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Protein

Bifunctional phosphoglucose/phosphomannose isomerase

Gene

PAE1610

Organism
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

Kineticsi

  1. KM=2.7 mM for glucose 6-phosphate (at 50 degrees Celsius)1 Publication
  2. KM=0.3 mM for fructose 6-phosphate (at 50 degrees Celsius)1 Publication
  3. KM=1.9 mM for glucose 6-phosphate (at 80 degrees Celsius)1 Publication
  4. KM=0.06 mM for fructose 6-phosphate (at 80 degrees Celsius)1 Publication
  5. KM=0.49 mM for mannose 6-phosphate (at 80 degrees Celsius)1 Publication
  1. Vmax=50 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 50 degrees Celsius)1 Publication
  2. Vmax=31.3 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 50 degrees Celsius)1 Publication
  3. Vmax=150 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 80 degrees Celsius)1 Publication
  4. Vmax=109 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 80 degrees Celsius)1 Publication
  5. Vmax=117 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at 80 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.4.1 Publication

Temperature dependencei

Optimum temperature is 100 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei48Substrate1
Binding sitei87Substrate1
Binding sitei92Substrate1
Active sitei203Proton acceptorCurated1
Active sitei219Proton donorCurated1
Active sitei298Proton acceptorCurated1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BRENDAi5.3.1.8. 5239.
5.3.1.9. 5239.
SABIO-RKQ8ZWV0.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional phosphoglucose/phosphomannose isomerase
Alternative name(s):
Glucose-6-phosphate isomerase (EC:5.3.1.9)
Short name:
GPI
Mannose-6-phosphate isomerase (EC:5.3.1.8)
Phosphoglucose isomerase
Short name:
PGI
Phosphomannose isomerase
Short name:
PMI
Gene namesi
Ordered Locus Names:PAE1610
OrganismiPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Taxonomic identifieri178306 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
Proteomesi
  • UP000002439 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002277941 – 302Bifunctional phosphoglucose/phosphomannose isomeraseAdd BLAST302

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi178306.PAE1610.

Structurei

Secondary structure

1302
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 9Combined sources7
Helixi10 – 14Combined sources5
Beta strandi23 – 27Combined sources5
Beta strandi30 – 33Combined sources4
Beta strandi38 – 43Combined sources6
Helixi46 – 61Combined sources16
Beta strandi65 – 71Combined sources7
Beta strandi79 – 86Combined sources8
Beta strandi88 – 90Combined sources3
Helixi93 – 104Combined sources12
Beta strandi109 – 115Combined sources7
Helixi118 – 120Combined sources3
Beta strandi121 – 123Combined sources3
Beta strandi125 – 127Combined sources3
Helixi134 – 137Combined sources4
Helixi138 – 153Combined sources16
Helixi168 – 178Combined sources11
Beta strandi183 – 187Combined sources5
Helixi188 – 190Combined sources3
Helixi191 – 203Combined sources13
Beta strandi210 – 214Combined sources5
Helixi216 – 219Combined sources4
Helixi221 – 224Combined sources4
Beta strandi229 – 233Combined sources5
Beta strandi235 – 237Combined sources3
Helixi239 – 252Combined sources14
Beta strandi255 – 258Combined sources4
Helixi263 – 284Combined sources22
Helixi292 – 300Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TZBX-ray1.16A/B1-302[»]
1TZCX-ray1.45A/B1-302[»]
1X9HX-ray1.50A/B1-302[»]
1X9IX-ray1.16A/B1-302[»]
ProteinModelPortaliQ8ZWV0.
SMRiQ8ZWV0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ZWV0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 160SISPROSITE-ProRule annotationAdd BLAST134

Sequence similaritiesi

Belongs to the PGI/PMI family.Curated
Contains 1 SIS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG00052. Archaea.
COG0166. LUCA.
HOGENOMiHOG000222946.
InParanoidiQ8ZWV0.
KOiK15916.
OMAiHHNWIEG.

Family and domain databases

InterProiIPR011857. Glu6P/Mann6P_isomerase.
IPR019490. Glu6P/Mann6P_isomerase_C.
IPR001347. SIS.
[Graphical view]
PfamiPF10432. bact-PGI_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02128. G6PI_arch. 1 hit.
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8ZWV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLLQDYLN WENYILRRVD FPTSYVVEGE VVRIEAMPRL YISGMGGSGV
60 70 80 90 100
VADLIRDFSL TWNWEVEVIA VKDYFLKARD GLLIAVSYSG NTIETLYTVE
110 120 130 140 150
YAKRRRIPAV AITTGGRLAQ MGVPTVIVPK ASAPRAALPQ LLTAALHVVA
160 170 180 190 200
KVYGIDVKIP EGLEPPNEAL IHKLVEEFQK RPTIIAAESM RGVAYRVKNE
210 220 230 240 250
FNENAKIEPS VEILPEAHHN WIEGSERAVV ALTSPHIPKE HQERVKATVE
260 270 280 290 300
IVGGSIYAVE MHPKGVLSFL RDVGIASVKL AEIRGVNPLA TPRIDALKRR

LQ
Length:302
Mass (Da):33,548
Last modified:March 1, 2002 - v1
Checksum:i853E7B8E4BA9AA21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009441 Genomic DNA. Translation: AAL63599.1.

Genome annotation databases

EnsemblBacteriaiAAL63599; AAL63599; PAE1610.
KEGGipai:PAE1610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009441 Genomic DNA. Translation: AAL63599.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TZBX-ray1.16A/B1-302[»]
1TZCX-ray1.45A/B1-302[»]
1X9HX-ray1.50A/B1-302[»]
1X9IX-ray1.16A/B1-302[»]
ProteinModelPortaliQ8ZWV0.
SMRiQ8ZWV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi178306.PAE1610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL63599; AAL63599; PAE1610.
KEGGipai:PAE1610.

Phylogenomic databases

eggNOGiarCOG00052. Archaea.
COG0166. LUCA.
HOGENOMiHOG000222946.
InParanoidiQ8ZWV0.
KOiK15916.
OMAiHHNWIEG.

Enzyme and pathway databases

BRENDAi5.3.1.8. 5239.
5.3.1.9. 5239.
SABIO-RKQ8ZWV0.

Miscellaneous databases

EvolutionaryTraceiQ8ZWV0.

Family and domain databases

InterProiIPR011857. Glu6P/Mann6P_isomerase.
IPR019490. Glu6P/Mann6P_isomerase_C.
IPR001347. SIS.
[Graphical view]
PfamiPF10432. bact-PGI_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02128. G6PI_arch. 1 hit.
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGMI_PYRAE
AccessioniPrimary (citable) accession number: Q8ZWV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2002
Last modified: November 2, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.