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C7ND26 (C7ND26_LEPBD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 30. 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
Ordered Locus Names:Lebu_2043 EMBL ACV39904.1
OrganismLeptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249) [Complete proteome] [HAMAP] EMBL ACV39904.1
Taxonomic identifier523794 [NCBI]
Taxonomic lineageBacteriaFusobacteriaFusobacterialesLeptotrichiaceaeLeptotrichia

Protein attributes

Sequence length228 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
   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

Region20 – 2122-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region86 – 8942-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region113 – 11422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site81Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1811 By similarity HAMAP-Rule MF_01039
Binding site1412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site5912-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18312-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
C7ND26 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 2CD28F57620C70DB

FASTA22826,087
        10         20         30         40         50         60 
MKLVLIRHGE SQWNLENKFT GWKDVDLSPK GIEEAKSGGK KLKEMGFVFD VAYTSYLKRA 

        70         80         90        100        110        120 
IKTLDYVLEE LDELYIPVYK SWRLNERHYG ALQGLNKAET AKKYGDEQVL IWRRSFDVAP 

       130        140        150        160        170        180 
PAIDKSSEYY PKSDRRYAEL SDSEAPLGES LKDTIARVLP YWHSHISKSL REGKNVIVAA 

       190        200        210        220 
HGNSLRALIK YLLNISDDDI LKLNLTTGKP LVFEMDKDLN VLSSPDSF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001685 Genomic DNA. Translation: ACV39904.1.
RefSeqYP_003164895.1. NC_013192.1.

3D structure databases

ProteinModelPortalC7ND26.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING523794.Lebu_2043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACV39904; ACV39904; Lebu_2043.
GeneID8408762.
KEGGlba:Lebu_2043.
PATRIC22403435. VBILepBuc70646_2065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBCLSK2518865.

Enzyme and pathway databases

BioCycLBUC523794:GHCR-2083-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 nameC7ND26_LEPBD
AccessionPrimary (citable) accession number: C7ND26
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: February 19, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)