ID   GUND_RUMCH              Reviewed;         584 AA.
AC   P25472; B8I8I3;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Endoglucanase D;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase D;
DE   AltName: Full=EGCCD;
DE   AltName: Full=Endo-1,4-beta-glucanase D;
DE   Flags: Precursor;
GN   Name=celCCD; OrderedLocusNames=Ccel_0840;
OS   Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10) (Clostridium cellulolyticum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=394503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1916275; DOI=10.1016/0378-1119(91)90461-j;
RA   Shima S., Igarashi Y., Kodama T.;
RT   "Nucleotide sequence analysis of the endoglucanase-encoding gene, celCCD,
RT   of Clostridium cellulolyticum.";
RL   Gene 104:33-38(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC       requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC       cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC       cut the disaccharide cellobiose from the non-reducing end of the
CC       cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC       cellobiose and other short cello-oligosaccharides to glucose.
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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; D90341; BAA14354.1; -; Genomic_DNA.
DR   EMBL; CP001348; ACL75216.1; -; Genomic_DNA.
DR   RefSeq; WP_015924376.1; NC_011898.1.
DR   AlphaFoldDB; P25472; -.
DR   SMR; P25472; -.
DR   STRING; 394503.Ccel_0840; -.
DR   CAZy; CBM11; Carbohydrate-Binding Module Family 11.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblBacteria; ACL75216; ACL75216; Ccel_0840.
DR   KEGG; cce:Ccel_0840; -.
DR   eggNOG; COG2730; Bacteria.
DR   HOGENOM; CLU_484782_0_0_9; -.
DR   OMA; WFRTTAL; -.
DR   OrthoDB; 1395441at2; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001349; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1330.10; -; 1.
DR   InterPro; IPR005087; CBM_fam11.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF03425; CBM_11; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..584
FT                   /note="Endoglucanase D"
FT                   /id="PRO_0000007846"
FT   DOMAIN          354..584
FT                   /note="CBM11"
FT   DOMAIN          524..584
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   REGION          25..328
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        159
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   584 AA;  66062 MW;  0FC41257E81322C3 CRC64;
     MKKILALIIS CSIIMSFLPM SVYGAINSQD MVKKMGIGMN LGNTFDAPTE GSWSKAAQEY
     YFDDFKQAGF KHVRIPIRWD QHTLANSPYT VDSNFLNRIE TVIDWSLSRG FVTVINSHHD
     TWLMDNYSQN IGRFEKIWEQ IAQRFKGKSE NLVFEILNEP HGNITDSQIN DMNKRILNII
     RKTNPTRNVI IGAGYWNSYN SLSQLEIPND PNLIATFHYY DPYSFTHQWQ GTWGTKNDMD
     AIAMVFNHVK KWSDKNNIPV YLGEYGVMGH SDRTSAVKWF DFVSDQAISH GFSCGAWDNG
     VFGSVDNDMA FYNRDTRQFD KEILNAILTT GTTYDWTPPT ETNPDPPRTP ATPAYGEQLI
     EDFEGAMQWA AYSGVDATAS CKISSGKSNN GLEITYAGSS NGYWGVVDNE HRNQDWEKWQ
     KISFDIKSSN TNEVRLLIAE QSKIEGEDGE HWTYVIKPST SWTTIEIPFS SFTKRMDYQP
     PAQDGSETFD LYKVGSLHFM YSNSNSGTLN IDNIKLIGLP EEQIGGKIGD VNEDGNIDAI
     DFALLKKYLL DSSISINKVN ADINLDGDIN AIDFAKLKMM LLGD