GUXB_CELFA
ID GUXB_CELFA Reviewed; 1090 AA.
AC P50899; F4H1U3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Exoglucanase B;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase B;
DE AltName: Full=CBP120;
DE AltName: Full=Exocellobiohydrolase B;
DE Flags: Precursor;
GN Name=cbhB; Synonyms=cenE; OrderedLocusNames=Celf_3400;
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas.
OX NCBI_TaxID=590998;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 456-461.
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
RX PubMed=7575482; DOI=10.1042/bj3110067;
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 cellulolytic
RT bacterium Cellulomonas fimi.";
RL Biochem. J. 311:67-74(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 54-75.
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
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).
RN [4]
RP PROTEIN SEQUENCE OF 54-78.
RX PubMed=8147863; DOI=10.1006/bbrc.1994.1361;
RA Shen H., Tomme P., Meinke A., Gilkes N.R., Kilburn D.G., Warren R.A.J.,
RA Miller R.C. Jr.;
RT "Stereochemical course of hydrolysis catalysed by Cellulomonas fimi CenE, a
RT 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 hydrolyzed
CC cellopentaose to cellotriose and cellobiose, and cellotetraose to
CC cellobiose, but it did not hydrolyze cellotriose. Has also weak
CC endoglucanase activity. Hydrolyzes glucosidic bonds with inversion of
CC anomeric configuration.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 48 (cellulase L) family.
CC {ECO:0000305}.
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DR EMBL; L38827; AAB00822.1; -; Genomic_DNA.
DR EMBL; CP002666; AEE47513.1; -; Genomic_DNA.
DR PIR; S59077; S59077.
DR RefSeq; WP_013772537.1; NC_015514.1.
DR AlphaFoldDB; P50899; -.
DR SMR; P50899; -.
DR STRING; 590998.Celf_3400; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH48; Glycoside Hydrolase Family 48.
DR EnsemblBacteria; AEE47513; AEE47513; Celf_3400.
DR KEGG; cfi:Celf_3400; -.
DR eggNOG; COG4733; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_009014_0_0_11; -.
DR OMA; WLWLEAL; -.
DR OrthoDB; 191946at2; -.
DR Proteomes; UP000008460; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.170.160.10; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 4.10.870.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR InterPro; IPR027390; Endoglucanase_F_dom3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR000556; Glyco_hydro_48F.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF02011; Glyco_hydro_48; 1.
DR PRINTS; PR00844; GLHYDRLASE48.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 3.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49384; SSF49384; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS50853; FN3; 3.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..53
FT /evidence="ECO:0000269|PubMed:8147863,
FT ECO:0000269|PubMed:8458833"
FT /id="PRO_0000008028"
FT CHAIN 54..1090
FT /note="Exoglucanase B"
FT /id="PRO_0000008029"
FT DOMAIN 706..791
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 797..887
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 897..984
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 983..1090
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 54..699
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 1069..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 513
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 990..1089
FT /evidence="ECO:0000250"
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
