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O28523 (APGM1_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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-independent phosphoglycerate mutase 1
Short name=BPG-independent PGAM 1
Short name=Phosphoglyceromutase 1
Short name=aPGAM 1
EC=5.4.2.1
Gene names
Name:apgM1
Ordered Locus Names:AF_1751
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. Ref.2

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01402_A

Cofactor

Manganese. The activity is stimulated by 50 µM of manganese in the presence of 5 mM of magnesium. Ref.2

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01402_A

Subunit structure

Monomer. Ref.2

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.8 mM for 3-phosphoglycerate Ref.2

KM=0.2 mM for 2-phosphoglycerate

Vmax=3.3 µmol/min/mg enzyme toward 3-phosphoglycerate

Vmax=0.8 µmol/min/mg enzyme toward 2-phosphoglycerate

pH dependence:

Optimum pH is 7.1.

Temperature dependence:

Optimum temperature is 60 degrees Celsius. Does not lose activity after 120 minutes at 60 degrees Celsius at pH7 with 50 µM of manganese chloride and 5 mM of magnesium chloride.

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglycerate mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4084082,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 HAMAP MF_01402_A
PRO_0000138131

Sequences

Sequence LengthMass (Da)Tools
O28523 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 5A2228F3264B370E

FASTA40844,096
        10         20         30         40         50         60 
MPVLLIVVDG LSDRPIDGKT PLSVARKPNL DRLAEMGING IMDTIAPGIR PGSDTSHLAL 

        70         80         90        100        110        120 
LGYDPYKYYS GRGPIEAAGV GIEIKPGDVA FRANFATVEG EGSIFDKTVV DRRAGRIEDT 

       130        140        150        160        170        180 
SELIKALREI ELPVELLVER GTGHRAAVVF RGEGLSDRVS DTDPKAVGKK VKRCVPLADD 

       190        200        210        220        230        240 
AKAKKTAEIV NEFMQKAHEV LENHPLNRER AEKGLLKANA LLLRGAGEMP HVPSFKDKTG 

       250        260        270        280        290        300 
LRLCVIAATA LIKGVGRVVG ADVITPEGAT GNKNTNLEAK VKAAINALES YDVVLLHIKA 

       310        320        330        340        350        360 
TDELGHDGDF EGKKAFIEKL DEKIAPLLDL DFSKTCLILT ADHSTPIKVK DHTADPVPVV 

       370        380        390        400 
IVHEDVRRDE VSSFSEFEAY KGGLCRIRGM DLLNIALDLL NIAKKFGA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000782 Genomic DNA. Translation: AAB89499.1.
PIRF69468.
RefSeqNP_070579.1. NC_000917.1.

3D structure databases

ProteinModelPortalO28523.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1484974.
GenomeReviewsGene locus AF_1751 in contig AE000782_GR.
KEGGafu:AF1751.
NMPDRfig|224325.1.peg.1740.
TIGRAF_1751.

Phylogenomic databases

HOGENOMHBG463247.
OMADIAFRCN.
ProtClustDBPRK04024.

Enzyme and pathway databases

BioCycAFUL224325:AF_1751-MONOMER.

Family and domain databases

HAMAPMF_01402_A. ApgM_A.
[Tree]
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR023665. ApgAM.
IPR004456. BisP-indep_Pglycerate_Mutase.
IPR006124. Metalloenzyme.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 2 hits.
KOK15635.
PfamPF01676. Metalloenzyme. 1 hit.
PF10143. PhosphMutase. 1 hit.
[Graphical view]
PIRSFPIRSF006392. IPGAM_arch. 1 hit.
SUPFAMSSF53649. Alkaline_phosphatase_core. 1 hit.
TIGRFAMsTIGR00306. ApgM. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPGM1_ARCFU
AccessionPrimary (citable) accession number: O28523
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 70 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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