ID   CBHB_ASPFU              Reviewed;         532 AA.
AC   Q4WM08;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Probable 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=AFUA_6G11610;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   INDUCTION.
RX   PubMed=16984401; DOI=10.1111/j.1574-6968.2006.00462.x;
RA   Bromley M., Gordon C., Rovira-Graells N., Oliver J.;
RT   "The Aspergillus fumigatus cellobiohydrolase B (cbhB) promoter is tightly
RT   regulated and can be exploited for controlled protein expression and
RT   RNAi.";
RL   FEMS Microbiol. Lett. 264:246-254(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}.
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   -!- INDUCTION: Expressed at high levels in the presence of
CC       carboxymethylcellulose and repressed in the presence of glucose.
CC       {ECO:0000269|PubMed:16984401}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; AAHF01000006; EAL89006.1; -; Genomic_DNA.
DR   RefSeq; XP_751044.1; XM_745951.1.
DR   PDB; 4V1Z; X-ray; 1.78 A; A=28-466.
DR   PDB; 4V20; X-ray; 1.50 A; A=28-466.
DR   PDBsum; 4V1Z; -.
DR   PDBsum; 4V20; -.
DR   AlphaFoldDB; Q4WM08; -.
DR   SMR; Q4WM08; -.
DR   STRING; 330879.Q4WM08; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   GlyCosmos; Q4WM08; 1 site, No reported glycans.
DR   EnsemblFungi; EAL89006; EAL89006; AFUA_6G11610.
DR   GeneID; 3508349; -.
DR   KEGG; afm:AFUA_6G11610; -.
DR   VEuPathDB; FungiDB:Afu6g11610; -.
DR   eggNOG; ENOG502QPHV; Eukaryota.
DR   HOGENOM; CLU_020817_3_2_1; -.
DR   InParanoid; Q4WM08; -.
DR   OMA; CGFNGAL; -.
DR   OrthoDB; 3014058at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..532
FT                   /note="Probable 1,4-beta-D-glucan cellobiohydrolase B"
FT                   /id="PRO_0000393548"
FT   DOMAIN          496..532
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          27..461
FT                   /note="Catalytic"
FT   REGION          462..496
FT                   /note="Thr-rich linker"
FT   REGION          462..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        238
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        243
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        504..521
FT                   /evidence="ECO:0000250"
FT   DISULFID        515..531
FT                   /evidence="ECO:0000250"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           104..108
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          116..130
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          132..139
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          151..158
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          166..173
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   TURN            177..183
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           190..193
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          231..235
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          238..244
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          249..254
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          262..265
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           266..269
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          279..282
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   TURN            291..295
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          299..301
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          304..307
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          312..320
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          329..338
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          341..344
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          356..358
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           360..370
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           375..378
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           381..391
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          393..401
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   TURN            403..407
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           408..411
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          412..415
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   TURN            423..425
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   HELIX           437..443
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   STRAND          448..458
FT                   /evidence="ECO:0007829|PDB:4V20"
FT   TURN            459..464
FT                   /evidence="ECO:0007829|PDB:4V20"
SQ   SEQUENCE   532 AA;  56457 MW;  03EBC7D15A5EAE78 CRC64;
     MLASTFSYRM YKTALILAAL LGSGQAQQVG TSQAEVHPSM TWQSCTAGGS CTTNNGKVVI
     DANWRWVHKV GDYTNCYTGN TWDTTICPDD ATCASNCALE GANYESTYGV TASGNSLRLN
     FVTTSQQKNI GSRLYMMKDD STYEMFKLLN QEFTFDVDVS NLPCGLNGAL YFVAMDADGG
     MSKYPTNKAG AKYGTGYCDS QCPRDLKFIN GQANVEGWQP SSNDANAGTG NHGSCCAEMD
     IWEANSISTA FTPHPCDTPG QVMCTGDACG GTYSSDRYGG TCDPDGCDFN SFRQGNKTFY
     GPGMTVDTKS KFTVVTQFIT DDGTSSGTLK EIKRFYVQNG KVIPNSESTW TGVSGNSITT
     EYCTAQKSLF QDQNVFEKHG GLEGMGAALA QGMVLVMSLW DDHSANMLWL DSNYPTTASS
     TTPGVARGTC DISSGVPADV EANHPDAYVV YSNIKVGPIG STFNSGGSNP GGGTTTTTTT
     QPTTTTTTAG NPGGTGVAQH YGQCGGIGWT GPTTCASPYT CQKLNDYYSQ CL
//