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Reviewed, UniProtKB/Swiss-Prot Q8PX04 (APGM_METMA)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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: MM_1418
OrganismMethanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier2209 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

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.

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   Technical termComplete 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3973972,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01402
PRO_0000138137

Sequences

Sequence LengthMass (Da)Tools
Q8PX04-1 [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: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases

AE008384 Genomic DNA. Translation: AAM31114.1. Different initiation.
RefSeqNP_633442.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1479760.
GenomeReviewsGene locus MM_1418 in contig AE008384_GR.
KEGGmma:MM_1418.
NMPDRfig|192952.1.peg.1418.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8PX04.

Enzyme and pathway databases

BioCycMMAZ192952:MM1418-MON.
BRENDA5.4.2.1. 261165.

Family and domain databases

HAMAPMF_01402.
[Tree]
InterProIPR004456. APGAM_arc.
IPR019304. bisP-indep_Pglycerate_Mutase.
IPR013371. Homoserine_kin_put.
IPR006124. Metalloenzyme.
[Graphical view]
PfamPF01676. Metalloenzyme. 1 hit.
PF10143. PhosphMutase. 1 hit.
[Graphical view]
PIRSFPIRSF006392. IPGAM_arch. 1 hit.
ProDomPD004704. APGAM_DeoB. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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 16, 2009
This is version 44 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)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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