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Protein

Glucan endo-1,3-beta-glucosidase

Gene

glcI

Organism
Arthrobacter sp. (strain YCWD3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Lysis of cellular walls containing beta-1,3-glucans. Implicated in the defense against fungal pathogens (By similarity).By similarity

Catalytic activityi

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Keywords - Ligandi

Lectin

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH64. Glycoside Hydrolase Family 64.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan endo-1,3-beta-glucosidase (EC:3.2.1.39)
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name:
(1->3)-beta-glucanase
Gene namesi
Name:glcI
OrganismiArthrobacter sp. (strain YCWD3)
Taxonomic identifieri79671 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Subcellular locationi

Periplasm By similarity

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Tat-type signalPROSITE-ProRule annotationAdd
BLAST
Chaini37 – 548512Glucan endo-1,3-beta-glucosidasePRO_0000012234Add
BLAST

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Structurei

3D structure databases

ProteinModelPortaliQ59146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini422 – 548127Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 64 family.Curated
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR000772. Ricin_B_lectin.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q59146-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHDRKNSSR RAWAALCAAV LAVSGALVGV AAPASAVPAT IPLTITNDSG
60 70 80 90 100
RGPIYLYVLG ERDGVAGWAD AGGTFHPWPG GVGPVPVPAP DASIAGPGPG
110 120 130 140 150
QSVTIRLPKL SGRVYYSYGQ KMTFQIVLDG RLVQPAVQND SDPNRNILFN
160 170 180 190 200
WTEYTLNDGG LWINSTQVDH WSAPYQVGVQ RADGQVLSTG MLKPNGYEAF
210 220 230 240 250
YTALESAGWG GLVQRAPDGS RLRALNPSHG IDVGKISSAS IDSYVTEVWN
260 270 280 290 300
SYRTRDMCVT PFSHEPGTQF RGRVDGDWFR FRNGSGQEVA AFKKPDASSV
310 320 330 340 350
YGCHKDLQAP NDHVVGPIAR TLCAALVRTT ALTNPNQPDA NSAGFYQDAR
360 370 380 390 400
TNVYAKLAHQ QMANGKAYAF AFDDVGAHES LVHDGNPQAA YIKLDPFTGT
410 420 430 440 450
ATPIANGGST EQPGTPGGLP AGTGALRIGS TLCLDVPWAD PTDTNQVQLA
460 470 480 490 500
TCSGNAAQQW TRGTDGTVRA LGKCLDVARS GTADGTAVWI YTCNGTGAQK
510 520 530 540
WTYDSATKAL RNPQSGKCLD AQGGAPLRDG QKVQLWTCNQ TEAQRWTL
Length:548
Mass (Da):58,164
Last modified:November 1, 1996 - v1
Checksum:iBD56354315750596
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D23668 Genomic DNA. Translation: BAA04892.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D23668 Genomic DNA. Translation: BAA04892.1.

3D structure databases

ProteinModelPortaliQ59146.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH64. Glycoside Hydrolase Family 64.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR000772. Ricin_B_lectin.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Watanabe T., Hasegawa H., Tanaka H., Doi A., Doi K.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiE13B_ARTSW
AccessioniPrimary (citable) accession number: Q59146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 68 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.