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B5BHY7 (B5BHY7_SALPK) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 40. 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-independent phosphoglycerate mutase HAMAP-Rule MF_01038

Short name=BPG-independent PGAM HAMAP-Rule MF_01038
Short name=Phosphoglyceromutase HAMAP-Rule MF_01038
Short name=iPGM HAMAP-Rule MF_01038
EC=5.4.2.12 HAMAP-Rule MF_01038
Gene names
Name:gpmI HAMAP-Rule MF_01038
Ordered Locus Names:SSPA3319 EMBL CAR61585.1
OrganismSalmonella paratyphi A (strain AKU_12601) [Complete proteome] [HAMAP] EMBL CAR61585.1
Taxonomic identifier554290 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length507 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_01038 SAAS SAAS011258

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01038 SAAS SAAS011258

Cofactor

Binds 2 manganese ions per subunit By similarity. HAMAP-Rule MF_01038 SAAS SAAS006124

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01038 SAAS SAAS011258

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01038

Sequence similarities

Belongs to the BPG-independent phosphoglycerate mutase family. HAMAP-Rule MF_01038

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site571Phosphoserine intermediate By similarity HAMAP-Rule MF_01038
Metal binding71Manganese 2 By similarity HAMAP-Rule MF_01038
Metal binding571Manganese 2 By similarity HAMAP-Rule MF_01038
Metal binding3961Manganese 1 By similarity HAMAP-Rule MF_01038
Metal binding4001Manganese 1 By similarity HAMAP-Rule MF_01038
Metal binding4371Manganese 2 By similarity HAMAP-Rule MF_01038
Metal binding4381Manganese 2 By similarity HAMAP-Rule MF_01038
Metal binding4561Manganese 1 By similarity HAMAP-Rule MF_01038

Sequences

Sequence LengthMass (Da)Tools
B5BHY7 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 96F6B95A297D4123

FASTA50755,497
        10         20         30         40         50         60 
MVLVILDGYG YREEQQDNAI LNAKTPVMDA LWAKRPHTLI DASGLEVGLP DRQMGNSEVG 

        70         80         90        100        110        120 
HVNLGAGRIV YQDLTRLDVE IKERTFFANP VLTNAVDQAK NAGKAVHIMG LLSAGGVHSH 

       130        140        150        160        170        180 
EDHIMAMVEL AAERGAEKIY LHAFLDGRDT PPRSAEASLK KFEDKFAALG KGRVASIVGR 

       190        200        210        220        230        240 
YYAMDRDNRW DRVEKAYDLM TLAQGEFQAD TAVAGLQAAY ARDENDEFVK ATVIRAEGQA 

       250        260        270        280        290        300 
DAAMEDGDTL IFMNFRADRA REITRAFVNA DFDGFARKKV VNLNFVMLTE YAADIKTAVA 

       310        320        330        340        350        360 
YPPASLANTF GEWMAKNDKT QLRISETEKY AHVTFFFNGG VEEPFAGEER ILINSPKVAT 

       370        380        390        400        410        420 
YDLQPEMSSA ELTEKLVAAI ESGKYDTIIC NYPNGDMVGH TGVMEAAIKA VEALDNCIEQ 

       430        440        450        460        470        480 
VTKAVESVGG QLLITADHGN AEQMRDPATG QAHTAHTNLP VPLIYVGEKN VKAVEGGKLS 

       490        500 
DIAPTMLSLM GMEIPQEMTG KPLFIVE 

« Hide

References

[1]"Pseudogene accumulation in the evolutionary histories of Salmonella enterica serovars Paratyphi A and Typhi."
Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A., Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N., Mungall K., Dougan G., Parkhill J.
BMC Genomics 10:36-36(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AKU_12601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM200053 Genomic DNA. Translation: CAR61585.1.
RefSeqYP_002144158.1. NC_011147.1.

3D structure databases

ProteinModelPortalB5BHY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING554290.SSPA3319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR61585; CAR61585; SSPA3319.
PATRIC32347201. VBISalEnt134303_3790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0696.
HOGENOMHOG000223664.
OMAGVHSHIE.
OrthoDBEOG6HJ22X.
ProtClustDBPRK05434.

Enzyme and pathway databases

BioCycSENT554290:GJDA-3564-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
HAMAPMF_01038. GpmI.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFPIRSF001492. IPGAM. 1 hit.
SUPFAMSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
TIGRFAMsTIGR01307. pgm_bpd_ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB5BHY7_SALPK
AccessionPrimary (citable) accession number: B5BHY7
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)