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Reviewed, UniProtKB/Swiss-Prot Q9HIC2 (PGMI_THEAC)

Last modified November 3, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Bifunctional phosphoglucose/phosphomannose isomerase
Alternative name(s):
    Glucose-6-phosphate isomerase
      Short name=GPI
    EC=5.3.1.9
    Phosphoglucose isomerase
      Short name=PGI
    Mannose-6-phosphate isomerase
    EC=5.3.1.8
    Phosphomannose isomerase
      Short name=PMI
Gene names
Ordered Locus Names: Ta1419
OrganismThermoplasma acidophilum [Complete proteome] [HAMAP]
Taxonomic identifier2303 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 erythrose 4-phosphate and 6-phosphogluconate.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the PGI/PMI family.

Contains 1 SIS domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.72 mM for glucose 6-phosphate

KM=0.2 mM for fructose 6-phosphate

KM=0.25 mM for mannose 6-phosphate

Vmax=83 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 50 degrees Celsius)

Vmax=57 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 50 degrees Celsius)

Vmax=75 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at 50 degrees Celsius)

pH dependence:

Optimum pH is 7.6.

Temperature dependence:

Optimum temperature is 75 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Bifunctional phosphoglucose/phosphomannose isomerase
PRO_0000227545

Regions

Domain22 – 152131SIS

Sites

Active site2021Proton acceptor By similarity
Active site2181Proton donor By similarity
Active site3061Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HIC2-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A88423F901339B1F

FASTA31035,045
        10         20         30         40         50         60 
MLRSHCMEFS EELKTLKDQV RFDGSFRTGT FSNIVIAGMG GSGIAGRIFS EMYSAKPVFV 

        70         80         90        100        110        120 
CDDYHIPEFV DGNTEFIAVS YSGNTEETLS AAEEAIKKGA KVHAITSGGR LSEMGVDTIK 

       130        140        150        160        170        180 
IPGGLQPRSA VGYLTMPIIN TFIRPKHEDI EEAAGLLSDL DKNNTVQENI ATEIYAGRRI 

       190        200        210        220        230        240 
PVIYGSTPYR SVAYRWKTQF NENAKILAYS NYFSELNHND TMPLRDTYRK DEFYFMAFDS 

       250        260        270        280        290        300 
TDERIRKRIE VTQKITGTSF KKIEARGSSL IARIFYLIHF GDYVTYHLAR IRNVDPQDVS 

       310 
AIEDLKKRIS 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed: 11029001] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / AMRC-C165 / DSM 1728 / IFO 15155 / JCM 9062.
[2]"Bifunctional phosphoglucose/phosphomannose isomerases from the archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily."
Hansen T., Wendor ff D., Schoenheit P.
J. Biol. Chem. 279:2262-2272(2004) [PubMed: 14551194] [Abstract]
Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

AL445067 Genomic DNA. Translation: CAC12539.1.
RefSeqNP_394873.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1456878.
GenomeReviewsGene locus Ta1419 in contig AL139299_GR.
KEGGtac:Ta1419.
NMPDRfig|273075.1.peg.1395.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9HIC2.
OMAGNTEETL.

Enzyme and pathway databases

BioCycTACI273075:TA1419-MON.
BRENDA5.3.1.8. 435.
5.3.1.9. 435.

Family and domain databases

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

Entry information

Entry namePGMI_THEAC
AccessionPrimary (citable) accession number: Q9HIC2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2001
Last modified: November 3, 2009
This is version 40 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

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