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Reviewed, UniProtKB/Swiss-Prot A0B6L2 (APGM_METTP)

Last modified November 3, 2009. Version 21. 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: Mthe_0545
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length392 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 – 3923922,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01402
PRO_1000068384

Sequences

Sequence LengthMass (Da)Tools
A0B6L2-1 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 94EAEA1F1AEA025E

FASTA39242,413
        10         20         30         40         50         60 
MKYVVLLGDG MADWPMEALG GRTPLQVARK PNMDSIARIG RCGLARTVPE GMTPGSDVAN 

        70         80         90        100        110        120 
LSIMGYDPRR YYTGRAPLEA AAMRIPLGEK EVAFRCNFVT VMDGIMDDYS AGHITSEEGA 

       130        140        150        160        170        180 
EIAESLKKVI PGGRIYPGVS YRNIVVLKVC RDAVCTPPHD IMGKPISDHL PRGDDAHILI 

       190        200        210        220        230        240 
DIMERARPLL EEHPVNRRRV SMGLKPANMI WLWGQGPAPS MPRFHEIYGL KGAVISAVDL 

       250        260        270        280        290        300 
LKGLGVCAGW RVIDVPGATG TIDTNYAGKV RAALEALGSV DLVYLHIEAP DEAAHSGDVE 

       310        320        330        340        350        360 
QKIRAIELFD ERVVGPMIHG LERSGEAWRV LLLPDHPTPI EIRTHSTDPV PFAIAGSGVC 

       370        380        390 
VDSVDAFDEI SASEGGYGMI EGNDLIRLLI AG 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000477 Genomic DNA. Translation: ABK14336.1.
RefSeqYP_842976.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0B6L2.

Genome annotation databases

GeneID4463005.
GenomeReviewsGene locus Mthe_0545 in contig CP000477_GR.
KEGGmtp:Mthe_0545.
NMPDRfig|349307.7.peg.562.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAGATGYLD.

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_METTP
AccessionPrimary (citable) accession number: A0B6L2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 28, 2006
Last modified: November 3, 2009
This is version 21 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