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P26225

- GUNB_CELFI

UniProt

P26225 - GUNB_CELFI

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Protein
Endoglucanase B
Gene
cenB
Organism
Cellulomonas fimi
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

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 sitei410 – 4101 By similarity
Active sitei449 – 4491 By similarity
Active sitei458 – 4581 By 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

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase B (EC:3.2.1.4)
Alternative name(s):
Cellulase B
Endo-1,4-beta-glucanase B
Gene namesi
Name:cenB
OrganismiCellulomonas fimi
Taxonomic identifieri1708 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333 Reviewed prediction
Add
BLAST
Chaini34 – 10451012Endoglucanase B
PRO_0000007945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi946 ↔ 1044 By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP26225.
SMRiP26225. Positions 35-641.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini493 – 642150CBM3
Add
BLAST
Domaini653 – 74391Fibronectin type-III 1
Add
BLAST
Domaini751 – 84090Fibronectin type-III 2
Add
BLAST
Domaini849 – 94092Fibronectin type-III 3
Add
BLAST
Domaini939 – 1045107CBM2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 492459Catalytic
Add
BLAST
Regioni644 – 6507Linker ("hinge") (Pro-Thr box)
Regioni734 – 74815Linker ("hinge") (Pro-Thr box)
Add
BLAST
Regioni831 – 84616Linker ("hinge") (Pro-Thr box)
Add
BLAST
Regioni931 – 94414Linker ("hinge") (Pro-Thr box)
Add
BLAST

Domaini

The linker region (also termed "hinge") may be a potential site for proteolysis.1 Publication

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 3 hits.
2.60.40.290. 1 hit.
2.60.40.710. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR003961. Fibronectin_type3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00942. CBM_3. 1 hit.
PF00041. fn3. 3 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM01067. CBM_3. 1 hit.
SM00060. FN3. 3 hits.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49265. SSF49265. 2 hits.
SSF49384. SSF49384. 2 hits.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51172. CBM3. 1 hit.
PS50853. FN3. 3 hits.
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.

P26225-1 [UniParc]FASTAAdd to Basket

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MLRQVPRTLV AGGSALAVAV GVLVAPLATG AAAAPTYNYA EALQKSMFFY     50
QAQRSGDLPA DFPVSWRGDS GLTDGADVGK DLTGGWYDAG DHVKFGFPMA 100
FSATMLAWGA IESPTGYSKA GSLDELKDNL RFVSDYFVKA HTAPNELYVQ 150
VGDGEADHKW WGPAEVMTMA RPSHKISASC PGSDVAAETA AALASSAIVL 200
KGDDPAYAAT LVSHAKQLYT FADTYRGAYS DCVTAASAYY KSWSGYQDEL 250
VWGAYWLYKA TGDATYLAKA EAEYDKLGTE NQSTTRSYKW TIAWDNKQFG 300
TYALLAMETG KQKYVDDANR WLDYWTVGVN GQKVPYSPGG QAVLDSWGAL 350
RYAANTSFVA LVYSDWMTDA TRKARYHDFG VRQINYALGD NPRSSSYVVG 400
FGANPPTAPH HRTAHGSWLD SITTPAQSRH VLYGALVGGP GSPNDAYTDS 450
RQDYVANEVA TDYNAGFTSA LARLVEEYGG TPLASFPTPE QPDGDQLFVE 500
AMLNQPPSGT FTEVKAMIRN QSAFPARSLK NAKVRYWFTT DGFAASDVTL 550
SANYSECGAQ SGKGVSAGGT LGYVELSCVG QDIHPGGQSQ HRREIQFRLT 600
GPAGWNPAND PSYTGLTQTA LAKASAITLY DGSTLVWGKE PTGTTTDTTP 650
PTTPGTPVAT GVTTVGASLS WAASTDAGSG VAGYELYRVQ GTTQTLVGTT 700
TAAAYILRDL TPGTAYSYVV KAKDVAGNVS AASAAVTFTT DTTGETEPPT 750
TPGTPVASAV TSTGATLAWA PSTGDPAVSG YDVLRVQGTT TTVVAQTTVP 800
TVTLSGLTPS TAYTYAVRAK NVAGDVSALS APVTFTTAAP PVDTVAPTVP 850
GTPVASNVAT TGATLTWTAS TDSGGSGLAG YEVLRVSGTT QTLVASPTTA 900
TVALAGLTPA TAYSYVVRAK DGAGNVSAVS SPVTFTTLPV TSTPSCTVVY 950
STNSWNVGFT GSVKITNTGT TPLTWTLGFA FPSGQQVTQG WSATWSQTGT 1000
TVTATGLSWN ATLQPGQSTD IGFNGSHPGT NTNPASFTVN GEVCG 1045
Length:1,045
Mass (Da):108,991
Last modified:May 1, 1992 - v1
Checksum:iAC2F7B84E4E3C4F0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64644 Genomic DNA. Translation: AAA23086.1.
PIRiA39199.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64644 Genomic DNA. Translation: AAA23086.1 .
PIRi A39199.

3D structure databases

ProteinModelPortali P26225.
SMRi P26225. Positions 35-641.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
2.60.40.10. 3 hits.
2.60.40.290. 1 hit.
2.60.40.710. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR003961. Fibronectin_type3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR013783. Ig-like_fold.
[Graphical view ]
Pfami PF00553. CBM_2. 1 hit.
PF00942. CBM_3. 1 hit.
PF00041. fn3. 3 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view ]
SMARTi SM00637. CBD_II. 1 hit.
SM01067. CBM_3. 1 hit.
SM00060. FN3. 3 hits.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF49265. SSF49265. 2 hits.
SSF49384. SSF49384. 2 hits.
PROSITEi PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51172. CBM3. 1 hit.
PS50853. FN3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Unusual sequence organization in CenB, an inverting endoglucanase from Cellulomonas fimi."
    Meinke A., Braun C., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
    J. Bacteriol. 173:308-314(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Multiple domains in endoglucanase B (CenB) from Cellulomonas fimi: functions and relatedness to domains in other polypeptides."
    Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
    J. Bacteriol. 173:7126-7135(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.

Entry informationi

Entry nameiGUNB_CELFI
AccessioniPrimary (citable) accession number: P26225
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: December 11, 2013
This is version 88 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

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