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Protein

Endoglucanase

Gene
N/A
Organism
Bacillus akibai (strain ATCC 43226 / DSM 21942 / JCM 9157 / 1139)
Status
Reviewed-Annotation score: Annotation score: 2 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.

pH dependencei

Optimum pH is 9.0.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei190Proton donorBy similarity1
Active sitei305NucleophileBy similarity1

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

CAZyiCBM17. Carbohydrate-Binding Module Family 17.
CBM28. Carbohydrate-Binding Module Family 28.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase (EC:3.2.1.4)
Alternative name(s):
Alkaline cellulase
Endo-1,4-beta-glucanase
OrganismiBacillus akibai (strain ATCC 43226 / DSM 21942 / JCM 9157 / 1139)
Taxonomic identifieri1236973 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000000783731 – 800EndoglucanaseAdd BLAST770

Proteomic databases

PRIDEiP06564.

Structurei

Secondary structure

1800
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi588 – 590Combined sources3
Beta strandi594 – 596Combined sources3
Beta strandi600 – 602Combined sources3
Beta strandi613 – 617Combined sources5
Beta strandi620 – 628Combined sources9
Turni637 – 640Combined sources4
Beta strandi643 – 647Combined sources5
Beta strandi658 – 669Combined sources12
Beta strandi674 – 681Combined sources8
Helixi684 – 686Combined sources3
Beta strandi696 – 699Combined sources4
Helixi700 – 705Combined sources6
Beta strandi712 – 720Combined sources9
Beta strandi735 – 744Combined sources10
Beta strandi748 – 759Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UWWX-ray1.40A/B571-761[»]
ProteinModelPortaliP06564.
SMRiP06564.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06564.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR005086. CBM_fam_17/28.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03424. CBM_17_28. 2 hits.
PF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLRKKTKQL ISSILILVLL LSLFPTALAA EGNTREDNFK HLLGNDNVKR
60 70 80 90 100
PSEAGALQLQ EVDGQMTLVD QHGEKIQLRG MSTHGLQWFP EILNDNAYKA
110 120 130 140 150
LANDWESNMI RLAMYVGENG YASNPELIKS RVIKGIDLAI ENDMYVIVDW
160 170 180 190 200
HVHAPGDPRD PVYAGAEDFF RDIAALYPNN PHIIYELANE PSSNNNGGAG
210 220 230 240 250
IPNNEEGWNA VKEYADPIVE MLRDSGNADD NIIIVGSPNW SQRPDLAADN
260 270 280 290 300
PIDDHHTMYT VHFYTGSHAA STESYPPETP NSERGNVMSN TRYALENGVA
310 320 330 340 350
VFATEWGTSQ ANGDGGPYFD EADVWIEFLN ENNISWANWS LTNKNEVSGA
360 370 380 390 400
FTPFELGKSN ATSLDPGPDQ VWVPEELSLS GEYVRARIKG VNYEPIDRTK
410 420 430 440 450
YTKVLWDFND GTKQGFGVNG DSPVEDVVIE NEAGALKLSG LDASNDVSEG
460 470 480 490 500
NYWANARLSA DGWGKSVDIL GAEKLTMDVI VDEPTTVSIA AIPQGPSANW
510 520 530 540 550
VNPNRAIKVE PTNFVPLEDK FKAELTITSA DSPSLEAIAM HAENNNINNI
560 570 580 590 600
ILFVGTEGAD VIYLDNIKVI GTEVEIPVVH DPKGEAVLPS VFEDGTRQGW
610 620 630 640 650
DWAGESGVKT ALTIEEANGS NALSWEFGYP EVKPSDNWAT APRLDFWKSD
660 670 680 690 700
LVRGENDYVT FDFYLDPVRA TEGAMNINLV FQPPTNGYWV QAPKTYTINF
710 720 730 740 750
DELEEPNQVN GLYHYEVKIN VRDITNIQDD TLLRNMMIIF ADVESDFAGR
760 770 780 790 800
VFVDNVRFEG AATTEPVEPE PVDPGEETPP VDEKEAKTEQ KEAEKEEKEE
Length:800
Mass (Da):88,602
Last modified:January 1, 1988 - v1
Checksum:i7CCA4D7B6DAD55CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15743 Genomic DNA. Translation: AAA22305.1.
D00066 Genomic DNA. Translation: BAA00045.1.
PIRiA29003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15743 Genomic DNA. Translation: AAA22305.1.
D00066 Genomic DNA. Translation: BAA00045.1.
PIRiA29003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UWWX-ray1.40A/B571-761[»]
ProteinModelPortaliP06564.
SMRiP06564.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM17. Carbohydrate-Binding Module Family 17.
CBM28. Carbohydrate-Binding Module Family 28.
GH5. Glycoside Hydrolase Family 5.

Proteomic databases

PRIDEiP06564.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP06564.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR005086. CBM_fam_17/28.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03424. CBM_17_28. 2 hits.
PF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUN_BACA3
AccessioniPrimary (citable) accession number: P06564
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 2, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Alkalophilic Bacillus sp strain 1139 is not a true cellulolytic micro-organism because the enzyme is unable to hydrolyze native cellulose.

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

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 one 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.