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P26414

- GUNA_THEBI

UniProt

P26414 - GUNA_THEBI

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Protein
Endoglucanase A
Gene
celA
Organism
Thermobispora bispora (Microbispora bispora)
Status
Reviewed - 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 – 1131 By similarity
Active sitei151 – 1511Proton donor By similarity
Active sitei300 – 3001Nucleophile By similarity

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 – 3030 Reviewed prediction
Add
BLAST
Chaini31 – 456426Endoglucanase A
PRO_0000007905Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP26414.
SMRiP26414. Positions 36-321, 356-449.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini353 – 456104CBM2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 322292Catalytic
Add
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

MSRIRRFLAT ALAAATAGVG AIVTAIASAG PAHAYDSPFY VDPQSNAAKW    50
VAANPNDPRT PVIRDRIAAV PTGRWFANYN PSTVRAEVDA YVGAAAAAGK 100
IPIMVVYAMP NRDCGGPSAG GAPNHTAYRA WIDEIAAGLR NRPAVIILEP 150
DALPIMTNCM SPSEQAEVQA SAVGAGKKFK AASSQAKVYF DAGHDAWVPA 200
DEMASRLRGA DIANSADGIA LNVSNYRYTS GLISYAKSVL SAIGASHLRA 250
VIDTSRNGNG PLGSEWCDPP GRATGTWSTT DTGDPAIDAF LWIKPPGEAD 300
GCIATPGVFV PDRAYELAMN AAPPTYSPSP TPSTPSPSPS QSDPGSPSPS 350
PSQPPAGRAC EATYALVNQW PGGFQAEVTV KNTGSSPING WTVQWTLPSG 400
QSITQLWNGD LSTSGSNVTV RNVSWNGNVP AGGSTSFGFL GSGTGQLSSS 450
ITCSAS 456
Length:456
Mass (Da):47,011
Last modified:August 1, 1992 - v1
Checksum:iB06D8595E322848F
GO

Cross-referencesi

3D structure databases

ProteinModelPortali P26414.
SMRi P26414. Positions 36-321, 356-449.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProi IPR016288. 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 ]
Pfami PF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view ]
PRINTSi PR00733. GLHYDRLASE6.
SMARTi SM00637. CBD_II. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 (1989)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiGUNA_THEBI
AccessioniPrimary (citable) accession number: P26414
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 16, 2013
This is version 75 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

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