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Q9HIC2 (PGMI_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:Ta1419
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length310 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 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 Ref.2

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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
[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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445067 Genomic DNA. Translation: CAC12539.1.
RefSeqNP_394873.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HIC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta1419.

Proteomic databases

PRIDEQ9HIC2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12539; CAC12539; CAC12539.
GeneID1456878.
KEGGtac:Ta1419.

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000020037.
KOK15916.
OMAIAERWKG.

Enzyme and pathway databases

BRENDA5.3.1.8. 6324.
SABIO-RKQ9HIC2.

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...

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: 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