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Cellulase/esterase CelE (CtCel5C-CE2) [Includes: Cellulase E (EC 3.2.1.4) (CtCel5C) (Endo-1,4-beta-glucanase E) (EGE) (Endoglucanase E); Acetylxylan esterase / glucomannan deacetylase (EC 3.1.1.-) (EC 3.1.1.72) (CtCE2)]

 CELE_CLOTH              Reviewed;         814 AA.
P10477; A3DDK3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
14-OCT-2015, sequence version 2.
28-FEB-2018, entry version 110.
RecName: Full=Cellulase/esterase CelE {ECO:0000305};
AltName: Full=CtCel5C-CE2 {ECO:0000303|PubMed:19338387};
Includes:
RecName: Full=Cellulase E {ECO:0000303|PubMed:3066698};
EC=3.2.1.4 {ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698};
AltName: Full=CtCel5C {ECO:0000303|PubMed:19338387};
AltName: Full=Endo-1,4-beta-glucanase E {ECO:0000303|PubMed:3066698};
Short=EGE {ECO:0000303|PubMed:3066698};
Short=Endoglucanase E {ECO:0000303|PubMed:3066698};
Includes:
RecName: Full=Acetylxylan esterase / glucomannan deacetylase {ECO:0000305|PubMed:19338387};
EC=3.1.1.- {ECO:0000269|PubMed:19338387};
EC=3.1.1.72 {ECO:0000269|PubMed:19338387};
AltName: Full=CtCE2 {ECO:0000303|PubMed:19338387};
Flags: Precursor;
Name=celE {ECO:0000303|PubMed:3066698};
OrderedLocusNames=Cthe_0797 {ECO:0000312|EMBL:ABN52032.1};
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 /
NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium
thermocellum).
Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
Ruminiclostridium.
NCBI_TaxID=203119;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-58,
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536
/ VPI 7372;
PubMed=3066698; DOI=10.1016/0378-1119(88)90375-7;
Hall J., Hazlewood G.P., Barker P.J., Gilbert H.J.;
"Conserved reiterated domains in Clostridium thermocellum
endoglucanases are not essential for catalytic activity.";
Gene 69:29-38(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536
/ VPI 7372;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.;
"Complete sequence of Clostridium thermocellum ATCC 27405.";
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, CATALYTIC ACTIVITY, CELLULOSE-BINDING, AND DOMAIN.
PubMed=1991028; DOI=10.1042/bj2730289;
Durrant A.J., Hall J., Hazlewood G.P., Gilbert H.J.;
"The non-catalytic C-terminal region of endoglucanase E from
Clostridium thermocellum contains a cellulose-binding domain.";
Biochem. J. 273:289-293(1991).
[4]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 485-814 OF WILD-TYPE AND
MUTANT ALA-612 IN COMPLEX WITH CELLOHEXAOSE, FUNCTION, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, ENZYME REGULATION,
MUTAGENESIS OF SER-612; ASP-789 AND HIS-791, ACTIVE SITE, AND PATHWAY.
STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536
/ VPI 7372;
PubMed=19338387; DOI=10.1371/journal.pbio.1000071;
Montanier C., Money V.A., Pires V.M., Flint J.E., Pinheiro B.A.,
Goyal A., Prates J.A., Izumi A., Stalbrand H., Morland C.,
Cartmell A., Kolenova K., Topakas E., Dodson E.J., Bolam D.N.,
Davies G.J., Fontes C.M., Gilbert H.J.;
"The active site of a carbohydrate esterase displays divergent
catalytic and noncatalytic binding functions.";
PLoS Biol. 7:E71-E71(2009).
[5]
X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 51-386.
Bianchetti C.M., Takasuka T.E., Fox B.G.;
"Multifunctional cellulase, xylanase, mannanase.";
Submitted (JAN-2013) to the PDB data bank.
-!- FUNCTION: Multifunctional enzyme involved in the degradation of
plant cell wall polysaccharides. Displays endoglucanase activity
against carboxymethyl cellulose (CMC) and barley beta-glucan
(PubMed:3066698, PubMed:1991028). Also catalyzes the deacetylation
of acetylated birchwood xylan and glucomannan, with a preference
for the latter, and of the synthetic substrate 4-nitrophenyl
acetate (4-NPAc) (PubMed:19338387). {ECO:0000269|PubMed:19338387,
ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698}.
-!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
linkages in cellulose, lichenin and cereal beta-D-glucans.
{ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698}.
