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Q8ZWV0

- PGMI_PYRAE

UniProt

Q8ZWV0 - PGMI_PYRAE

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
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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

    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 – 97
    Helixi10 – 145
    Beta strandi23 – 275
    Beta strandi30 – 334
    Beta strandi38 – 436
    Helixi46 – 6116
    Beta strandi65 – 717
    Beta strandi79 – 868
    Beta strandi88 – 903
    Helixi93 – 10412
    Beta strandi109 – 1157
    Helixi118 – 1203
    Beta strandi121 – 1233
    Beta strandi125 – 1273
    Helixi134 – 1374
    Helixi138 – 15316
    Helixi168 – 17811
    Beta strandi183 – 1875
    Helixi188 – 1903
    Helixi191 – 20313
    Beta strandi210 – 2145
    Helixi216 – 2194
    Helixi221 – 2244
    Beta strandi229 – 2335
    Beta strandi235 – 2373
    Helixi239 – 25214
    Beta strandi255 – 2584
    Helixi263 – 28422
    Helixi292 – 3009

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSQLLQDYLN WENYILRRVD FPTSYVVEGE VVRIEAMPRL YISGMGGSGV    50
    VADLIRDFSL TWNWEVEVIA VKDYFLKARD GLLIAVSYSG NTIETLYTVE 100
    YAKRRRIPAV AITTGGRLAQ MGVPTVIVPK ASAPRAALPQ LLTAALHVVA 150
    KVYGIDVKIP EGLEPPNEAL IHKLVEEFQK RPTIIAAESM RGVAYRVKNE 200
    FNENAKIEPS VEILPEAHHN WIEGSERAVV ALTSPHIPKE HQERVKATVE 250
    IVGGSIYAVE MHPKGVLSFL RDVGIASVKL AEIRGVNPLA TPRIDALKRR 300
    LQ 302
    Length:302
    Mass (Da):33,548
    Last modified:March 1, 2002 - v1
    Checksum:i853E7B8E4BA9AA21
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009441 Genomic DNA. Translation: AAL63599.1.
    RefSeqiNP_559417.1. NC_003364.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009441 Genomic DNA. Translation: AAL63599.1 .
    RefSeqi NP_559417.1. NC_003364.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 66 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