EXGB_ASPOR
ID EXGB_ASPOR Reviewed; 406 AA.
AC Q2TZQ9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Probable glucan endo-1,6-beta-glucosidase B;
DE EC=3.2.1.75;
DE AltName: Full=Beta-1,6-glucanase B;
DE AltName: Full=Endo-1,6-beta-D-glucanase B;
DE AltName: Full=Endo-1,6-beta-glucanase B;
DE Flags: Precursor;
GN Name=exgB; ORFNames=AO090011000757;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC the main structural component of the cell wall. Acts on lutean,
CC pustulan and 1,6-oligo-beta-D-glucosides (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC glucans.; EC=3.2.1.75;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007171; BAE65206.1; -; Genomic_DNA.
DR RefSeq; XP_001826339.1; XM_001826287.2.
DR AlphaFoldDB; Q2TZQ9; -.
DR SMR; Q2TZQ9; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblFungi; BAE65206; BAE65206; AO090011000757.
DR GeneID; 5998442; -.
DR KEGG; aor:AO090011000757; -.
DR VEuPathDB; FungiDB:AO090011000757; -.
DR HOGENOM; CLU_004624_7_0_1; -.
DR OMA; WMLPAEW; -.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..406
FT /note="Probable glucan endo-1,6-beta-glucosidase B"
FT /id="PRO_0000394708"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 322
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 406 AA; 46614 MW; 9A8781C383B12BA6 CRC64;
MKVTRLAVLN TLATLTVAWL PTTDKTITSS NGTDLFKASH GKIRGVNLGS QFVFEPWIAT
KAWSELGCEG QESEFDCVMK LGQDAANKAF AKHWDSWITK EDIKEIRSYG LNTIRIPVGY
WMNEDLIYHD SEYFPHGGFA YLEKLCGWAS DAGLYIIIDL HGAPGAQVAK NAFTGQFADT
PGFYVDFQYQ RALEFLEWMT IKVHTLHNFR NVGMLEVVNE PVQNPQVTTT LRSNYYPNAF
HSIRKVEGAL SIDRKDYLHI QMMDGAWGAG DPHEHLTDDY YAAYDNHRYL KWDPRVEVSK
DSYIKTSCND NVATNWPAII GEWSLGVPDN VQETADWKPY SNLDFYQKWF AAQVQNYEQH
QGWIFWTWKT QLDEYRWSYR DGVKAGVIPT DLNAVFREDV CKGRSS