-!- CATALYTIC ACTIVITY: Deacetylation of xylans and xylo-
oligosaccharides. {ECO:0000269|PubMed:19338387}.
-!- ENZYME REGULATION: Esterase activity of the CE2 module is
inhibited when this domain binds to cellohexaose or beta-glucan.
{ECO:0000269|PubMed:19338387}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=165 uM for 4-nitrophenyl acetate
{ECO:0000269|PubMed:19338387};
KM=2.7 mM for acetylated birchwood xylan
{ECO:0000269|PubMed:19338387};
KM=0.019 mM for acetylated glucomannan
{ECO:0000269|PubMed:19338387};
Note=kcat is 7032 min(-1) for the deacetylation of 4-nitrophenyl
acetate. kcat is 12 min(-1) for the deacetylation of birchwood
xylan. kcat is 1.1 min(-1) for the deacetylation of glucomannan.
{ECO:0000269|PubMed:19338387};
-!- PATHWAY: Glycan metabolism; cellulose degradation.
{ECO:0000269|PubMed:3066698}.
-!- PATHWAY: Glycan degradation; xylan degradation.
{ECO:0000269|PubMed:19338387}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- DOMAIN: Contains an N-terminal module that displays cellulase
activity (CtCel5C), a central type I dockerin module (Doc) that
facilitates the integration of the enzyme into the cellulosome,
and a C-terminal module, CtCE2, which displays dual activities: it
catalyzes the deacetylation of plant polysaccharides and also
potentiates the activity of its appended cellulase catalytic
module through its non-catalytic cellulose binding function.
{ECO:0000269|PubMed:19338387, ECO:0000269|PubMed:1991028}.
-!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
hydrolase 5 (cellulase A) family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the carbohydrate
esterase 2 (CE2) family. {ECO:0000305|PubMed:19338387}.
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EMBL; M22759; AAA23224.1; -; Genomic_DNA.
EMBL; CP000568; ABN52032.1; -; Genomic_DNA.
PIR; JT0347; CZCLEM.
RefSeq; WP_011837903.1; NC_009012.1.
PDB; 2WAB; X-ray; 1.90 A; A=485-814.
PDB; 2WAO; X-ray; 1.80 A; A=485-814.
PDB; 4IM4; X-ray; 2.42 A; A/B/C/D/E/F=51-386.
PDBsum; 2WAB; -.
PDBsum; 2WAO; -.
PDBsum; 4IM4; -.
ProteinModelPortal; P10477; -.
SMR; P10477; -.
STRING; 203119.Cthe_0797; -.
CAZy; GH5; Glycoside Hydrolase Family 5.
EnsemblBacteria; ABN52032; ABN52032; Cthe_0797.
KEGG; cth:Cthe_0797; -.
eggNOG; ENOG4108K2F; Bacteria.
eggNOG; COG2730; LUCA.
KO; K01179; -.
OMA; CAYGNEG; -.
OrthoDB; POG091H14IK; -.
BioCyc; CTHE203119:G1G86-831-MONOMER; -.
BioCyc; MetaCyc:MONOMER-16425; -.
UniPathway; UPA00114; -.
UniPathway; UPA00696; -.
EvolutionaryTrace; P10477; -.
Proteomes; UP000002145; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046555; F:acetylxylan esterase activity; IDA:UniProtKB.
GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
GO; GO:0030248; F:cellulose binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
GO; GO:2000884; P:glucomannan catabolic process; IDA:UniProtKB.
GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
CDD; cd01831; Endoglucanase_E_like; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.1110; -; 1.
InterPro; IPR037461; CtCE2_like_dom.
InterPro; IPR002105; Dockerin_1_rpt.
InterPro; IPR016134; Dockerin_dom.
InterPro; IPR036439; Dockerin_dom_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR001547; Glyco_hydro_5.
InterPro; IPR018087; Glyco_hydro_5_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR013830; SGNH_hydro.
InterPro; IPR036514; SGNH_hydro_sf.
Pfam; PF00150; Cellulase; 1.
Pfam; PF00404; Dockerin_1; 2.
Pfam; PF13472; Lipase_GDSL_2; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF63446; SSF63446; 1.
PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
PROSITE; PS51766; DOCKERIN; 1.
PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
1: Evidence at protein level;
3D-structure; Calcium; Carbohydrate metabolism; Cellulose degradation;
Complete proteome; Direct protein sequencing; Glycosidase; Hydrolase;
Metal-binding; Multifunctional enzyme; Polysaccharide degradation;
Reference proteome; Secreted; Signal.
