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Q9YE01 (PGMI_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:APE_0768.1
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length333 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=3.5 mM for glucose 6-phosphate Ref.2

KM=0.44 mM for fructose 6-phosphate

KM=1.1 mM for mannose 6-phosphate

Vmax=225 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 80 degrees Celsius)

Vmax=195 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 80 degrees Celsius)

Vmax=209 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at 80 degrees Celsius)

pH dependence:

Optimum pH is 7.6.

Temperature dependence:

Optimum temperature is above 98 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Bifunctional phosphoglucose/phosphomannose isomerase
PRO_0000227544

Regions

Domain22 – 160139SIS

Sites

Active site2111Proton acceptor By similarity
Active site2271Proton donor By similarity
Active site3221Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YE01 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 3E94DE8CCF7E5DC3

FASTA33335,942
        10         20         30         40         50         60 
MEDLYLSWPK WFSEALARYS SLEGALEGVE EIYYCGMGGS GAAGDYIEAL LSIYAPQGPE 

        70         80         90        100        110        120 
FRVVKDFRPP RPPRHRGYGL VLASYSGNTL ETVECGSLLS PAAGRVVAVT SGGRLLEMAK 

       130        140        150        160        170        180 
ERGWLVARLP GGILPRVSFP WMLAASTAML SGALGVDLEA LKRLAGGLDT QGLKGEAERL 

       190        200        210        220        230        240 
AGFISRYRIA SLVTCGPGIP LAVRLKNELA ENAKMPSRLE IYPESSHNDI VALEAAEGLY 

       250        260        270        280        290        300 
GAVFIWIEHE GSLCPAVLDV VEGIYREYGV DTISIESSAR GGPNATVAEY LSRTLVFGLA 

       310        320        330 
SVRLALMRGF NPEETPPIDK YKRRLGEALR SQA 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
[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.
Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA79746.2.
PIRB72668.
RefSeqNP_147479.2. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YE01.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_0768.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA79746; BAA79746; APE_0768.1.
GeneID1444882.
KEGGape:APE_0768.1.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000222946.
KOK15916.
ProtClustDBPRK08674.

Enzyme and pathway databases

BioCycAPER272557:GJD6-558-MONOMER.
BRENDA5.3.1.8. 171.
SABIO-RKQ9YE01.

Family and domain databases

InterProIPR011857. Glu6P/Mann6P_isomerase.
IPR019490. Glu6P/Mann6P_isomerase_C.
IPR001347. SIS.
[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_AERPE
AccessionPrimary (citable) accession number: Q9YE01
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: June 26, 2007
Last modified: October 16, 2013
This is version 61 of the entry and version 2 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