CELDZ_THESZ
ID CELDZ_THESZ Reviewed; 385 AA.
AC A0A0U4EBH5;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Cellulase CelDZ1;
DE EC=3.2.1.4 {ECO:0000269|PubMed:26741138};
GN Name=celDZ1a {ECO:0000312|EMBL:ALX38276.1};
OS Thermoanaerobacterium sp.
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium;
OC unclassified Thermoanaerobacterium.
OX NCBI_TaxID=40549;
RN [1] {ECO:0000312|EMBL:ALX38276.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS)
RP OF 50-383, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, AND ACTIVITY REGULATION.
RC STRAIN=A57Txylan {ECO:0000312|EMBL:ALX38276.1};
RX PubMed=26741138; DOI=10.1371/journal.pone.0146454;
RA Zarafeta D., Kissas D., Sayer C., Gudbergsdottir S.R., Ladoukakis E.,
RA Isupov M.N., Chatziioannou A., Peng X., Littlechild J.A., Skretas G.,
RA Kolisis F.N.;
RT "Discovery and characterization of a thermostable and highly halotolerant
RT GH5 cellulase from an Icelandic hot spring isolate.";
RL PLoS ONE 11:E0146454-E0146454(2016).
CC -!- FUNCTION: Thermostable endoglucanase that has high activity with
CC soluble polymeric substrates containing beta-1,4-glycosidic bonds, such
CC as carboxymethyl cellulose (CMC) and barley beta-D-glucan (in vitro).
CC Has no activity with cellobiose and filter paper. Has no activity with
CC substrates containing beta-1,3-linked glycans, such as laminarin.
CC Likewise, lacks activity with xylan, galactomannan and pectin.
CC {ECO:0000269|PubMed:26741138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000269|PubMed:26741138};
CC -!- ACTIVITY REGULATION: Activity is enhanced by 1mM Mn(2+), but is not
CC affected by 1mM Ca(2+), Mg(2+), Zn(2+), K(+), Na(+) or Li(+). Activity
CC is not inhibited by EDTA (in vitro). {ECO:0000269|PubMed:26741138}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.1 mg/ml for carboxymethyl cellulose
CC {ECO:0000269|PubMed:26741138};
CC Note=kcat is 46.3 sec(-1) with carboxymethyl cellulose as substrate.
CC {ECO:0000269|PubMed:26741138};
CC pH dependence:
CC Optimum pH is 5 with carboxymethyl cellulose as substrate. Retains
CC 80% activity at pH 6, and about 50% at pH 7. Inactive at pH values
CC below 4 and above 9. {ECO:0000269|PubMed:26741138};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Retains about 85% activity
CC after 24 hours at 65 degrees Celsius. Retains at least 50% activity
CC after 4 hours at 70 degrees Celsius. Rapidly looses activity at 75
CC degrees Celsius. {ECO:0000269|PubMed:26741138};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26741138}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- BIOTECHNOLOGY: Thermostable endoglucanase that retains activity in the
CC presence of high salt concentrations, suggesting it might be used as an
CC industrial enzyme for cellulose-based substrates.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000255|RuleBase:RU361153}.
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DR EMBL; KT844947; ALX38276.1; -; Genomic_DNA.
DR PDB; 5FIP; X-ray; 1.88 A; A/B/C/D=50-383.
DR PDBsum; 5FIP; -.
DR AlphaFoldDB; A0A0U4EBH5; -.
DR SMR; A0A0U4EBH5; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
DR InterPro; IPR005086; CBM_fam_17/28.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF03424; CBM_17_28; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell membrane;
KW Cellulose degradation; Glycosidase; Hydrolase; Membrane;
KW Polysaccharide degradation; Transmembrane; Transmembrane helix.
FT CHAIN 1..385
FT /note="Cellulase CelDZ1"
FT /id="PRO_0000440609"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:26741138"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:26741138"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 300..301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 333..335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
SQ SEQUENCE 385 AA; 43215 MW; 56C2B14AFD678221 CRC64;
MNKWHINKWY FFVGMLVIFA VIISLILKDT SLTFSSYDRE KFPHLIGNSM VKKPSLAGRL
KIIEIDGRKT LGDQHGNPIQ LRGMSTHGLQ WFPQIINNNA FSALSKDWEA NVIRLAMYVG
EGGYSTDPSV KEKVIEGINL AIKNDMYVIV DWHILNPGDP NAKIYSGAKE FFKEIASKYP
NDLHIIYELA NEPNPTESDI TNDIAGWEKV KKYAEPIIKM LRDMGNENII IVGNPEWSTR
PDLAVNDPID DKNVMYSAHF YTGSASVWEN GNKGHIARNI EKALENGLTV FVTEWGTSEA
SGDGGPYLNE ADEWLEFLNS NNISWVNWSL ANKNEASAAF LPTTSLDPGN GKVWAVNQLS
LSGEYVRARI KGIPYKPISR ETMGK
