ID   GUND_CELFI     STANDARD;      PRT;   747 AA.
AC   P50400;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   21-MAR-2006, entry version 46.
DE   Endoglucanase D precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase)
DE   (Cellulase).
GN   Name=cenD;
OS   Cellulomonas fimi.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93209933; PubMed=8458833;
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
RT   D (CenD), a family A beta-1,4-glucanase.";
RL   J. Bacteriol. 175:1910-1918(1993).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- PATHWAY: Cellulose degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
CC       family.
CC   -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
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DR   EMBL; L02544; AAA23089.1; -; Genomic_DNA.
DR   HSSP; P20533; 1K85.
DR   InterPro; IPR008965; Carb_bd.
DR   InterPro; IPR001919; CBD_bac.
DR   InterPro; IPR012291; CBD_carb_bd.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR008957; FN_III-like.
DR   InterPro; IPR003962; FnIII_subd.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00041; fn3; 2.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00060; FN3; 2.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL        1     39       Potential.
FT   CHAIN        40    747       Endoglucanase D.
FT                                /FTId=PRO_0000007843.
FT   DOMAIN      454    540       Fibronectin type-III 1.
FT   DOMAIN      550    635       Fibronectin type-III 2.
FT   DOMAIN      638    747       CBM2.
FT   ACT_SITE    208    208       Proton donor (By similarity).
FT   ACT_SITE    349    349       Nucleophile (By similarity).
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
//