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Reviewed, UniProtKB/Swiss-Prot Q9HL27 (APGM_THEAC)

Last modified February 9, 2010. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase
      Short name=Phosphoglyceromutase
      Short name=BPG-independent PGAM
      Short name=aPGAM
    EC=5.4.2.1
Gene names
Name: apgM
Ordered Locus Names: Ta0413
OrganismThermoplasma acidophilum [Complete proteome] [HAMAP]
Taxonomic identifier2303 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma

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Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP MF_01402

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01402

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01402

Sequence similarities

Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.

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Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: HAMAP

metal ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4044042,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01402
PRO_0000138150

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Sequences

Sequence LengthMass (Da)Tools
Q9HL27-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 06C0306580FE8BDF

FASTA40443,933
        10         20         30         40         50         60 
MMKSIILIVL DGLGDRPGSD LQNRTPLQAA FRPNLNWLAS HGINGIMHPI SPGIRCGSDT 

        70         80         90        100        110        120 
SHMSLLGYDP KVYYPGRGPF EALGLGMDIR PGDLAFRANF ATNRDGVIVD RRAGRENKGN 

       130        140        150        160        170        180 
EELADAISLD MGEYSFRVKS GVEHRAALVV SGPDLSDMIG DSDPHREGLP PEKIRPTDPS 

       190        200        210        220        230        240 
GDRTAEVMNA YLEEARRILS DHRVNKERVK NGRLPGNELL VRSAGKVPAI PSFTEKNRMK 

       250        260        270        280        290        300 
GACVVGSPWL KGLCRLLRMD VFDVPGATGT VGSNYRGKIE KAVDLTSSHD FVLVNIKATD 

       310        320        330        340        350        360 
VAGHDGNYPL KRDVIEDIDR AMEPLKSIGD HAVICVTGDH STPCSFKDHS GDPVPIVFYT 

       370        380        390        400 
DGVMNDGVHL FDELSSASGS LRITSYNVMD ILMQLAGRSD KFGS

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References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed: 11029001] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / AMRC-C165 / DSM 1728 / IFO 15155 / JCM 9062.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL445064 Genomic DNA. Translation: CAC11555.1.
RefSeqNP_393891.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IDDX-ray2.80A/B1-404[»]
3KD8X-ray2.60A/B2-397[»]
ModBaseSearch...

Genome annotation databases

GeneID1456023.
KEGGtac:Ta0413.
NMPDRfig|273075.1.peg.413.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG463247.
OMAITGDHST.

Enzyme and pathway databases

BioCycTACI273075:TA0413-MONOMER.
BRENDA5.4.2.1. 435.

Family and domain databases

HAMAPMF_01402_A. ApgM_A.
[Tree]
InterProIPR017850. Alkaline_phosphatase_core.
IPR004456. APGAM_arc.
IPR019304. bisP-indep_Pglycerate_Mutase.
IPR006124. Metalloenzyme.
[Graphical view]
PfamPF01676. Metalloenzyme. 1 hit.
PF10143. PhosphMutase. 1 hit.
[Graphical view]
PIRSFPIRSF006392. IPGAM_arch. 1 hit.
TIGRFAMsTIGR00306. apgM. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameAPGM_THEAC
AccessionPrimary (citable) accession number: Q9HL27
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: March 1, 2001
Last modified: February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents