ID   CBHB_EMENI              Reviewed;         526 AA.
AC   Q8NK02; C8VSY4; Q5BG36;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=1,4-beta-D-glucan cellobiohydrolase B;
DE            EC=3.2.1.91;
DE   AltName: Full=Beta-glucancellobiohydrolase B;
DE   AltName: Full=Exocellobiohydrolase B;
DE   AltName: Full=Exoglucanase B;
DE   Flags: Precursor;
GN   Name=cbhB; ORFNames=AN0494;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12409103; DOI=10.1016/s1087-1845(02)00504-2;
RA   Lockington R.A., Rodbourn L., Barnett S., Carter C.J., Kelly J.M.;
RT   "Regulation by carbon and nitrogen sources of a family of cellulases in
RT   Aspergillus nidulans.";
RL   Fungal Genet. Biol. 37:190-196(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4]
RP   FUNCTION.
RX   PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA   Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT   "Development and application of a suite of polysaccharide-degrading enzymes
RT   for analyzing plant cell walls.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
CC   -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC       requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC       cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC       cut the disaccharide cellobiose from the non-reducing end of the
CC       cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC       cellobiose and other short cello-oligosaccharides to glucose.
CC       {ECO:0000250, ECO:0000269|PubMed:16844780}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; AF420020; AAM54070.1; -; Genomic_DNA.
DR   EMBL; AACD01000007; EAA66593.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF89371.1; -; Genomic_DNA.
DR   RefSeq; XP_658098.1; XM_653006.1.
DR   AlphaFoldDB; Q8NK02; -.
DR   SMR; Q8NK02; -.
DR   STRING; 227321.Q8NK02; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   CLAE; CBH7B_EMENI; -.
DR   GlyCosmos; Q8NK02; 2 sites, No reported glycans.
DR   EnsemblFungi; CBF89371; CBF89371; ANIA_00494.
DR   GeneID; 2876273; -.
DR   KEGG; ani:AN0494.2; -.
DR   eggNOG; ENOG502QPHV; Eukaryota.
DR   HOGENOM; CLU_020817_3_2_1; -.
DR   InParanoid; Q8NK02; -.
DR   OMA; CGFNGAL; -.
DR   OrthoDB; 3014058at2759; -.
DR   BRENDA; 3.2.1.91; 517.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IDA:UniProtKB.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF2; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..526
FT                   /note="1,4-beta-D-glucan cellobiohydrolase B"
FT                   /id="PRO_0000393550"
FT   DOMAIN          490..526
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          24..458
FT                   /note="Catalytic"
FT   REGION          459..490
FT                   /note="Ser/Thr-rich linker"
FT   REGION          464..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        235
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        240
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        498..515
FT                   /evidence="ECO:0000250"
FT   DISULFID        509..525
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  56123 MW;  9A9CD7C5BEBCB6C9 CRC64;
     MASSFQLYKA LLFFSSLLSA VQAQKVGTQQ AEVHPGLTWQ TCTSSGSCTT VNGEVTIDAN
     WRWLHTVNGY TNCYTGNEWD TSICTSNEVC AEQCAVDGAN YASTYGITTS GSSLRLNFVT
     QSQQKNIGSR VYLMDDEDTY TMFYLLNKEF TFDVDVSELP CGLNGAVYFV SMDADGGKSR
     YATNEAGAKY GTGYCDSQCP RDLKFINGVA NVEGWESSDT NPNGGVGNHG SCCAEMDIWE
     ANSISTAFTP HPCDTPGQTL CTGDSCGGTY SNDRYGGTCD PDGCDFNSYR QGNKTFYGPG
     LTVDTNSPVT VVTQFLTDDN TDTGTLSEIK RFYVQNGVVI PNSESTYPAN PGNSITTEFC
     ESQKELFGDV DVFSAHGGMA GMGAALEQGM VLVLSLWDDN YSNMLWLDSN YPTDADPTQP
     GIARGTCPTD SGVPSEVEAQ YPNAYVVYSN IKFGPIGSTF GNGGGSGPTT TVTTSTATST
     TSSATSTATG QAQHWEQCGG NGWTGPTVCA SPWACTVVNS WYSQCL
//