ID   GUXB_CELFI     STANDARD;      PRT;  1090 AA.
AC   P50899;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   21-MAR-2006, entry version 44.
DE   Exoglucanase B precursor (EC 3.2.1.91) (Exocellobiohydrolase B)
DE   (1,4-beta-cellobiohydrolase B) (CBP120).
GN   Name=cbhB; Synonyms=cenE;
OS   Cellulomonas fimi.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 456-461.
RC   STRAIN=ATCC 484;
RX   MEDLINE=96003898; PubMed=7575482;
RA   Shen H., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.;
RT   "Cellobiohydrolase B, a second exo-cellobiohydrolase from the
RT   cellulolytic bacterium Cellulomonas fimi.";
RL   Biochem. J. 311:67-74(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 54-75.
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 54-78.
RX   MEDLINE=94197708; PubMed=8147863;
RA   Shen H., Tomme P., Meinke A., Gilkes N.R., Kilburn D.G.,
RA   Warren R.A.J., Miller R.C. Jr.;
RT   "Stereochemical course of hydrolysis catalysed by Cellulomonas fimi
RT   CenE, a member of a new family of beta-1,4-glucanases.";
RL   Biochem. Biophys. Res. Commun. 199:1223-1228(1994).
CC   -!- FUNCTION: Hydrolyzes cellohexaose to a mixture of cellotetraose,
CC       cellotriose and cellobiose, with only a trace of glucose. It
CC       hydrolyzed cellopentaose to cellotriose and cellobiose, and
CC       cellotetraose to cellobiose, but it did not hydrolyze cellotriose.
CC       Has also weak endoglucanase activity. Hydrolyzes glucosidic bonds
CC       with inversion of anomeric configuration.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of 1,4-beta-D-glucosidic linkages
CC       in cellulose and cellotetraose, releasing cellobiose from the non-
CC       reducing ends of the chains.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 48 (cellulase L)
CC       family.
CC   -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
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DR   EMBL; L38827; AAB00822.1; -; Genomic_DNA.
DR   PIR; S59077; S59077.
DR   HSSP; P37698; 1FAE.
DR   InterPro; IPR008928; 6hp_glycosidase.
DR   InterPro; IPR008965; Carb_bd.
DR   InterPro; IPR001919; CBD_bac.
DR   InterPro; IPR012291; CBD_carb_bd.
DR   InterPro; IPR012341; CelA/Cel48F_cat.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR008957; FN_III-like.
DR   InterPro; IPR000556; Glyco_hydro_48.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF02011; Glyco_hydro_48; 1.
DR   PRINTS; PR00844; GLHYDRLASE48.
DR   ProDom; PD011903; Glyco_hydro_48; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00060; FN3; 3.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS50853; FN3; 3.
KW   Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL        1     33       Potential.
FT   PROPEP       34     53
FT                                /FTId=PRO_0000008028.
FT   CHAIN        54   1090       Exoglucanase B.
FT                                /FTId=PRO_0000008029.
FT   DOMAIN      704    787       Fibronectin type-III 1.
FT   DOMAIN      794    883       Fibronectin type-III 2.
FT   DOMAIN      895    981       Fibronectin type-III 3.
FT   DOMAIN      983   1090       CBM2.
FT   REGION       54    699       Catalytic (By similarity).
FT   ACT_SITE    513    513       Nucleophile (By similarity).
FT   DISULFID    990   1089       By similarity.
SQ   SEQUENCE   1090 AA;  114829 MW;  046BB9D956F2F399 CRC64;
     MSSTTRRRSA WVAAATVGVS SFLAVAGITP AIAAAGAGQP ATVTVPAASP VRAAVDGEYA
     QRFLAQYDKI KDPANGYFSA QGIPYHAVET LMVEAPDYGH ETTSEAYSYW LWLEALYGQV
     TQDWAPLNHA WDTMEKYMIP QSVDQPTNSF YNPNSPATYA PEFNHPSSYP SQLNSGISGG
     TDPIGAELKA TYGNADVYQM HWLADVDNIY GFGATPGAGC TLGPTATGTS FINTFQRGPQ
     ESVWETVPQP SCEEFKYGGK NGYLDLFTKD ASYAKQWKYT SASDADARAV EAVYWANQWA
     TEQGKAADVA ATVAKAAKMG DYLRYTLFDK YFKKIGCTSP TCAAGQGREA AHYLLSWYMA
     WGGATDTSSG WAWRIGSSHA HFGYQNPLAA WALSTDPKLT PKSPTAKADW AASMQRQLEF
     YTWLQASNGG IAGGATNSWD GAYAQPPAGT PTFYGMGYTE APVYVDPPSN RWFGMQAWGV
     QRVAELYYAS GNAQAKKILD KWVPWVVANI STDGASWKVP SELKWTGKPD TWNAAAPTGN
     PGLTVEVTSY GQDVGVAADT ARALLFYAAK SGDTASRDKA KALLDAIWAN NQDPLGVSAV
     ETRGDYKRFD DTYVANGDGI YIPSGWTGTM PNGDVIKPGV SFLDIRSFYK KDPNWSKVQT
     FLDGGAEPQF RYHRFWAQTA VAGALADYAR LFDDGTTTPD TTAPTVPTGL QAGVVTSTEA
     TISWTASTDD TRVTGYDVYR GATKVGTATT TSFTDTGLTA STAYAYTVRA FDAAGNVSAP
     SAALTVTTKA TPSDTTAPSV PAITSSSSTA NSVTIGWSAS TDNAGGSGLA GYDVYRGATR
     VAQTTALTFT DTGLTASTAY EYTVRARDVA GNVSAPSTAV SVTTKSDTTP DTTAPSVPAG
     LAAMTVTETS VALTWNASTD TGGSGLKGYD VYRGATRVGS TTTASYTDTG LTAATAYQYT
     VRATDNAGNV SAASAALSVT TKTPQTGGSC SVAYNASSWN SGFTASVRIT NTGTTTINGW
     SLGFDLTAGQ KVQQGWSATW TQSGSTVTAT NAPWNGTLAP GQTVDVGFNG SHTGQNPNPA
     SFTLNGASCT
//