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Q84C00

- GUB_CLOTM

UniProt

Q84C00 - GUB_CLOTM

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Protein

Beta-glucanase

Gene

licB

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei136 – 1361NucleophilePROSITE-ProRule annotation
Active sitei140 – 1401Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. licheninase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucanase (EC:3.2.1.73)
Alternative name(s):
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Endo-beta-1,3-1,4 glucanase
Laminarinase
Lichenase
Gene namesi
Name:licB
Synonyms:lam1
OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 334307Beta-glucanasePRO_0000011792Add
BLAST

Interactioni

Subunit structurei

May form part of a multienzyme complex (cellulosome).

Structurei

3D structure databases

ProteinModelPortaliQ84C00.
SMRiQ84C00. Positions 33-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati273 – 296241Add
BLAST
Repeati308 – 331242Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni273 – 331592 X 24 AA approximate repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi252 – 26918Pro/Thr-rich (linker)Add
BLAST

Domaini

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 16 family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR013320. ConA-like_dom.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]
PfamiPF00404. Dockerin_1. 2 hits.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q84C00 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE
60 70 80 90 100
KADWANGSVF NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRSKSF
110 120 130 140 150
FGYGYYEVRM KAAKNVGIVS SFFTYTGPSD NNPWDEIDIE FLGKDTTKAQ
160 170 180 190 200
FNWYKNEVGG NEYLHNLGFD ASQDFHTYGF EWRPDYIDFY VDGKKVYRGT
210 220 230 240 250
RNIPVTPGKI MMNLWPGKGV DEWLGRYDGR TPLQAEYEYV KYYPNGVPQD
260 270 280 290 300
NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP
310 320 330
VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL
Length:334
Mass (Da):37,942
Last modified:June 1, 2003 - v1
Checksum:i3079DEF1CEE5A664
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971S → T in CAA41281. (PubMed:1755832)Curated
Sequence conflicti97 – 971S → T1 PublicationCurated
Sequence conflicti149 – 1491A → V in CAA41281. (PubMed:1755832)Curated
Sequence conflicti149 – 1491A → V1 PublicationCurated
Sequence conflicti157 – 1571E → G in CAA41281. (PubMed:1755832)Curated
Sequence conflicti157 – 1571E → G1 PublicationCurated
Sequence conflicti218 – 2181K → I in CAA41281. (PubMed:1755832)Curated
Sequence conflicti218 – 2181K → I1 PublicationCurated
Sequence conflicti304 – 33431QSVAD…AIPSL → PQDGCGRHDRVVDSGSK in CAA41281. (PubMed:1755832)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58392 Genomic DNA. Translation: CAA41281.1.
AY225318 Genomic DNA. Translation: AAO74890.1.
PIRiJS0611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58392 Genomic DNA. Translation: CAA41281.1 .
AY225318 Genomic DNA. Translation: AAO74890.1 .
PIRi JS0611.

3D structure databases

ProteinModelPortali Q84C00.
SMRi Q84C00. Positions 33-246.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
2.60.120.200. 1 hit.
InterProi IPR008264. Beta_glucanase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR013320. ConA-like_dom.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view ]
Pfami PF00404. Dockerin_1. 2 hits.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view ]
PRINTSi PR00737. GLHYDRLASE16.
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the Clostridium thermocellum laminarinase gene."
    Zverlov V.V., Laptev D.A., Tishkov V.I., Velikodvorskaja G.A.
    Biochem. Biophys. Res. Commun. 181:507-512(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: F7.
  2. Zverlov V.V.
    Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Lv W.-P., Xu Z.-R., Li W.-F., Sun J.-Y., Xu Y.-X., Gu S.-H.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning the Clostridium thermocellum thermostable laminarinase gene in Escherichia coli; the properties of the enzyme thus produced."
    Zverlov V.V., Velikodvorskaja G.A.
    Biotechnol. Lett. 12:811-816(1990)
    Cited for: CHARACTERIZATION.
    Strain: F7.

Entry informationi

Entry nameiGUB_CLOTM
AccessioniPrimary (citable) accession number: Q84C00
Secondary accession number(s): P29716, P37074
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 56 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