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P28622

- GUN4_BACS5

UniProt

P28622 - GUN4_BACS5

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Protein

Endoglucanase 4

Gene
N/A
Organism
Bacillus sp. (strain KSM-522)
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 sitei400 – 4001By similarity
Active sitei438 – 4381By similarity
Active sitei447 – 4471By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose 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

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

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase 4 (EC:3.2.1.4)
Alternative name(s):
Cellulase 4
EG-IV
Endo-1,4-beta-glucanase 4
OrganismiBacillus sp. (strain KSM-522)
Taxonomic identifieri120046 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 636611Endoglucanase 4PRO_0000007952Add
BLAST

Proteomic databases

PRIDEiP28622.

Structurei

3D structure databases

ProteinModelPortaliP28622.
SMRiP28622. Positions 27-634.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini478 – 635158CBM3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

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.

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

P28622-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTRRWSFLVQ CFTFKKKEGV RSRYMSDYNY VEVLQKSILF YEAQRSGKLP
60 70 80 90 100
ESNRLNWRGD SGLEDGKDVG HDLTGGWYDA GDHVKFGLPM AYSAAVLAWT
110 120 130 140 150
VYEYREAYEE AELLDDMLDQ IKWATDYFLK AHTGPNEFWA QVGDGNADHG
160 170 180 190 200
WWGPAEVMPM NRPAFKIDEH CPGTEVAAQT AAALAAGSII FKETDAPYAA
210 220 230 240 250
KLLTHAKQLY AFADQYRGEY TDCVTNAQPF YNSWSGYIDE LIWGGIWLYL
260 270 280 290 300
ATNDQTYLNK ALKAVEEWPK DWDYTFTMSW DNTFFLSQIL LARITKEKRF
310 320 330 340 350
IESTERNLDY WSTGFVQNGK VERITYTPGG LAWLDQWGSL RYTANAAFLA
360 370 380 390 400
FVYADWVSDQ EKKNRYQTFA IRQTHYMLGD NPQNRSYVVG FGKNPPMHPH
410 420 430 440 450
HRTAHGSWSN QLTTPSSHRH TLYGPLVGGP NRQDQYTDDI SDYVSNEVAT
460 470 480 490 500
DYNAAFTGNG AAVWSGQSKL PNFPPKEKVE DEFFVEAAVM SNDTTSTQIK
510 520 530 540 550
AILYNRSGWP ARSSQSLSFR YYVNLSEIFA KGFTDKDIQV TAVYNEGASL
560 570 580 590 600
SPLTVYDASS HIYFTEIDFT GVAIFPGGES LHKKEIQFRL SAPNGANIWD
610 620 630
ASNDYSFQGL TSNMQKTARI PVFDQGDLVF GTLPNK
Length:636
Mass (Da):72,245
Last modified:May 30, 2000 - v2
Checksum:i76718BF57A8EF6A2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti530 – 5345AKGFT → CEGIH(PubMed:2113383)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB004098 Genomic DNA. Translation: BAA24918.1.
PIRiJC5874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB004098 Genomic DNA. Translation: BAA24918.1 .
PIRi JC5874.

3D structure databases

ProteinModelPortali P28622.
SMRi P28622. Positions 27-634.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Proteomic databases

PRIDEi P28622.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
2.60.40.710. 1 hit.
InterProi IPR008928. 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 ]
Pfami PF00942. CBM_3. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view ]
SMARTi SM01067. CBM_3. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 1 hit.
PROSITEi PS51172. CBM3. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Amino acid sequence and stereoselective hydrolytic reaction of an endo-1,4-beta-glucanase from a Bacillus strain."
    Hitomi J., Hatada Y., Kawaminami S., Kawai S., Ito S.
    Biosci. Biotechnol. Biochem. 61:2004-2009(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of Clostridium cellulovorans endo-1,4-beta-glucanase genes."
    Shoseyov O., Foong F., Hamamoto T., Doi R.H.
    Biochem. Biophys. Res. Commun. 169:667-672(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-534.
  3. Doi R.H.
    Unpublished observations (JAN-2000)
    Cited for: SHOWS THAT SEQUENCE DID NOT ORIGINATE FROM C.CELLULOVORANS.

Entry informationi

Entry nameiGUN4_BACS5
AccessioniPrimary (citable) accession number: P28622
Secondary accession number(s): O50589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to originate from Clostridium cellulovorans and was termed endoglucanase C (engC).1 Publication

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