ID   GUNA_CELFI     STANDARD;      PRT;   449 AA.
AC   P07984;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   21-MAR-2006, entry version 58.
DE   Endoglucanase A precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase)
DE   (Cellulase).
GN   Name=cenA;
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=87055249; PubMed=3023193; DOI=10.1016/0378-1119(86)90196-4;
RA   Wong W.K.R., Gerhard B., Guo Z.M., Kilburn D.G., Warren R.A.J.,
RA   Miller R.C. Jr.;
RT   "Characterization and structure of an endoglucanase gene cenA of
RT   Cellulomonas fimi.";
RL   Gene 44:315-324(1986).
RN   [2]
RP   DOMAINS.
RX   MEDLINE=90036847; PubMed=2681184;
RA   Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.;
RT   "Structural and functional analysis of a bacterial cellulase by
RT   proteolysis.";
RL   J. Biol. Chem. 264:17802-17808(1989).
RN   [3]
RP   DISULFIDE BONDS.
RX   MEDLINE=92104156; PubMed=1761039;
RA   Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A.,
RA   Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.;
RT   "Structural and functional relationships in two families of
RT   beta-1,4-glycanases.";
RL   Eur. J. Biochem. 202:367-377(1991).
CC   -!- FUNCTION: The biological conversion of cellulose to glucose
CC       generally requires three types of hydrolytic enzymes: (1)
CC       Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2)
CC       Exocellobiohydrolases that cut the dissaccharide cellobiose from
CC       the nonreducing end of the cellulose polymer chain; (3)
CC       Beta-1,4-glucosidases which hydrolyze the cellobiose and other
CC       short cello-oligosaccharides to glucose.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- PTM: The linker region (also termed "hinge") may be a potential
CC       site for proteolysis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B)
CC       family.
CC   -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
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DR   EMBL; M15823; AAA23084.1; -; Genomic_DNA.
DR   PIR; A24993; A24993.
DR   HSSP; P07986; 1EXG.
DR   InterPro; IPR008965; Carb_bd.
DR   InterPro; IPR001919; CBD_bac.
DR   InterPro; IPR012291; CBD_carb_bd.
DR   InterPro; IPR001524; Glyco_hydro_6.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   ProDom; PD003733; Glyco_hydro_6; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL        1     31
FT   CHAIN        32    449       Endoglucanase A.
FT                                /FTId=PRO_0000007903.
FT   DOMAIN       32    137       CBM2.
FT   REGION      139    168       Linker ("hinge") (Pro-Thr box).
FT   REGION      438    449       Catalytic.
FT   ACT_SITE    247    247       By similarity.
FT   ACT_SITE    283    283       Proton donor (By similarity).
FT   ACT_SITE    423    423       Nucleophile (By similarity).
FT   DISULFID     35    134
FT   DISULFID    248    291
FT   DISULFID    390    426
SQ   SEQUENCE   449 AA;  46731 MW;  67FF887814B3348D CRC64;
     MSTRRTAAAL LAAAAVAVGG LTALTTTAAQ AAPGCRVDYA VTNQWPGGFG ANVTITNLGD
     PVSSWKLDWT YTAGQRIQQL WNGTASTNGG QVSVTSLPWN GSIPTGGTAS FGFNGSWAGS
     NPTPASFSLN GTTCTGTVPT TSPTPTPTPT TPTPTPTPTP TPTPTVTPQP TSGFYVDPTT
     QGYRAWQAAS GTDKALLEKI ALTPQAYWVG NWADASHAQA EVADYTGRAV AAGKTPMLVV
     YAIPGRDCGS HSGGGVSESE YARWVDTVAQ GIKGNPIVIL EPDALAQLGD CSGQGDRVGF
     LKYAAKSLTL KGARVYIDAG HAKWLSVDTP VNRLNQVGFE YAVGFALNTS NYQTTADSKA
     YGQQISQRLG GKKFVIDTSR NGNGSNGEWC NPRGRALGER PVAVNDGSGL DALLWVKLPG
     ESDGACNGGP AAGQWWQEIA LEMARNARW
//