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Protein

Endoglucanase A

Gene

celA

Organism
Thermobispora bispora (Microbispora bispora)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 sitei113 – 1131PROSITE-ProRule annotation
Active sitei151 – 1511Proton donorPROSITE-ProRule annotation
Active sitei300 – 3001NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. polysaccharide binding Source: InterPro

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

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A
Gene namesi
Name:celA
OrganismiThermobispora bispora (Microbispora bispora)
Taxonomic identifieri2006 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeThermobispora

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 456426Endoglucanase APRO_0000007905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi114 ↔ 159By similarity
Disulfide bondi267 ↔ 302By similarity
Disulfide bondi360 ↔ 453By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

SMRiP26414. Positions 36-321, 356-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini353 – 456104CBM2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 322292CatalyticAdd
BLAST
Regioni323 – 35533Linker ("hinge") (Pro-Ser box)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P26414-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRIRRFLAT ALAAATAGVG AIVTAIASAG PAHAYDSPFY VDPQSNAAKW
60 70 80 90 100
VAANPNDPRT PVIRDRIAAV PTGRWFANYN PSTVRAEVDA YVGAAAAAGK
110 120 130 140 150
IPIMVVYAMP NRDCGGPSAG GAPNHTAYRA WIDEIAAGLR NRPAVIILEP
160 170 180 190 200
DALPIMTNCM SPSEQAEVQA SAVGAGKKFK AASSQAKVYF DAGHDAWVPA
210 220 230 240 250
DEMASRLRGA DIANSADGIA LNVSNYRYTS GLISYAKSVL SAIGASHLRA
260 270 280 290 300
VIDTSRNGNG PLGSEWCDPP GRATGTWSTT DTGDPAIDAF LWIKPPGEAD
310 320 330 340 350
GCIATPGVFV PDRAYELAMN AAPPTYSPSP TPSTPSPSPS QSDPGSPSPS
360 370 380 390 400
PSQPPAGRAC EATYALVNQW PGGFQAEVTV KNTGSSPING WTVQWTLPSG
410 420 430 440 450
QSITQLWNGD LSTSGSNVTV RNVSWNGNVP AGGSTSFGFL GSGTGQLSSS

ITCSAS
Length:456
Mass (Da):47,011
Last modified:July 31, 1992 - v1
Checksum:iB06D8595E322848F
GO

Cross-referencesi

3D structure databases

SMRiP26414. Positions 36-321, 356-449.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Yablonsky M.D., Elliston K.O., Eveleigh D.E.
    (In) Coughlan M.P. (eds.); Production, characterization and application of cellulose, hemicellulose and lignin enzyme degrading systems, pp.77-83, Elsevier, London (1988)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiGUNA_THEBI
AccessioniPrimary (citable) accession number: P26414
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1992
Last sequence update: July 31, 1992
Last modified: March 31, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.