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P46237

- GUNC_FUSOX

UniProt

P46237 - GUNC_FUSOX

Protein

Endoglucanase type C

Gene
N/A
Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei215 – 2151NucleophileBy similarity
    Active sitei220 – 2201Proton donorBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH7. Glycoside Hydrolase Family 7.
    mycoCLAPiEGL7A_FUSOX.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase type C (EC:3.2.1.4)
    Alternative name(s):
    Cellulase
    Endo-1,4-beta-glucanase
    Endoglucanase I
    Short name:
    EG I
    OrganismiFusarium oxysporum (Fusarium vascular wilt)
    Taxonomic identifieri5507 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium oxysporum species complex

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Chaini19 – 429411Endoglucanase type CPRO_0000007912Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Pyrrolidone carboxylic acid
    Disulfide bondi36 ↔ 42
    Disulfide bondi66 ↔ 88
    Glycosylationi74 – 741N-linked (GlcNAc...)
    Disulfide bondi78 ↔ 84
    Disulfide bondi156 ↔ 383
    Disulfide bondi190 ↔ 213
    Disulfide bondi194 ↔ 212
    Disulfide bondi233 ↔ 252
    Disulfide bondi241 ↔ 246
    Disulfide bondi257 ↔ 333
    Glycosylationi265 – 2651N-linked (GlcNAc...)
    Glycosylationi318 – 3181N-linked (GlcNAc...)

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Structurei

    Secondary structure

    1
    429
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 378
    Turni38 – 403
    Beta strandi41 – 5111
    Helixi53 – 564
    Turni75 – 773
    Helixi81 – 877
    Helixi95 – 1006
    Beta strandi103 – 1064
    Beta strandi109 – 1168
    Beta strandi124 – 1285
    Beta strandi132 – 1354
    Beta strandi144 – 1507
    Beta strandi158 – 1658
    Turni169 – 1724
    Helixi173 – 1753
    Helixi183 – 1853
    Beta strandi198 – 2003
    Beta strandi210 – 2123
    Beta strandi215 – 2217
    Beta strandi226 – 2316
    Beta strandi233 – 2353
    Beta strandi239 – 2413
    Helixi243 – 2464
    Beta strandi250 – 2523
    Helixi261 – 2644
    Beta strandi269 – 2735
    Beta strandi276 – 2794
    Beta strandi284 – 2929
    Beta strandi298 – 30710
    Beta strandi310 – 3134
    Beta strandi319 – 3224
    Beta strandi326 – 3283
    Helixi330 – 3356
    Helixi339 – 3435
    Helixi346 – 35611
    Beta strandi358 – 3669
    Turni368 – 3725
    Helixi373 – 3764
    Helixi378 – 3803
    Helixi390 – 3967
    Beta strandi401 – 41111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OVWX-ray2.70A/B/C/D20-416[»]
    2OVWX-ray2.30A/B/C/D20-429[»]
    3OVWX-ray2.30A/B20-429[»]
    4OVWX-ray2.30A/B20-429[»]
    ProteinModelPortaliP46237.
    SMRiP46237. Positions 19-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46237.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.70.100.10. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view]
    PfamiPF00840. Glyco_hydro_7. 1 hit.
    [Graphical view]
    PRINTSiPR00734. GLHYDRLASE7.
    SUPFAMiSSF49899. SSF49899. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P46237-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSLSLILSA LAVQVAVAQT PDKAKEQHPK LETYRCTKAS GCKKQTNYIV    50
    ADAGIHGIRQ KNGAGCGDWG QKPNATACPD EASCAKNCIL SGMDSNAYKN 100
    AGITTSGNKL RLQQLINNQL VSPRVYLLEE NKKKYEMLHL TGTEFSFDVE 150
    MEKLPCGMNG ALYLSEMPQD GGKSTSRNSK AGAYYGAGYC DAQCYVTPFI 200
    NGVGNIKGQG VCCNELDIWE ANSRATHIAP HPCSKPGLYG CTGDECGSSG 250
    ICDKAGCGWN HNRINVTDFY GRGKQYKVDS TRKFTVTSQF VANKQGDLIE 300
    LHRHYIQDNK VIESAVVNIS GPPKINFIND KYCAATGANE YMRLGGTKQM 350
    GDAMSRGMVL AMSVWWSEGD FMAWLDQGVA GPCDATEGDP KNIVKVQPNP 400
    EVTFSNIRIG EIGSTSSVKA PAYPGPHRL 429
    Length:429
    Mass (Da):46,445
    Last modified:November 1, 1995 - v1
    Checksum:iFAE8A880B1F880F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29378 mRNA. Translation: AAA65586.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29378 mRNA. Translation: AAA65586.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OVW X-ray 2.70 A/B/C/D 20-416 [» ]
    2OVW X-ray 2.30 A/B/C/D 20-429 [» ]
    3OVW X-ray 2.30 A/B 20-429 [» ]
    4OVW X-ray 2.30 A/B 20-429 [» ]
    ProteinModelPortali P46237.
    SMRi P46237. Positions 19-418.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi EGL7A_FUSOX.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P46237.

    Family and domain databases

    Gene3Di 2.70.100.10. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view ]
    Pfami PF00840. Glyco_hydro_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00734. GLHYDRLASE7.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The use of conserved cellulase family-specific sequences to clone cellulase homologue cDNAs from Fusarium oxysporum."
      Sheppard P.O., Grant F.J., Oort P.J., Sprecher C.A., Foster D.C., Hagen F.S., Upshall A., McKnight G.L., O'Hara P.J.
      Gene 150:163-167(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group."
      Sulzenbacher G., Driguez H., Henrissat B., Schuelein M., Davies G.J.
      Biochemistry 35:15280-15287(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    3. "Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3-A resolution."
      Sulzenbacher G., Schuelein M., Davies G.J.
      Biochemistry 36:5902-5911(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiGUNC_FUSOX
    AccessioniPrimary (citable) accession number: P46237
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3