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Protein

Endoglucanase/exoglucanase B

Gene

celB

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

This protein is made up of two domains: the N-terminal domain has exoglucanase activity while the C-terminal domain is an endoglucanase.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei177Proton donorSequence analysis1
Active sitei285NucleophilePROSITE-ProRule annotation1
Active sitei792By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Multifunctional enzyme
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM3 Carbohydrate-Binding Module Family 3
GH10 Glycoside Hydrolase Family 10
GH5 Glycoside Hydrolase Family 5

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase/exoglucanase B
Including the following 2 domains:
Alternative name(s):
Cellobiohydrolase
Cellulase
Endo-1,4-beta-glucanase
Exoglucanase (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase
Gene namesi
Name:celB
OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifieri44001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Add BLAST28
ChainiPRO_000000798329 – 1039Endoglucanase/exoglucanase BAdd BLAST1011

Structurei

3D structure databases

ProteinModelPortaliP10474
SMRiP10474
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 372GH10PROSITE-ProRule annotationAdd BLAST334
Domaini418 – 571CBM3PROSITE-ProRule annotationAdd BLAST154

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi376 – 416Pro/Thr-richAdd BLAST41
Compositional biasi574 – 618Pro/Thr-richAdd BLAST45

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyl hydrolase 10 (cellulase F) family.Curated
In the C-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105CYP Bacteria
COG2730 LUCA
COG3693 LUCA

Family and domain databases

Gene3Di2.60.40.710, 1 hit
InterProiView protein in InterPro
IPR008965 CBM2/CBM3_carb-bd_dom_sf
IPR001956 CBM3
IPR036966 CBM3_sf
IPR001000 GH10
IPR031158 GH10_AS
IPR001547 Glyco_hydro_5
IPR018087 Glyco_hydro_5_CS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00942 CBM_3, 1 hit
PF00150 Cellulase, 1 hit
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM01067 CBM_3, 1 hit
SM00633 Glyco_10, 1 hit
SUPFAMiSSF49384 SSF49384, 1 hit
SSF51445 SSF51445, 2 hits
PROSITEiView protein in PROSITE
PS51172 CBM3, 1 hit
PS00591 GH10_1, 1 hit
PS51760 GH10_2, 1 hit
PS00659 GLYCOSYL_HYDROL_F5, 1 hit

Sequencei

Sequence statusi: Complete.

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

P10474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRNLFRIVS RVVLIAFIAS ISLVGAMSYF PVETQAAPDW SIPSLCESYK
60 70 80 90 100
DDFMIGVAIP ARCLSNDTDK RMVLKHFNSI TAENEMKPES LLAGQTSTGL
110 120 130 140 150
SYRFSTADAF VDFASTNKIG IRGHTLVWHN QTPDWFFKDS NGQRLSKDAL
160 170 180 190 200
LARLKQYIYD VVGRYKGKVY AWDVVNEAID ENQPDSYRRS TWYEICGPEY
210 220 230 240 250
IEKAFIWAHE ADPNAKLFYN DYNTEISKKR DFIYNMVKNL KSKGIPIHGI
260 270 280 290 300
GMQCHINVNW PSVSEIENSI KLFSSIPGIE IHITELDMSL YNYGSSENYS
310 320 330 340 350
TPPQDLLQKQ SQKYKEIFTM LKKYKNVVKS VTFWGLKDDY SWLRSFYGKN
360 370 380 390 400
DWPLLFFEDY SAKPAYWAVI EASGVTTSSP TPTPTPTVTV TPTPTPTPTP
410 420 430 440 450
TVTATPTPTP TPVSTPATGG QIKVLYANKE TNSTTNTIRP WLKVVNSGSS
460 470 480 490 500
SIDLSRVTIR YWYTVDGERA QSAVSDWAQI GASNVTFKFV KLSSSVSGAD
510 520 530 540 550
YYLEIGFKSG AGQLQPGKDT GEIQIRFNKS DWSNYNQGND WSWLQSMTSY
560 570 580 590 600
GENEKVTAYI DGVLVWGQEP SGATPAPTMT VAPTATPTPT LSPTVTPTPA
610 620 630 640 650
PTQTAIPTPT LTPNPTPTSS IPDDTNDDWL YVSGNKIVDK DGRPVWLTGI
660 670 680 690 700
NWFGYNTGTN VFDGVWSCNL KDTLAEIANR GFNLLRVPIS AELILNWSQG
710 720 730 740 750
IYPKPNINYY VNPELEGKNS LEVFDIVVQT CKEVGLKIML DIHSIKTDAM
760 770 780 790 800
GHIYPVWYDE KFTPEDFYKA CEWITNRYKN DDTIIAFDLK NEPHGKPWQD
810 820 830 840 850
TTFAKWDNST DINNWKYAAE TCAKRILNIN PNLLIVIEGI EAYPKDDVTW
860 870 880 890 900
TSKSSSDYYS TWWGGNLRGV RKYPINLGKY QNKVVYSPHD YGPSVYQQPW
910 920 930 940 950
FYPGFTKESL LQDCWRPNWA YIMEENIAPL LIGEWGGHLD GADNEKWMKY
960 970 980 990 1000
LRDYIIENHI HHTFWCFNAN SGDTGGLVGY DFTTWDEKKY SFLKPALWQD
1010 1020 1030
SQGRFVGLDH KRPLGTNGKN INITTYYNNN EPEPVPASK
Length:1,039
Mass (Da):117,641
Last modified:July 1, 1989 - v1
Checksum:i0E0378171594DDAE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13602 Genomic DNA Translation: CAA31936.1
PIRiS02711

Similar proteinsi

Entry informationi

Entry nameiGUNB_CALSA
AccessioniPrimary (citable) accession number: P10474
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 28, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health