CBHB_ASPFU
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 25-MAY-2022, entry version 103.
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 Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
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 / Af293 / CBS 101355 / FGSC A1100;
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; 746128.CADAFUBP00007567; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
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; VYSNIKV; -.
DR OrthoDB; 875234at2759; -.
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; -; 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; PTHR33753; 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; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 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
