Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06564

- GUN_BACA3

UniProt

P06564 - GUN_BACA3

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Endoglucanase

Gene
N/A
Organism
Bacillus akibai (strain ATCC 43226 / DSM 21942 / JCM 9157 / 1139)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei190 – 1901Proton donorBy similarity
Active sitei305 – 3051NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

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

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 800770EndoglucanasePRO_0000007837Add
BLAST

Structurei

Secondary structure

1
800
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi588 – 5903
Beta strandi594 – 5963
Beta strandi600 – 6023
Beta strandi613 – 6175
Beta strandi620 – 6289
Turni637 – 6404
Beta strandi643 – 6475
Beta strandi658 – 66912
Beta strandi674 – 6818
Helixi684 – 6863
Beta strandi696 – 6994
Helixi700 – 7056
Beta strandi712 – 7209
Beta strandi735 – 74410
Beta strandi748 – 75912

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UWWX-ray1.40A/B571-761[»]
ProteinModelPortaliP06564.
SMRiP06564. Positions 44-570, 578-761.
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:
EMBL
GenBank
DDBJ
Links Updated
M15743 Genomic DNA. Translation: AAA22305.1.
D00066 Genomic DNA. Translation: BAA00045.1.
PIRiA29003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15743 Genomic DNA. Translation: AAA22305.1 .
D00066 Genomic DNA. Translation: BAA00045.1 .
PIRi A29003.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UWW X-ray 1.40 A/B 571-761 [» ]
ProteinModelPortali P06564.
SMRi P06564. Positions 44-570, 578-761.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM17. Carbohydrate-Binding Module Family 17.
CBM28. Carbohydrate-Binding Module Family 28.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P06564.

Family and domain databases

Gene3Di 2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProi IPR005086. 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 ]
Pfami PF03424. CBM_17_28. 2 hits.
PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of the alkaline cellulase gene from the alkalophilic Bacillus sp. strain 1139."
    Fukumori F., Kudo T., Narahashi Y., Horikoshi K.
    J. Gen. Microbiol. 132:2329-2335(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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: October 1, 2014
This is version 97 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

External Data

Dasty 3