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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Borrelia afzelii (strain PKo)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.UniRule annotation

Pathway: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. no protein annotated in this organism
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91Tele-phosphohistidine intermediateUniRule annotation
Binding sitei60 – 601SubstrateUniRule annotation
Binding sitei98 – 981SubstrateUniRule annotation
Active sitei182 – 1821UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutaseUniRule annotation (EC:5.4.2.11UniRule annotation)
Short name:
BPG-dependent PGAMUniRule annotation
Short name:
PGAMUniRule annotation
Short name:
PhosphoglyceromutaseUniRule annotation
Short name:
dPGMUniRule annotation
Gene namesi
Name:gpmAUniRule annotation
Ordered Locus Names:BAPKO_0702, BafPKo_0682
OrganismiBorrelia afzelii (strain PKo)
Taxonomic identifieri390236 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorreliaBorrelia burgdorferi group
ProteomesiUP000005216 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2482482,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_1000064033Add
BLAST

Proteomic databases

PRIDEiQ0SMJ5.

Interactioni

Protein-protein interaction databases

STRINGi390236.BAPKO_0702.

Structurei

3D structure databases

ProteinModelPortaliQ0SMJ5.
SMRiQ0SMJ5. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 158Substrate bindingUniRule annotation
Regioni21 – 222Substrate bindingUniRule annotation
Regioni87 – 904Substrate bindingUniRule annotation
Regioni114 – 1152Substrate bindingUniRule annotation
Regioni183 – 1842Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0SMJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYKLVLVRHG ESEWNKENLF TGWTDVKLSD KGVDEAIEAG LLLKQEGYFF
60 70 80 90 100
DIAFSSLLSR ANDTLNIILK ELGQSYISVK KTWRLNERHY GALQGLNKSE
110 120 130 140 150
TAAKYGEDKV LIWRRSYDVP PMSLDESDDR HPIKDPRYKY IPKRELPSTE
160 170 180 190 200
CLKDTIARVI PYWIDEIAKE ILEGKKVIVA AHGNSLRALV KYLDNLSEED
210 220 230 240
VLKLNIPTGI PLVYELDKDL NPIKHYYLGD ENKIKKAMES VASQGKLR
Length:248
Mass (Da):28,499
Last modified:September 5, 2006 - v1
Checksum:i342F369B47AB0E0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000395 Genomic DNA. Translation: ABH01933.1.
CP002933 Genomic DNA. Translation: AEL69878.1.
RefSeqiWP_004790089.1. NC_017238.1.
YP_005592868.1. NC_017238.1.
YP_710109.1. NC_008277.1.

Genome annotation databases

EnsemblBacteriaiABH01933; ABH01933; BAPKO_0702.
AEL69878; AEL69878; BafPKo_0682.
KEGGibaf:BAPKO_0702.
bafz:BafPKo_0682.
PATRICi37189661. VBIBorAfz3878_0718.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000395 Genomic DNA. Translation: ABH01933.1.
CP002933 Genomic DNA. Translation: AEL69878.1.
RefSeqiWP_004790089.1. NC_017238.1.
YP_005592868.1. NC_017238.1.
YP_710109.1. NC_008277.1.

3D structure databases

ProteinModelPortaliQ0SMJ5.
SMRiQ0SMJ5. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi390236.BAPKO_0702.

Proteomic databases

PRIDEiQ0SMJ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABH01933; ABH01933; BAPKO_0702.
AEL69878; AEL69878; BafPKo_0682.
KEGGibaf:BAPKO_0702.
bafz:BafPKo_0682.
PATRICi37189661. VBIBorAfz3878_0718.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
    Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M.
    BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PKo.
  2. "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates."
    Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E.
    J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PKo.

Entry informationi

Entry nameiGPMA_BORAP
AccessioniPrimary (citable) accession number: Q0SMJ5
Secondary accession number(s): G0IQK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: June 24, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.