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Q8ZWV0 (PGMI_PYRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:
Bifunctional phosphoglucose/phosphomannose isomerase
Alternative name(s):
Glucose-6-phosphate isomerase
Short name=GPI
EC=5.3.1.9
Mannose-6-phosphate isomerase
EC=5.3.1.8
Phosphoglucose isomerase
Short name=PGI
Phosphomannose isomerase
Short name=PMI
Gene names
Ordered Locus Names:PAE1610
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827) [Reference proteome] [HAMAP]
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.

Catalytic activity

D-glucose 6-phosphate = D-fructose 6-phosphate.

D-mannose 6-phosphate = D-fructose 6-phosphate.

Enzyme regulation

Inhibited by 5-phosphoarabinonate (PAB) and 6-phosphogluconate.

Subunit structure

Homodimer. Ref.3

Miscellaneous

The lack of any movement in response to the binding of ligand may be due to its inherent thermostability, which would tend to restrict any flexibility in the protein.

Sequence similarities

Belongs to the PGI/PMI family.

Contains 1 SIS domain.

Biophysicochemical properties

Kinetic parameters:

KM=2.7 mM for glucose 6-phosphate (at 50 degrees Celsius) Ref.2

KM=0.3 mM for fructose 6-phosphate (at 50 degrees Celsius)

KM=1.9 mM for glucose 6-phosphate (at 80 degrees Celsius)

KM=0.06 mM for fructose 6-phosphate (at 80 degrees Celsius)

KM=0.49 mM for mannose 6-phosphate (at 80 degrees Celsius)

Vmax=50 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 50 degrees Celsius)

Vmax=31.3 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 50 degrees Celsius)

Vmax=150 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 80 degrees Celsius)

Vmax=109 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 80 degrees Celsius)

Vmax=117 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at 80 degrees Celsius)

pH dependence:

Optimum pH is 7.4.

Temperature dependence:

Optimum temperature is 100 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Bifunctional phosphoglucose/phosphomannose isomerase
PRO_0000227794

Regions

Domain27 – 160134SIS

Sites

Active site2031Proton acceptor Probable
Active site2191Proton donor Probable
Active site2981Proton acceptor Probable
Binding site481Substrate
Binding site871Substrate
Binding site921Substrate

Secondary structure

...................................................... 302
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8ZWV0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 853E7B8E4BA9AA21

FASTA30233,548
        10         20         30         40         50         60 
MSQLLQDYLN WENYILRRVD FPTSYVVEGE VVRIEAMPRL YISGMGGSGV VADLIRDFSL 

        70         80         90        100        110        120 
TWNWEVEVIA VKDYFLKARD GLLIAVSYSG NTIETLYTVE YAKRRRIPAV AITTGGRLAQ 

       130        140        150        160        170        180 
MGVPTVIVPK ASAPRAALPQ LLTAALHVVA KVYGIDVKIP EGLEPPNEAL IHKLVEEFQK 

       190        200        210        220        230        240 
RPTIIAAESM RGVAYRVKNE FNENAKIEPS VEILPEAHHN WIEGSERAVV ALTSPHIPKE 

       250        260        270        280        290        300 
HQERVKATVE IVGGSIYAVE MHPKGVLSFL RDVGIASVKL AEIRGVNPLA TPRIDALKRR 


LQ 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.
[2]"Bifunctional phosphoglucose/phosphomannose isomerase from the hyperthermophilic archaeon Pyrobaculum aerophilum."
Hansen T., Urbanke C., Schoenheit P.
Extremophiles 8:507-512(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
[3]"A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolution."
Swan M.K., Hansen T., Schoenheit P., Davies C.
J. Biol. Chem. 279:39838-39845(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH 5-PHOSPHOARABINONATE, ISOMERIZATION MECHANISM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009441 Genomic DNA. Translation: AAL63599.1.
RefSeqNP_559417.1. NC_003364.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TZBX-ray1.16A/B1-302[»]
1TZCX-ray1.45A/B1-302[»]
1X9HX-ray1.50A/B1-302[»]
1X9IX-ray1.16A/B1-302[»]
ProteinModelPortalQ8ZWV0.
SMRQ8ZWV0. Positions 2-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING178306.PAE1610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL63599; AAL63599; PAE1610.
GeneID1465847.
KEGGpai:PAE1610.

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000222946.
KOK15916.
OMANWIEGSE.

Enzyme and pathway databases

BioCycPAER178306:GCEO-1140-MONOMER.
SABIO-RKQ8ZWV0.

Family and domain databases

InterProIPR011857. Glu6P/Mann6P_isomerase.
IPR019490. Glu6P/Mann6P_isomerase_C.
IPR001347. SIS.
[Graphical view]
PfamPF10432. bact-PGI_C. 1 hit.
PF01380. SIS. 1 hit.
[Graphical view]
TIGRFAMsTIGR02128. G6PI_arch. 1 hit.
PROSITEPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8ZWV0.

Entry information

Entry namePGMI_PYRAE
AccessionPrimary (citable) accession number: Q8ZWV0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 65 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references