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Q8FSH0 (GPMA_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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:CE0423
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

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_0000179870

Sites

Active site131Tele-phosphohistidine intermediate By similarity
Active site1841 By similarity
Site641Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FSH0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A13B8F1288688CC1

FASTA25027,637
        10         20         30         40         50         60 
MVMTNGKLIL LRHGQSAWNA SNQFTGWVDV DLTTIGEAEA KRGGELLVEN NVLPDVVYTS 

        70         80         90        100        110        120 
LLRRAIRTAN LALDAADRHW IPVVRDWRLN ERHYGALQGL NKAETKDKYG DEQYMAWRRS 

       130        140        150        160        170        180 
YGTPPPELAD DAEYSQAGDV RYKDLESVPR TECLKDVVER FIPYFEEEIL PRVKKGENVL 

       190        200        210        220        230        240 
IAAHGNSLRA LVKHLDNISD DDIAELNIPT GIPLVYEITP EGTVVNPGGT YLDPEAAAAG 

       250 
AAAVANQGGK

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000035 Genomic DNA. Translation: BAC17233.1.
RefSeqNP_737033.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FSH0.
SMRQ8FSH0. Positions 6-240.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1032545.
GenomeReviewsGene locus CE0423 in contig BA000035_GR.
KEGGcef:CE0423.
NMPDRfig|196164.1.peg.423.
PATRIC21487000. VBICorEff9312_0446.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG658938.
OMAEWNALNL.
PhylomeDBQ8FSH0.
ProtClustDBPRK14120.

Enzyme and pathway databases

BioCycCEFF196164:CE0423-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_COREF
AccessionPrimary (citable) accession number: Q8FSH0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 49 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

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