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Protein

Endoglucanase B

Gene

cenB

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score: 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 – 4101By similarity
Active sitei449 – 4491By similarity
Active sitei458 – 4581By similarity

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaActinobacteriaMicrococcalesCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 10451012Endoglucanase BPRO_0000007945Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi590998.Celf_0019.

Structurei

3D structure databases

ProteinModelPortaliP26225.
SMRiP26225. Positions 35-641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini493 – 642150CBM3PROSITE-ProRule annotationAdd
BLAST
Domaini653 – 74391Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini751 – 84090Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini849 – 94092Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini939 – 1045107CBM2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 492459CatalyticAdd
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

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

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. FN3_dom.
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

« Hide

        10         20         30         40         50
MLRQVPRTLV AGGSALAVAV GVLVAPLATG AAAAPTYNYA EALQKSMFFY
60 70 80 90 100
QAQRSGDLPA DFPVSWRGDS GLTDGADVGK DLTGGWYDAG DHVKFGFPMA
110 120 130 140 150
FSATMLAWGA IESPTGYSKA GSLDELKDNL RFVSDYFVKA HTAPNELYVQ
160 170 180 190 200
VGDGEADHKW WGPAEVMTMA RPSHKISASC PGSDVAAETA AALASSAIVL
210 220 230 240 250
KGDDPAYAAT LVSHAKQLYT FADTYRGAYS DCVTAASAYY KSWSGYQDEL
260 270 280 290 300
VWGAYWLYKA TGDATYLAKA EAEYDKLGTE NQSTTRSYKW TIAWDNKQFG
310 320 330 340 350
TYALLAMETG KQKYVDDANR WLDYWTVGVN GQKVPYSPGG QAVLDSWGAL
360 370 380 390 400
RYAANTSFVA LVYSDWMTDA TRKARYHDFG VRQINYALGD NPRSSSYVVG
410 420 430 440 450
FGANPPTAPH HRTAHGSWLD SITTPAQSRH VLYGALVGGP GSPNDAYTDS
460 470 480 490 500
RQDYVANEVA TDYNAGFTSA LARLVEEYGG TPLASFPTPE QPDGDQLFVE
510 520 530 540 550
AMLNQPPSGT FTEVKAMIRN QSAFPARSLK NAKVRYWFTT DGFAASDVTL
560 570 580 590 600
SANYSECGAQ SGKGVSAGGT LGYVELSCVG QDIHPGGQSQ HRREIQFRLT
610 620 630 640 650
GPAGWNPAND PSYTGLTQTA LAKASAITLY DGSTLVWGKE PTGTTTDTTP
660 670 680 690 700
PTTPGTPVAT GVTTVGASLS WAASTDAGSG VAGYELYRVQ GTTQTLVGTT
710 720 730 740 750
TAAAYILRDL TPGTAYSYVV KAKDVAGNVS AASAAVTFTT DTTGETEPPT
760 770 780 790 800
TPGTPVASAV TSTGATLAWA PSTGDPAVSG YDVLRVQGTT TTVVAQTTVP
810 820 830 840 850
TVTLSGLTPS TAYTYAVRAK NVAGDVSALS APVTFTTAAP PVDTVAPTVP
860 870 880 890 900
GTPVASNVAT TGATLTWTAS TDSGGSGLAG YEVLRVSGTT QTLVASPTTA
910 920 930 940 950
TVALAGLTPA TAYSYVVRAK DGAGNVSAVS SPVTFTTLPV TSTPSCTVVY
960 970 980 990 1000
STNSWNVGFT GSVKITNTGT TPLTWTLGFA FPSGQQVTQG WSATWSQTGT
1010 1020 1030 1040
TVTATGLSWN ATLQPGQSTD IGFNGSHPGT NTNPASFTVN GEVCG
Length:1,045
Mass (Da):108,991
Last modified:May 1, 1992 - v1
Checksum:iAC2F7B84E4E3C4F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64644 Genomic DNA. Translation: AAA23086.1.
PIRiA39199.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64644 Genomic DNA. Translation: AAA23086.1.
PIRiA39199.

3D structure databases

ProteinModelPortaliP26225.
SMRiP26225. Positions 35-641.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi590998.Celf_0019.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. FN3_dom.
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]
ProtoNetiSearch...

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: June 24, 2015
This is version 91 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.