Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8L1Z7 (GPMA_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 70. 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
Synonyms:pgm
Ordered Locus Names:BH12450
OrganismBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier283166 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length206 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

Catalytic activity

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

Pathway

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

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2062062,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_0000179848

Sites

Active site101Tele-phosphohistidine intermediate By similarity
Active site1581 By similarity
Site611Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8L1Z7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: F2AA8D379630D994

FASTA20623,252
        10         20         30         40         50         60 
MERTLVLIRH GQSEWNLKNL FTGWKDPGLT EKGRTEAIAA GKKLKETGLK FDIAYTSALQ 

        70         80         90        100        110        120 
RAQKTAQNIL EQMEQSDLEL IKTPALNERN YGDLSGLNKD EVRQKWGEQQ VQIWRRSYTI 

       130        140        150        160        170        180 
APPNGESLRD TGARVWPYYL HHIQPHILRS QTVLIAAHGN SLRALIMALE GLNSEEIISQ 

       190        200 
ELATGIPIVY TFNSDSTISS KTIITP 

« Hide

References

« Hide 'large scale' references
[1]"The global phylogeny of glycolytic enzymes."
Canback B., Andersson S.G.E., Kurland C.G.
Proc. Natl. Acad. Sci. U.S.A. 99:6097-6102(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.
[2]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY074773 Genomic DNA. Translation: AAL74286.1.
BX897699 Genomic DNA. Translation: CAF28027.1.
RefSeqYP_033999.1. NC_005956.1.

3D structure databases

ProteinModelPortalQ8L1Z7.
SMRQ8L1Z7. Positions 5-204.
ModBaseSearch...

Protein-protein interaction databases

STRING283166.BH12450.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF28027; CAF28027; BH12450.
GeneID2865050.
KEGGbhe:BH12450.
PATRIC20546369. VBIBarHen29080_1314.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAGQSDWNL.
ProtClustDBPRK01295.

Enzyme and pathway databases

BioCycBHEN283166:GIVZ-1240-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 nameGPMA_BARHE
AccessionPrimary (citable) accession number: Q8L1Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: October 1, 2002
Last modified: May 29, 2013
This is version 70 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