: BAK59667.1.
RefSeqYP_005869951.1. NC_017490.1.

3D structure databases

ProteinModelPortalF9VH34.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAK59667; BAK59667; LCGL_0207.
GeneID12478749.
KEGGlgv:LCGL_0207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.

Enzyme and pathway databases

BioCycLGAR420890:GLFD-217-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 nameF9VH34_LACGL
AccessionPrimary (citable) accession number: F9VH34
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: February 19, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)