SIGNAL 1 34 {ECO:0000269|PubMed:3066698}.
CHAIN 35 814 Cellulase/esterase CelE.
/FTId=PRO_0000007852.
DOMAIN 409 479 Dockerin. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
REGION 35 354 Cellulase. {ECO:0000305}.
REGION 490 814 Esterase. {ECO:0000305}.
ACT_SITE 193 193 Proton donor; for cellulase activity.
{ECO:0000250}.
ACT_SITE 316 316 Nucleophile; for cellulase activity.
{ECO:0000250|UniProtKB:A7LXT7}.
ACT_SITE 612 612 Nucleophile; for esterase activity.
{ECO:0000305|PubMed:19338387}.
METAL 415 415 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 417 417 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 419 419 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 420 420 Calcium 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU01102}.
METAL 421 421 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU01102}.
METAL 426 426 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 451 451 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 451 451 Calcium 3. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 452 452 Calcium 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU01102}.
METAL 453 453 Calcium 3. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 455 455 Calcium 3. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 457 457 Calcium 2; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU01102}.
METAL 457 457 Calcium 3; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU01102}.
METAL 462 462 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
METAL 462 462 Calcium 3. {ECO:0000255|PROSITE-
ProRule:PRU01102}.
SITE 658 658 Transition state stabilizer.
{ECO:0000250|UniProtKB:B3PIB0}.
SITE 705 705 Transition state stabilizer.
{ECO:0000250|UniProtKB:B3PIB0}.
SITE 791 791 Increases nucleophilicity of active site
Ser. {ECO:0000305|PubMed:19338387}.
MUTAGEN 612 612 S->A: Loss of esterase activity. 8-fold
increase in the binding affinity to
cellohexaose.
{ECO:0000269|PubMed:19338387}.
MUTAGEN 789 789 D->A,N: Retains significant esterase
activity against 4-NPAc and the polymeric
substrates.
{ECO:0000269|PubMed:19338387}.
MUTAGEN 791 791 H->A: Loss of esterase activity. 20-fold
decrease in the binding affinity to
cellohexaose.
{ECO:0000269|PubMed:19338387}.
CONFLICT 147 147 V -> L (in Ref. 1; AAA23224).
{ECO:0000305}.
HELIX 57 64 {ECO:0000244|PDB:4IM4}.
STRAND 66 70 {ECO:0000244|PDB:4IM4}.
STRAND 76 78 {ECO:0000244|PDB:4IM4}.
TURN 79 82 {ECO:0000244|PDB:4IM4}.
HELIX 89 97 {ECO:0000244|PDB:4IM4}.
STRAND 102 105 {ECO:0000244|PDB:4IM4}.
HELIX 110 112 {ECO:0000244|PDB:4IM4}.
TURN 116 118 {ECO:0000244|PDB:4IM4}.
HELIX 123 138 {ECO:0000244|PDB:4IM4}.
STRAND 142 145 {ECO:0000244|PDB:4IM4}.
TURN 151 153 {ECO:0000244|PDB:4IM4}.
TURN 158 160 {ECO:0000244|PDB:4IM4}.
HELIX 161 178 {ECO:0000244|PDB:4IM4}.
TURN 179 181 {ECO:0000244|PDB:4IM4}.
STRAND 186 190 {ECO:0000244|PDB:4IM4}.
TURN 200 205 {ECO:0000244|PDB:4IM4}.
HELIX 208 226 {ECO:0000244|PDB:4IM4}.
TURN 230 234 {ECO:0000244|PDB:4IM4}.
STRAND 237 239 {ECO:0000244|PDB:4IM4}.
HELIX 242 244 {ECO:0000244|PDB:4IM4}.
HELIX 248 251 {ECO:0000244|PDB:4IM4}.
HELIX 257 259 {ECO:0000244|PDB:4IM4}.
STRAND 263 268 {ECO:0000244|PDB:4IM4}.
HELIX 273 276 {ECO:0000244|PDB:4IM4}.
HELIX 288 304 {ECO:0000244|PDB:4IM4}.
HELIX 306 308 {ECO:0000244|PDB:4IM4}.
STRAND 312 317 {ECO:0000244|PDB:4IM4}.
HELIX 325 340 {ECO:0000244|PDB:4IM4}.
TURN 341 343 {ECO:0000244|PDB:4IM4}.
