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I1W8V3 (I1W8V3_BIFAR) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 10. 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 AFI62685.1
Ordered Locus Names:BANAN_02325 EMBL AFI62685.1
OrganismBifidobacterium animalis subsp. animalis (strain ATCC 25527 / DSM 20104 / JCM 1190 / R101-8) [Complete proteome] [HAMAP] EMBL AFI62685.1
Taxonomic identifier703613 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length246 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 EMBL AFI62685.1
   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

Region22 – 2322-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region88 – 9142-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region115 – 11622-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site101Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1801 By similarity HAMAP-Rule MF_01039
Binding site1612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6112-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9912-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
I1W8V3 [UniParc].

Last modified July 11, 2012. Version 1.
Checksum: 0163C61149720FE5

FASTA24627,644
        10         20         30         40         50         60 
MTYKLVLLRH GQSEWNKTNQ FTGWVDVPLT EKGREEAKNG GKLMKDKGVL PDIVFTSLLR 

        70         80         90        100        110        120 
RAINTANIAL DEADRLWIPV KRDWRLNERH YGALQGKNKS EIREEYGDEK FMLWRRSYGT 

       130        140        150        160        170        180 
PPPEIDPNDQ YAQNNDPRYA GDPVPEAECL ADVVERVKPY FEAEIEPELK DGKTVLIAAH 

       190        200        210        220        230        240 
GNSLRAIVKM LDGLTEEEIA KVNIPTAIPL VYELDENFKP IKKGGEYLDP EAAAAGAAAV 


AAQGQK 

« Hide

References

[1]"Short communication: the complete genome sequence of Bifidobacterium animalis subspecies animalis ATCC 25527(T) and comparative analysis of growth in milk with B. animalis subspecies lactis DSM 10140(T)."
Loquasto J.R., Barrangou R., Dudley E.G., Roberts R.F.
J. Dairy Sci. 94:5864-5870(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25527 EMBL AFI62685.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002567 Genomic DNA. Translation: AFI62685.1.
RefSeqYP_006279648.1. NC_017834.1.

3D structure databases

ProteinModelPortalI1W8V3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFI62685; AFI62685; BANAN_02325.
GeneID12834931.
KEGGbni:BANAN_02325.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.
OMASYYLGDQ.

Enzyme and pathway databases

BioCycBANI703613:GL91-474-MONOMER.
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 nameI1W8V3_BIFAR
AccessionPrimary (citable) accession number: I1W8V3
Entry history
Integrated into UniProtKB/TrEMBL: July 11, 2012
Last sequence update: July 11, 2012
Last modified: February 19, 2014
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)