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P46237

- GUNC_FUSOX

UniProt

P46237 - GUNC_FUSOX

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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

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
Complete GO annotation...

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

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.
InterProiIPR013320. ConA-like_dom.
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

        10         20         30         40         50
MKSLSLILSA LAVQVAVAQT PDKAKEQHPK LETYRCTKAS GCKKQTNYIV
60 70 80 90 100
ADAGIHGIRQ KNGAGCGDWG QKPNATACPD EASCAKNCIL SGMDSNAYKN
110 120 130 140 150
AGITTSGNKL RLQQLINNQL VSPRVYLLEE NKKKYEMLHL TGTEFSFDVE
160 170 180 190 200
MEKLPCGMNG ALYLSEMPQD GGKSTSRNSK AGAYYGAGYC DAQCYVTPFI
210 220 230 240 250
NGVGNIKGQG VCCNELDIWE ANSRATHIAP HPCSKPGLYG CTGDECGSSG
260 270 280 290 300
ICDKAGCGWN HNRINVTDFY GRGKQYKVDS TRKFTVTSQF VANKQGDLIE
310 320 330 340 350
LHRHYIQDNK VIESAVVNIS GPPKINFIND KYCAATGANE YMRLGGTKQM
360 370 380 390 400
GDAMSRGMVL AMSVWWSEGD FMAWLDQGVA GPCDATEGDP KNIVKVQPNP
410 420
EVTFSNIRIG EIGSTSSVKA PAYPGPHRL
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 IPR013320. ConA-like_dom.
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 29, 2014
This is version 87 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