STRAND 345 350 {ECO:0000244|PDB:4IM4}.
TURN 367 370 {ECO:0000244|PDB:4IM4}.
STRAND 371 373 {ECO:0000244|PDB:4IM4}.
HELIX 375 385 {ECO:0000244|PDB:4IM4}.
STRAND 493 496 {ECO:0000244|PDB:2WAO}.
STRAND 514 522 {ECO:0000244|PDB:2WAO}.
STRAND 524 540 {ECO:0000244|PDB:2WAO}.
STRAND 548 560 {ECO:0000244|PDB:2WAO}.
STRAND 565 574 {ECO:0000244|PDB:2WAO}.
HELIX 578 580 {ECO:0000244|PDB:2WAO}.
STRAND 583 589 {ECO:0000244|PDB:2WAO}.
STRAND 593 595 {ECO:0000244|PDB:2WAO}.
STRAND 603 611 {ECO:0000244|PDB:2WAO}.
HELIX 612 615 {ECO:0000244|PDB:2WAO}.
TURN 616 620 {ECO:0000244|PDB:2WAO}.
HELIX 630 632 {ECO:0000244|PDB:2WAO}.
HELIX 635 637 {ECO:0000244|PDB:2WAO}.
HELIX 639 646 {ECO:0000244|PDB:2WAO}.
STRAND 649 655 {ECO:0000244|PDB:2WAO}.
HELIX 665 667 {ECO:0000244|PDB:2WAO}.
HELIX 673 676 {ECO:0000244|PDB:2WAO}.
STRAND 679 681 {ECO:0000244|PDB:2WAO}.
TURN 682 685 {ECO:0000244|PDB:2WAO}.
HELIX 690 692 {ECO:0000244|PDB:2WAO}.
STRAND 696 701 {ECO:0000244|PDB:2WAO}.
HELIX 704 707 {ECO:0000244|PDB:2WAO}.
STRAND 708 710 {ECO:0000244|PDB:2WAO}.
HELIX 714 731 {ECO:0000244|PDB:2WAO}.
STRAND 736 741 {ECO:0000244|PDB:2WAO}.
HELIX 747 766 {ECO:0000244|PDB:2WAO}.
STRAND 771 776 {ECO:0000244|PDB:2WAO}.
HELIX 788 790 {ECO:0000244|PDB:2WAO}.
HELIX 794 812 {ECO:0000244|PDB:2WAO}.
SEQUENCE 814 AA; 90230 MW; 9913A8E252CBBF8D CRC64;
MKKIVSLVCV LVMLVSILGS FSVVAASPVK GFQVSGTKLL DASGNELVMR GMRDISAIDL
VKEIKIGWNL GNTLDAPTET AWGNPRTTKA MIEKVREMGF NAVRVPVTWD THIGPAPDYK
IDEAWLNRVE EVVNYVLDCG MYAIINVHHD NTWIIPTYAN EQRSKEKLVK VWEQIATRFK
DYDDHLLFET MNEPREVGSP MEWMGGTYEN RDVINRFNLA VVNTIRASGG NNDKRFILVP
TNAATGLDVA LNDLVIPNND SRVIVSIHAY SPYFFAMDVN GTSYWGSDYD KASLTSELDA
IYNRFVKNGR AVIIGEFGTI DKNNLSSRVA HAEHYAREAV SRGIAVFWWD NGYYNPGDAE
TYALLNRKTL SWYYPEIVQA LMRGAGVEPL VSPTPTPTLM PTPSPTVTAN ILYGDVNGDG
KINSTDCTML KRYILRGIEE FPSPSGIIAA DVNADLKINS TDLVLMKKYL LRSIDKFPAE
DSQTPDEDNP GILYNGRFDF SDPNGPKCAW SGSNVELNFY GTEASVTIKS GGENWFQAIV
DGNPLPPFSV NATTSTVKLV SGLAEGAHHL VLWKRTEASL GEVQFLGFDF GSGKLLAAPK
PLERKIEFIG DSITCAYGNE GTSKEQSFTP KNENSYMSYA AITARNLNAS ANMIAWSGIG
LTMNYGGAPG PLIMDRYPYT LPYSGVRWDF SKYVPQVVVI NLGTNDFSTS FADKTKFVTA
YKNLISEVRR NYPDAHIFCC VGPMLWGTGL DLCRSYVTEV VNDCNRSGDL KVYFVEFPQQ
DGSTGYGEDW HPSIATHQLM AERLTAEIKN KLGW


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