ID   GUND_CELFI              Reviewed;         747 AA.
AC   P50400;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   28-JUN-2023, entry version 121.
DE   RecName: Full=Endoglucanase D;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase D;
DE   AltName: Full=Endo-1,4-beta-glucanase D;
DE   Flags: Precursor;
GN   Name=cenD;
OS   Cellulomonas fimi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8458833; DOI=10.1128/jb.175.7.1910-1918.1993;
RA   Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.;
RT   "Cellulose-binding polypeptides from Cellulomonas fimi: endoglucanase D
RT   (CenD), a family A beta-1,4-glucanase.";
RL   J. Bacteriol. 175:1910-1918(1993).
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; L02544; AAA23089.1; -; Genomic_DNA.
DR   PIR; B47093; B47093.
DR   RefSeq; WP_013771080.1; NZ_LR134387.1.
DR   AlphaFoldDB; P50400; -.
DR   SMR; P50400; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   OrthoDB; 4902692at2; -.
DR   UniPathway; UPA00696; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00041; fn3; 2.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..747
FT                   /note="Endoglucanase D"
FT                   /id="PRO_0000007843"
FT   DOMAIN          456..543
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          552..639
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          638..747
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   REGION          456..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   747 AA;  78937 MW;  BD15473C9D8B42BD CRC64;
     MHSASRTRAR TRVRTAVSGL LAATVLAAPL TLVAAPAQAA TGDDWLHVEG NTIVDSTGKE
     AILSGVNWFG FNASERVFHG LWSGNITQIT QQMAQRGINV VRVPVSTQLL LEWKAGTFLK
     PNVNTYANPE LEGKNSLQIF EYWLTLCQKY GIKVFLDVHS AEADNSGHVY NMWWKGDITT
     EDVYEGWEWA ATRWKDDDTI VGADIKNEPH GTQGSTERAK WDGTTDKDNF KHFAETASKK
     ILAINPNWLV FVEGVEIYPK PGVPWTSTGL TDYYGTWWGG NLRGVRDHPI DLGAHQDQLV
     YSPHDYGPLV FDQKWFQKDF DKASLTADVW GPNWLFIHDE DIAPLLIGEW GGRLGQDPRQ
     DKWMAALRDL VAERRLSQTF WVLNPNSGDT GGLLLDDWKT WDEVKYSTML EPTLWKHGGK
     YVGLDHQVPL GGVGSTTGTS ISQVGGGTPD TTAPTAPTGL RAGTPTASTV PLTWSASTDT
     GGSGVAGYEV YRGTTLVGTT TATSYTVTGL AADSAYTFSV RAKDGAGNTS AASAAVTART
     AAGGGDVTAP SVPTGLTAGT PTATSVPLTW TASTDTGGSG VTGYEVYRGS TLVARPTGTS
     HTVTGLSAAT AYTFTVRAVD AAGNVSAASA PVGVTTAPDP TTGSCAVTYT ANGWSGGFTA
     AVTLTNTGTT ALSGWTLGFA FPSGQTLTQG WSARWAQSGS SVTATNEAWN AVLAPGASVE
     IGFSGTHTGT NTAPATFTVG GATCTTR
//