ID   GUXA_CELFI     STANDARD;      PRT;   872 AA.
AC   P50401;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   21-MAR-2006, entry version 49.
DE   Exoglucanase A precursor (EC 3.2.1.91) (Exocellobiohydrolase A)
DE   (1,4-beta-cellobiohydrolase A) (CBP95).
GN   Name=cbhA;
OS   Cellulomonas fimi.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 484;
RX   MEDLINE=94344030; PubMed=8065260;
RA   Meinke A., Gilkes N.R., Kwan E., Kilburn D.G., Warren R.A.J.,
RA   Miller R.C. Jr.;
RT   "Cellobiohydrolase A (CbhA) from the cellulolytic bacterium
RT   Cellulomonas fimi is a beta-1,4-exocellobiohydrolase analogous to
RT   Trichoderma reesei CBH II.";
RL   Mol. Microbiol. 12:413-422(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 41-58.
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   -!- FUNCTION: This enzyme hydrolyzes 1,4-beta-D-glucosidic linkages of
CC       cellulose. Weak activity against carboxymethylcellulose, bacterial
CC       microcrystalline cellulose and barley beta-glucan. Has also weak
CC       endoglucanase activity. Hydrolyzes glucosidic bonds with inversion
CC       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 6 (cellulase B)
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; L25809; AAC36898.1; -; Unassigned_DNA.
DR   PIR; S49541; S49541.
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; IPR001524; Glyco_hydro_6.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   ProDom; PD003733; Glyco_hydro_6; 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.
DR   PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
KW   Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL        1     40
FT   CHAIN        41    872       Exoglucanase A.
FT                                /FTId=PRO_0000007904.
FT   DOMAIN      482    566       Fibronectin type-III 1.
FT   DOMAIN      577    664       Fibronectin type-III 2.
FT   DOMAIN      675    762       Fibronectin type-III 3.
FT   DOMAIN      763    872       CBM2.
FT   REGION       41    477       Catalytic.
FT   ACT_SITE    188    188       Proton donor (By similarity).
FT   ACT_SITE    410    410       Nucleophile (By similarity).
FT   DISULFID    140    202       By similarity.
FT   DISULFID    374    428       By similarity.
FT   DISULFID    770    869       By similarity.
SQ   SEQUENCE   872 AA;  89301 MW;  7883B407F995533B CRC64;
     MSTLGKRAGV RRRVRAVATA ATATALVAVP LTTLATSASA APVHVDNPYA GAVQYVNPTW
     AASVNAAAGR QSADPALAAK MRTVAGQPTA VWMDRISAIT GNADGNGLKF HLDNAVAQQK
     AAGVPLVFNL VIYDLPGRDC FALASNGELP ATDAGLARYK SEYIDPIADL LDNPEYESIR
     IAATIEPDSL PNLTTNISEP ACQQAAPYYR QGVKYALDKL HAIPNVYNYI DIGHSGWLGW
     DSNAGPSATL FAEVAKSTTA GFASIDGFVS DVANTTPLEE PLLSDSSLTI NNTPIRSSKF
     YEWNFDFDEI DYTAHMHRLL VAAGFPSSIG MLVDTSRNGW GGPNRPTSIT ASTDVNAYVD
     ANRVDRRVHR GAWCNPLGAG IGRFPEATPS GYAASHLDAF VWIKPPGESD GASTDIPNDQ
     GKRFDRMCDP TFVSPKLNNQ LTGATPNAPL AGQWFEEQFV TLVKNAYPVI GGTTPVEDLV
     APTVPTGLTA GTTTATSVPL SWTASTDNVA VTGYDVYRGT TLVGTTAATS YTVTGLTPAT
     AYSFTVRAKD AAGNVSAASA AAAATTQSGT VTDTTAPSVP AGLTAGTTTT TTVPLSWTAS
     TDNAGGSGVA GYEVLRGTTV VGTTTATSYT VTGLTAGTTY SFSVRAKDVA GNTSAASAAV
     SATTQTGTVV DTTAPSVPTG LTAGTTTTSS VPLTWTASTD NAGGSGVAGY EVFNGTTRVA
     TVTSTSYTVT GLAADTAYSF TVKAKDVAGN VSAASAAVSA RTQAATSGGC TVKYSASSWN
     TGFTGTVEVK NNGTAALNGW TLGFSFADGQ KVSQGWSAEW SQSGTAVTAK NAPWNGTLAA
     GSSVSIGFNG THNGTNTAPT AFTLNGVACT LG
//