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Protein

Endoglucanase EG-1

Gene

EG-1

Organism
Humicola grisea var. thermoidea
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei217NucleophileBy similarity1
Active sitei222Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH7 Glycoside Hydrolase Family 7
mycoCLAPiEGL7A_HUMGT

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase EG-1 (EC:3.2.1.4)
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:EG-1
OrganismiHumicola grisea var. thermoidea
Taxonomic identifieri5528 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
ChainiPRO_000000791621 – 435Endoglucanase EG-1Add BLAST415

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Pyrrolidone carboxylic acidBy similarity1
Disulfide bondi38 ↔ 44By similarity
Disulfide bondi71 ↔ 93By similarity
Disulfide bondi83 ↔ 89By similarity
Glycosylationi109N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi160 ↔ 385By similarity
Disulfide bondi192 ↔ 215By similarity
Disulfide bondi196 ↔ 214By similarity
Disulfide bondi235 ↔ 254By similarity
Disulfide bondi243 ↔ 248By similarity
Disulfide bondi259 ↔ 335By similarity
Glycosylationi267N-linked (GlcNAc...) asparagineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiQ12622

Structurei

3D structure databases

ProteinModelPortaliQ12622
SMRiQ12622
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

CDDicd07999 GH7_CBH_EG, 1 hit
Gene3Di2.70.100.10, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR001722 Glyco_hydro_7
IPR037019 Glyco_hydro_7_sf
PANTHERiPTHR33753 PTHR33753, 1 hit
PfamiView protein in Pfam
PF00840 Glyco_hydro_7, 1 hit
PRINTSiPR00734 GLHYDRLASE7
SUPFAMiSSF49899 SSF49899, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q12622-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARGTALLGL TSLLLGLVNG QKPGETKEVH PQLTTFRCTK KGGCKPATNY
60 70 80 90 100
IVLDSLSHPI HRAEGLGWGN CGDWGNPPPK DVCPDVESCA KNCIMEGIPD
110 120 130 140 150
YSQYGVTTNG TSLRLQHILP DGRVPSPRVY LLDKTERRYE MLHLTGFEFT
160 170 180 190 200
FDVDATKLPC GMNSALYLSE MHPTGAKSKH NPGGAYYGTG YCDAQCFVTP
210 220 230 240 250
FINGLGNIEG KGSCCNEMDI WEANSRASHV APHVCNKKGL YLCEGEECAF
260 270 280 290 300
EGVCDKNGCG WNPYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRKGKL
310 320 330 340 350
EKIHRFYVQD GKIIESFYTN KEGIPYTNMI EDEFCAATGS RKYMELGATQ
360 370 380 390 400
GMGEALTRGM VLAMSIWWDQ GGNMEWLDHG EAGPCAKGEG APSNVVQVEP
410 420 430
FPEVTYTNLR WGEIGSTYQE VQKPKPKPGP GPRSD
Length:435
Mass (Da):47,890
Last modified:November 1, 1996 - v1
Checksum:i25EB3D62D96B65FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63516 Genomic DNA Translation: BAA09786.1

Similar proteinsi

Entry informationi

Entry nameiGUN1_HUMGT
AccessioniPrimary (citable) accession number: Q12622
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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