Bifunctional phosphoglucose/phosphomannose isomerase

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Reviewed, UniProtKB/Swiss-Prot Q8ZWV0 (PGMI_PYRAE)

Last modified February 9, 2010. Version 44. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended 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:

PAE1610

Organism

Pyrobaculum aerophilum [Complete proteome] [HAMAP]

Taxonomic identifier

13773 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum

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Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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: K_M=2.7 mM for glucose 6-phosphate (at 50 degrees Celsius) K_M=0.3 mM for fructose 6-phosphate (at 50 degrees Celsius) K_M=1.9 mM for glucose 6-phosphate (at 80 degrees Celsius) K_M=0.06 mM for fructose 6-phosphate (at 80 degrees Celsius) K_M=0.49 mM for mannose 6-phosphate (at 80 degrees Celsius) V_max=50 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 50 degrees Celsius) V_max=31.3 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 50 degrees Celsius) V_max=150 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 80 degrees Celsius) V_max=109 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 80 degrees Celsius) V_max=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.

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Ontologies

Keywords
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	glucose-6-phosphate isomerase activity Inferred from electronic annotation. Source: EC mannose-6-phosphate isomerase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 302

302

Bifunctional phosphoglucose/phosphomannose isomerase

PRO_0000227794

Regions

Domain

27 – 160

134

SIS

Sites

Active site

203

Proton acceptor Probable

Active site

219

Proton donor Probable

Active site

298

Proton acceptor Probable

Binding site

Substrate

Binding site

Substrate

Binding site

Substrate

Secondary structure

302

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8ZWV0-1 [UniParc].

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

302

33,548

        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

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References

	« Hide 'large scale' referencesShow '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: 11792869] [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: 15290326] [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: 15252053] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH 5-PHOSPHOARABINONATE, ISOMERIZATION MECHANISM.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE009441 Genomic DNA. Translation: AAL63599.1.

RefSeq

NP_559417.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TZB	X-ray	1.16	A/B	1-302	[»]
1TZC	X-ray	1.45	A/B	1-302	[»]
1X9H	X-ray	1.50	A/B	1-302	[»]
1X9I	X-ray	1.16	A/B	1-302	[»]

ModBase

Search...

Genome annotation databases

GeneID

1465847.

GenomeReviews

Gene locus PAE1610 in contig AE009441_GR.

KEGG

pai:PAE1610.

NMPDR

fig|178306.1.peg.1107.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG646630.

OMA

AYRVKNE.

Enzyme and pathway databases

BioCyc

PAER178306:PAE1610-MONOMER.

BRENDA

5.3.1.8. 142830.
5.3.1.9. 142830.

Family and domain databases

InterPro

IPR011857. Glu6P/Mann6P_isomerase.
IPR019490. Glu6P/Mann6P_isomerase_C.
IPR001347. SIS.
[Graphical view]

Pfam

PF10432. bact-PGI_C. 1 hit.
PF01380. SIS. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02128. G6PI_arch. 1 hit.

PROSITE

PS51464. SIS. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

PGMI_PYRAE

Accession

Primary (citable) accession number: Q8ZWV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	March 1, 2002
Last modified:	February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families