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Q2L0A6 (GPMA_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Short name=BPG-dependent PGAM
Short name=PGAM
Short name=Phosphoglyceromutase
Short name=dPGM
EC=5.4.2.1
Gene names
Name:gpmA
Ordered Locus Names:BAV0243
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01039

Pathway

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

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphosphoglycerate mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2502502,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039
PRO_1000064032

Sites

Active site91Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Site601Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2L0A6 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: B316A962F1CE1A32

FASTA25028,377
        10         20         30         40         50         60 
MYKLVLMRHG ESQWNLENRF TGWTDVDLTE VGREQARRAG ELLKREGYTF DLAYASVLKR 

        70         80         90        100        110        120 
AIRTLWIALD AMDAMYTPVG LNWRLNERHY GQLQGLNKAE TAAKYGDEQV LIWRRAYAIA 

       130        140        150        160        170        180 
PEPLDIDDPR HPRFDSRYAK IPAEQLPATE CLRDTVARVL PFWNESIAPA IRAGRRVLVA 

       190        200        210        220        230        240 
AHGNSLRALI KHLDNISDDA IVELNIPTGQ PLVYELDENL RPIRHYYLGD AAEIEAAMAA 

       250 
VAAQGKAKKD 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ47848.1.
RefSeqYP_784781.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2L0A6.
SMRQ2L0A6. Positions 3-239.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2L0A6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6264588.
GenomeReviewsGene locus BAV0243 in contig AM167904_GR.
KEGGbav:BAV0243.
NMPDRfig|521.1.peg.2638.
PATRIC21126630. VBIBorAvi43433_0256.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658938.
OMAEWNALNL.
ProtClustDBPRK14115.

Enzyme and pathway databases

BioCycABAU360910:BAV0243-MONOMER.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
[Tree]
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
KOK01834.
PANTHERPTHR11931. Phosphogly_mut1. 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 nameGPMA_BORA1
AccessionPrimary (citable) accession number: Q2L0A6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families