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Protein

Endoglucanase B

Gene

cenB

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score: -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 disaccharide 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)DescriptionActionsGraphical viewLength
Active sitei410By similarity1
Active sitei449By similarity1
Active sitei458By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000000794534 – 1045Endoglucanase BAdd BLAST1012

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi946 ↔ 1044By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP26225

Structurei

3D structure databases

ProteinModelPortaliP26225
SMRiP26225
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini493 – 642CBM3PROSITE-ProRule annotationAdd BLAST150
Domaini653 – 743Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST91
Domaini751 – 840Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST90
Domaini849 – 940Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST92
Domaini939 – 1045CBM2PROSITE-ProRule annotationAdd BLAST107

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34 – 492CatalyticAdd BLAST459
Regioni644 – 650Linker ("hinge") (Pro-Thr box)7
Regioni734 – 748Linker ("hinge") (Pro-Thr box)Add BLAST15
Regioni831 – 846Linker ("hinge") (Pro-Thr box)Add BLAST16
Regioni931 – 944Linker ("hinge") (Pro-Thr box)Add BLAST14

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105CYP Bacteria
ENOG410XPC9 LUCA

Family and domain databases

CDDicd00063 FN3, 3 hits
Gene3Di1.50.10.10, 1 hit
2.60.40.10, 3 hits
2.60.40.290, 1 hit
2.60.40.710, 1 hit
InterProiView protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR001919 CBD2
IPR008965 CBM2/CBM3_carb-bd_dom_sf
IPR012291 CBM2_carb-bd_dom_sf
IPR018366 CBM2_CS
IPR001956 CBM3
IPR036966 CBM3_sf
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR001701 Glyco_hydro_9
IPR033126 Glyco_hydro_9_Asp/Glu_AS
IPR018221 Glyco_hydro_9_His_AS
IPR013783 Ig-like_fold
PfamiView protein in Pfam
PF00553 CBM_2, 1 hit
PF00942 CBM_3, 1 hit
PF00041 fn3, 3 hits
PF00759 Glyco_hydro_9, 1 hit
SMARTiView protein in SMART
SM00637 CBD_II, 1 hit
SM01067 CBM_3, 1 hit
SM00060 FN3, 3 hits
SUPFAMiSSF48208 SSF48208, 1 hit
SSF49265 SSF49265, 2 hits
SSF49384 SSF49384, 2 hits
PROSITEiView protein in PROSITE
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

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

Similar proteinsi

Entry informationi

Entry nameiGUNB_CELFI
AccessioniPrimary (citable) accession number: P26225
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 23, 2018
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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