EXGB_EMENI
ID EXGB_EMENI Reviewed; 409 AA.
AC Q5B6Q3; C8V716; Q1HFT3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=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=AN3777;
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 [MRNA], AND FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
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).
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).
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.
CC {ECO:0000269|PubMed:16844780}.
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; DQ490491; ABF50867.1; -; mRNA.
DR EMBL; AACD01000061; EAA59985.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF75405.1; -; Genomic_DNA.
DR RefSeq; XP_661381.1; XM_656289.1.
DR AlphaFoldDB; Q5B6Q3; -.
DR SMR; Q5B6Q3; -.
DR STRING; 162425.CADANIAP00004938; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PRIDE; Q5B6Q3; -.
DR EnsemblFungi; CBF75405; CBF75405; ANIA_03777.
DR EnsemblFungi; EAA59985; EAA59985; AN3777.2.
DR GeneID; 2873201; -.
DR KEGG; ani:AN3777.2; -.
DR VEuPathDB; FungiDB:AN3777; -.
DR eggNOG; ENOG502RBRB; Eukaryota.
DR HOGENOM; CLU_004624_7_0_1; -.
DR InParanoid; Q5B6Q3; -.
DR OMA; WMLPAEW; -.
DR OrthoDB; 916629at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IDA:AspGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central.
DR GO; GO:0009251; P:glucan catabolic process; IDA:AspGD.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..409
FT /note="Glucan endo-1,6-beta-glucosidase B"
FT /id="PRO_0000394710"
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 409 AA; 46267 MW; 83704098EDC15087 CRC64;
MKFILPLFTS LPVALAWLPG IDKDIYSAAG TNIFNVTSAS SKRWLPASKK IRGVNLGSHF
VIEPWMASMA WSNMGCSGQR SEFDCVMALG QETADQAFAD HWGSWITQDD INQMVQYGLN
TIRIPVGYWL KEDLVYADSE HFPKGGIGYL EDVCGWASDA GMYIIIDLHG APGAQQPKQP
FTGQYAPNPG FYQDYQYDRA LEFLEWMTTS IHQNNKFRNV GMLEIVNEPV QNADQASSMI
NSYYPSAFTR IRNTESSLGI TSNNYLHIQM MNEKWGSGDP TQSLTDNYFA AYDDHRYVKW
DSSVAVDKES YISASCVDDR GGNWPTIVGE WSLSVPDNVE HTADWEPSSN TDFYARWFAA
QAIAYEKQEG WVFWSWKAQL GDYRWSYKDA VDAGVIPKDL DSIYDYSPC
