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Q8ZWV0

- PGMI_PYRAE

UniProt

Q8ZWV0 - PGMI_PYRAE

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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: 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

Vmax=50 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 50 degrees Celsius)1 Publication

Vmax=31.3 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 50 degrees Celsius)1 Publication

Vmax=150 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 80 degrees Celsius)1 Publication

Vmax=109 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 80 degrees Celsius)1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481Substrate
Binding sitei87 – 871Substrate
Binding sitei92 – 921Substrate
Active sitei203 – 2031Proton acceptorCurated
Active sitei219 – 2191Proton donorCurated
Active sitei298 – 2981Proton acceptorCurated

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. glucose-6-phosphate isomerase activity Source: UniProtKB-EC
  3. mannose-6-phosphate isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciPAER178306:GCEO-1140-MONOMER.
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
ProteomesiUP000002439: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Bifunctional phosphoglucose/phosphomannose isomerasePRO_0000227794Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi178306.PAE1610.

Structurei

Secondary structure

1
302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97Combined sources
Helixi10 – 145Combined sources
Beta strandi23 – 275Combined sources
Beta strandi30 – 334Combined sources
Beta strandi38 – 436Combined sources
Helixi46 – 6116Combined sources
Beta strandi65 – 717Combined sources
Beta strandi79 – 868Combined sources
Beta strandi88 – 903Combined sources
Helixi93 – 10412Combined sources
Beta strandi109 – 1157Combined sources
Helixi118 – 1203Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi125 – 1273Combined sources
Helixi134 – 1374Combined sources
Helixi138 – 15316Combined sources
Helixi168 – 17811Combined sources
Beta strandi183 – 1875Combined sources
Helixi188 – 1903Combined sources
Helixi191 – 20313Combined sources
Beta strandi210 – 2145Combined sources
Helixi216 – 2194Combined sources
Helixi221 – 2244Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi235 – 2373Combined sources
Helixi239 – 25214Combined sources
Beta strandi255 – 2584Combined sources
Helixi263 – 28422Combined sources
Helixi292 – 3009Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ZWV0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 160134SISPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0166.
HOGENOMiHOG000222946.
InParanoidiQ8ZWV0.
KOiK15916.
OMAiNWIEGSE.

Family and domain databases

InterProiIPR011857. Glu6P/Mann6P_isomerase.
IPR019490. Glu6P/Mann6P_isomerase_C.
IPR001347. SIS.
[Graphical view]
PfamiPF10432. bact-PGI_C. 1 hit.
PF01380. SIS. 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.
RefSeqiNP_559417.1. NC_003364.1.
WP_011008072.1. NC_003364.1.

Genome annotation databases

EnsemblBacteriaiAAL63599; AAL63599; PAE1610.
GeneIDi1465847.
KEGGipai:PAE1610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009441 Genomic DNA. Translation: AAL63599.1 .
RefSeqi NP_559417.1. NC_003364.1.
WP_011008072.1. NC_003364.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q8ZWV0.
SMRi Q8ZWV0. Positions 2-302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 178306.PAE1610.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL63599 ; AAL63599 ; PAE1610 .
GeneIDi 1465847.
KEGGi pai:PAE1610.

Phylogenomic databases

eggNOGi COG0166.
HOGENOMi HOG000222946.
InParanoidi Q8ZWV0.
KOi K15916.
OMAi NWIEGSE.

Enzyme and pathway databases

BioCyci PAER178306:GCEO-1140-MONOMER.
SABIO-RK Q8ZWV0.

Miscellaneous databases

EvolutionaryTracei Q8ZWV0.

Family and domain databases

InterProi IPR011857. Glu6P/Mann6P_isomerase.
IPR019490. Glu6P/Mann6P_isomerase_C.
IPR001347. SIS.
[Graphical view ]
Pfami PF10432. bact-PGI_C. 1 hit.
PF01380. SIS. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02128. G6PI_arch. 1 hit.
PROSITEi PS51464. SIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH 5-PHOSPHOARABINONATE, ISOMERIZATION MECHANISM.

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 26, 2014
This is version 68 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

External Data

Dasty 3