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Q8PX04 (APGM_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Short name=BPG-independent PGAM
Short name=Phosphoglyceromutase
Short name=aPGAM
EC=5.4.2.12
Gene names
Name:apgM
Ordered Locus Names:MM_1418
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length397 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_01402_A

Catalytic activity

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

Pathway

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

Sequence similarities

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

Sequence caution

The sequence AAM31114.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglycerate mutase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3973972,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01402_A
PRO_0000138137

Sequences

Sequence LengthMass (Da)Tools
Q8PX04 [UniParc].

Last modified October 10, 2002. Version 1.
Checksum: FFB8BC932E9E15EC

FASTA39743,175
        10         20         30         40         50         60 
MKYAILIGDG MADYPIEKLG NRTILQAART PAMDSIAARG RAGLAKTVPD SFPPGSDVAN 

        70         80         90        100        110        120 
MSILGYDPAT YYSGRAPLEA ASMGVALAAD DVAFRCNLIT TEHGMIKDYS AGHISSDEAE 

       130        140        150        160        170        180 
ILIDTLDYEL STENIRFYPG ISYRHLIVAG NNLGAETECT PPHDITGEKI DKYLPRGKDG 

       190        200        210        220        230        240 
EFFSELIEAS KVVLELHPVN LKRVEEGKNP ANSIWVWGQG YAPKFTAFMK LYGKKGAVIS 

       250        260        270        280        290        300 
AVDLLKGIGI YAGLDVIEVH GATGYLDTNY EGKVRAAIEA LKTRDLVFVH VEAPDEAGHE 

       310        320        330        340        350        360 
GSIEKKLKAV EDFDSRIVAP ILEYAENSDE PFTILVLPDH PTPISVKTHT RDPIPFAIYR 

       370        380        390 
TDKPETDNVE AFDEESVKNG SMGLVKASDL IGILIKS 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM31114.1. Different initiation.
RefSeqNP_633442.2. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PX04.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192952.MM_1418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM31114; AAM31114; MM_1418.
GeneID1479760.
KEGGmma:MM_1418.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3635.
HOGENOMHOG000004785.
KOK15635.
OMAYRHLMVW.

Enzyme and pathway databases

BioCycMMAZ192952:GCK2-1456-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.720.10. 2 hits.
HAMAPMF_01402_A. ApgM_A.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR023665. ApgAM.
IPR004456. BisP-indep_Pglycerate_Mutase.
IPR013371. Homoserine_kinase_put.
IPR006124. Metalloenzyme.
[Graphical view]
PfamPF01676. Metalloenzyme. 1 hit.
PF10143. PhosphMutase. 1 hit.
[Graphical view]
PIRSFPIRSF006392. IPGAM_arch. 1 hit.
SUPFAMSSF53649. SSF53649. 2 hits.
TIGRFAMsTIGR00306. apgM. 1 hit.
TIGR02535. hyp_Hser_kinase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPGM_METMA
AccessionPrimary (citable) accession number: Q8PX04
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: June 11, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways