CBHA_ASPFU
ID CBHA_ASPFU Reviewed; 452 AA.
AC Q4WNA2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Probable 1,4-beta-D-glucan cellobiohydrolase A;
DE EC=3.2.1.91;
DE AltName: Full=Beta-glucancellobiohydrolase A;
DE AltName: Full=Cellobiohydrolase D;
DE AltName: Full=Exocellobiohydrolase A;
DE AltName: Full=Exoglucanase A;
DE Flags: Precursor;
GN Name=cbhA; Synonyms=celD; ORFNames=AFUA_6G07070;
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).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL88562.1; -; Genomic_DNA.
DR RefSeq; XP_750600.1; XM_745507.1.
DR AlphaFoldDB; Q4WNA2; -.
DR SMR; Q4WNA2; -.
DR STRING; 746128.CADAFUBP00007108; -.
DR EnsemblFungi; EAL88562; EAL88562; AFUA_6G07070.
DR GeneID; 3508755; -.
DR KEGG; afm:AFUA_6G07070; -.
DR VEuPathDB; FungiDB:Afu6g07070; -.
DR eggNOG; ENOG502QPHV; Eukaryota.
DR HOGENOM; CLU_020817_3_2_1; -.
DR InParanoid; Q4WNA2; -.
DR OMA; ALTWSKC; -.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
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; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..452
FT /note="Probable 1,4-beta-D-glucan cellobiohydrolase A"
FT /id="PRO_0000393541"
FT REGION 405..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 452 AA; 48135 MW; B62A9D4115A45295 CRC64;
MHQRALLFSA LAVAANAQQV GTQTPETHPP LTWQKCTAAG SCSQQSGSVV IDANWRWLHS
TKDTTNCYTG NTWNTELCPD NESCAQNCAL DGADYAGTYG VTTSGSELKL SFVTGANVGS
RLYLMQDDET YQHFNLLNHE FTFDVDVSNL PCGLNGALYF VAMDADGGMS KYPSNKAGAK
YGTGYCDSQC PRDLKFINGM ANVEGWEPSS SDKNAGVGGH GSCCPEMDIW EANSISTAVT
PHPCDDVSQT MCSGDACGGT YSESRYAGTC DPDGCDFNPF RMGNESFYGP GKIVDTKSKM
TVVTQFITAD GTDSGALSEI KRLYVQNGKV IANSVSNVAG VSGNSITSDF CTAQKKAFGD
EDIFAKHGGL SGMGKALSEM VLIMSIWDDH HSSMMWLDST YPTDADPSKP GVARGTCEHG
AGDPENVESQ HPDASVTFSN IKFGPIGSTY EG
