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Q04CE3 (Q04CE3_LACDB) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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=5.4.2.1 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039
Ordered Locus Names:LBUL_0203
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365) [Complete proteome] [HAMAP] EMBL ABJ57879.1
Taxonomic identifier321956 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length229 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 SAAS013078

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Site601Interaction with carboxyl group of phosphoglycerates By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
Q04CE3 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 343F504EB9F04111

FASTA22926,091
        10         20         30         40         50         60 
MSKLVLIRHG QSEWNLSNQF TGWVDVNLSD KGVEEAKKAG RLIKEAGLEF DQAYTSVLTR 

        70         80         90        100        110        120 
AIKTLHFALE ESGQLWVPET KSWRLNERHY GALQGLNKAE TAEKYGDEQV HIWRRSYDVL 

       130        140        150        160        170        180 
PPVLADDSEF SQANDRRYAN LDPHIVPKAE NLKVTLDRVM PFWEDHIAPD LLAGKNVIIA 

       190        200        210        220 
AHGNSLRALT KYIENISDED IMDVEMKTGE PVVYTFDDKL NVVSKEKLD 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000412 Genomic DNA. Translation: ABJ57879.1.
RefSeqYP_812317.1. NC_008529.1.

3D structure databases

ProteinModelPortalQ04CE3.
SMRQ04CE3. Positions 1-228.
ModBaseSearch...

Protein-protein interaction databases

STRING321956.LBUL_0203.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ57879; ABJ57879; LBUL_0203.
GeneID4436232.
KEGGlbu:LBUL_0203.
PATRIC22220225. VBILacDel70259_0203.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAGQSDWNL.
ProtClustDBPRK14116.

Enzyme and pathway databases

BioCycLDEL321956:GI15-323-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 nameQ04CE3_LACDB
AccessionPrimary (citable) accession number: Q04CE3
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)