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Protein

Endoglucanase A

Gene

eglA

Organism
Bacillus pumilus (Bacillus mesentericus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Active on carboxymethyl cellulose and carboxymethyl cellulose-RBB but not avicel, xanthan gum, carboxymethyl-curdulan-RBB or carboxymethyl-xylan-RBB.1 Publication

Catalytic activityi

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

Enzyme regulationi

Strongly inhibited by ZnCl2 and by EDTA.1 Publication

pH dependencei

Optimum pH is 5-8.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius. Retains more than 90% activity after 24 hours at 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei419 – 4191By similarity
Active sitei457 – 4571By similarity
Active sitei466 – 4661By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Alternative name(s):
Endo-1,4-beta-glucanase A
Gene namesi
Name:eglA
OrganismiBacillus pumilus (Bacillus mesentericus)
Taxonomic identifieri1408 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659Endoglucanase APRO_5000091857Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ5YLG1.
SMRiQ5YLG1. Positions 45-657.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini501 – 658158CBM3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 500500CatalyticAdd
BLAST

Sequence similaritiesi

Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.710. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamiPF00942. CBM_3. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTiSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 1 hit.
PROSITEiPS51172. CBM3. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5YLG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIFETYLIL FKTVQITKRR IERRRLRLLN QCFTKKEGVS NREMASYNYV
60 70 80 90 100
EVLQKSMLFY EAQRSGRLPE SNRLNWRGDS GLKDGKDVGH DLTGGWYDAG
110 120 130 140 150
DHVKFGLPMA YSAAVLAWTV YEYREAYEEA ELLDEILDQI KWATDYFLKA
160 170 180 190 200
HTGPNEFWAQ VGDGNADHAW WGPAEVMPMN RPAFKIDEHC PGTEVAAQTA
210 220 230 240 250
AALAAGSIIF KETDASYAAK LLTHAKQLYA FADRYRGKYT DCVTNAQPFY
260 270 280 290 300
NSWSGYVDEL IWGGIWLYLA TNEETYLNKA LKAVEEWPQD WDYTFTMSWD
310 320 330 340 350
NTFFASQILL ARITKENRFI ESTERNLDYW TTGLVQNGKV ERITYTPGGL
360 370 380 390 400
AWLDQWGSLR YAANAAFLAF VYADWVSDQE KKNRYQSFAI KQTHYMLGDN
410 420 430 440 450
PLNRSYVVGF GQNSPKHPHH RTAHGSWSNQ LTNPPSHRHT LYGALVGGPN
460 470 480 490 500
AQDQYDDDIS DYISNEVATD YNAAFTGNIA KMVQLFGEGQ SKLPNFPPKE
510 520 530 540 550
QVEDEFFVEA AVMHNDTTST QVKAVLYNRS GWPARSSQTL SFRYYVNLSE
560 570 580 590 600
VFAKGFTEKD IQVTAAYNEG ASLSPLKVYD ASSRVYFAEI DFTGVVISPR
610 620 630 640 650
GESEHKKEIQ FRLSAPNGSN IWDASNDYSY QGLTSNMQKT TKIPVFEDGV

LVFGTLPDK
Length:659
Mass (Da):74,985
Last modified:November 23, 2004 - v1
Checksum:i13DE360B374DA139
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY339624 Genomic DNA. Translation: AAQ91573.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY339624 Genomic DNA. Translation: AAQ91573.1.

3D structure databases

ProteinModelPortaliQ5YLG1.
SMRiQ5YLG1. Positions 45-657.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.710. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamiPF00942. CBM_3. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTiSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 1 hit.
PROSITEiPS51172. CBM3. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: CL16.

Entry informationi

Entry nameiGUNA_BACPU
AccessioniPrimary (citable) accession number: Q5YLG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 2004
Last modified: July 22, 2015
This is version 48 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.