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A4YIX4 (APGM_METS5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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

Short name=BPG-independent PGAM
Short name=Phosphoglyceromutase
Short name=aPGAM
EC=5.4.2.1
Gene names
Name:apgM
Ordered Locus Names:Msed_2238
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP MF_01402_A

Catalytic activity

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

Pathway

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

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 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 – 4134132,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01402_A
PRO_1000073505

Sequences

Sequence LengthMass (Da)Tools
A4YIX4 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 21C3491B15C8BEDF

FASTA41344,562
        10         20         30         40         50         60 
MKKYKILLVI GDGLGDRQVA SLNGRTPLEN ADKPTIASLL RSSLVGLMDP IGPGIVPGSD 

        70         80         90        100        110        120 
TSHLAIFGLD PKKYYKGRGS FEALGAGAIL TEGDIAFRGN FATVDSNLVV IDRRAGRKIE 

       130        140        150        160        170        180 
EAEDLVKELN DKIQEIDGVK VRFYHGTEHR VSVVLSGDNL SDKVSDTDPH EVGKRILNSE 

       190        200        210        220        230        240 
PTDDALSSKR TANIINALTR RIYEVLSNSQ LNDKRVREGL PPANIVLLRG ASIHTELPKL 

       250        260        270        280        290        300 
KDYTGLSGAA VSATALIKGV CKSLGMEVVT PPGATGGIDT DYMAKAEAAA KLLEDHDLVF 

       310        320        330        340        350        360 
LHIKATDAAS HDGKVSEKVK AIEMIDRSIG RVLDRYGSEL VVLFTGDHAT PVELREHSGD 

       370        380        390        400        410 
PVPLMLYVPT NIIPDNVGDF NERQARKGSL KITGLNIIDL LLNFSNRATK YGA 

« Hide

References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed: 18083856] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000682 Genomic DNA. Translation: ABP96376.1.
RefSeqYP_001192300.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YIX4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4YIX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5104299.
GenomeReviewsGene locus Msed_2238 in contig CP000682_GR.
KEGGmse:Msed_2238.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04733.
HOGENOMHBG463247.
OMADIAFRCN.
ProtClustDBPRK04024.

Enzyme and pathway databases

BioCycMSED399549:MSED_2238-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 nameAPGM_METS5
AccessionPrimary (citable) accession number: A4YIX4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 33 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