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Reviewed, UniProtKB/Swiss-Prot O26518 (APGM2_METTH)

Last modified November 3, 2009. Version 53. 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 2
      Short name=Phosphoglyceromutase 2
      Short name=BPG-independent PGAM 2
      Short name=aPGAM 2
    EC=5.4.2.1
Gene names
Name: apgM2
Ordered Locus Names: MTH_418
OrganismMethanobacterium thermoautotrophicum [Complete proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length402 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 – 4024022,3-bisphosphoglycerate-independent phosphoglycerate mutase 2 HAMAP MF_01402
PRO_0000138140

Sequences

Sequence LengthMass (Da)Tools
O26518-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: EB5EF3B8A18E7617

FASTA40244,100
        10         20         30         40         50         60 
MITMKHVILV GDGMADYPLD ELDGKTPLQV ADKPNMDQLA GMGACGLLRT VPEGMEAGSD 

        70         80         90        100        110        120 
VANLSIMGYD PRRYYTGRGP LEAASIGVEL GDDDVAFRCN LINADERIVD FNAGHIETAE 

       130        140        150        160        170        180 
ASSLIDALNH ELETRGRFYA GVSYRNLFVI EGRGYTSVRV EPPHDIVGES VAAHLPSGSE 

       190        200        210        220        230        240 
EADHIRELML ESAGVLRSHE VNLKRESMGK RPATMIWLWG QGLRPSMEPF SERYGIRGAT 

       250        260        270        280        290        300 
ITAVDLIKGL GVYAGLENIH VPGATGYLDT DYRAKGRYAA GALEEYDFLY VHVEAPDEAG 

       310        320        330        340        350        360 
HAGDAEEKIR AIENIDRFVL GRLLDALSDH EHRIAVLPDH PTPIEIRTHV PDPVPCILAG 

       370        380        390        400 
DGVDADQVKS YDEFTVREGS LGTWEAHRLM EIMMDPAARL RQ 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Delta H.

Cross-references

Sequence databases

AE000666 Genomic DNA. Translation: AAB84924.1.
PIRD69154.
RefSeqNP_275561.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO26518.

Genome annotation databases

GeneID1470379.
GenomeReviewsGene locus MTH_418 in contig AE000666_GR.
KEGGmth:MTH418.
NMPDRfig|187420.1.peg.416.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO26518.
OMAGATGYLD.

Enzyme and pathway databases

BioCycMTHE187420:MTH418-MON.
BRENDA5.4.2.1. 270.

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 nameAPGM2_METTH
AccessionPrimary (citable) accession number: O26518
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: January 1, 1998
Last modified: November 3, 2009
This is version 53 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