NEG1_ASPFU
ID NEG1_ASPFU Reviewed; 488 AA.
AC Q4WBR2;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Endo-1,6-beta-D-glucanase neg1;
DE EC=3.2.1.75 {ECO:0000269|PubMed:19039584};
DE AltName: Full=Beta-1,6-glucanase neg1;
DE AltName: Full=Glucan endo-1,6-beta-glucosidase neg1;
DE Flags: Precursor;
GN Name=neg1 {ECO:0000303|PubMed:19039584}; ORFNames=AFUA_8G07120;
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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19039584; DOI=10.1007/s00253-008-1780-z;
RA Boisrame A., Gaillardin C.;
RT "Heterologous expression and characterization of a beta-1,6-glucanase from
RT Aspergillus fumigatus.";
RL Appl. Microbiol. Biotechnol. 82:663-669(2009).
CC -!- FUNCTION: Endoglucanase that has highest activity on the linear beta-
CC 1,6-glucan pustulan and lower activity against laminarin (beta-1,3-
CC glucans with beta-1,6-branches). Is active on C.albicans cell walls
CC allowing the release of a previously described cell wall proteins.
CC {ECO:0000269|PubMed:19039584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC glucans.; EC=3.2.1.75; Evidence={ECO:0000269|PubMed:19039584};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:19039584};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.
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DR EMBL; AAHF01000013; EAL85472.1; -; Genomic_DNA.
DR RefSeq; XP_747510.1; XM_742417.1.
DR AlphaFoldDB; Q4WBR2; -.
DR SMR; Q4WBR2; -.
DR STRING; 746128.CADAFUBP00007857; -.
DR CLAE; BGN30A_ASPFU; -.
DR EnsemblFungi; EAL85472; EAL85472; AFUA_8G07120.
DR GeneID; 3504964; -.
DR KEGG; afm:AFUA_8G07120; -.
DR VEuPathDB; FungiDB:Afu8g07120; -.
DR eggNOG; KOG2566; Eukaryota.
DR HOGENOM; CLU_014379_3_1_1; -.
DR InParanoid; Q4WBR2; -.
DR OMA; FGGIAWH; -.
DR OrthoDB; 644299at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IDA:AspGD.
DR GO; GO:0004348; F:glucosylceramidase activity; IBA:GO_Central.
DR GO; GO:0006680; P:glucosylceramide catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; PTHR11069; 1.
DR Pfam; PF02055; Glyco_hydro_30; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..488
FT /note="Endo-1,6-beta-D-glucanase neg1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432744"
FT ACT_SITE 241
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04062"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04062"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 488 AA; 51430 MW; 9529EA5DF0E2418C CRC64;
MRISVGALLG LTALSHATTE KRAASASAYC SNSAGNYKLS SIAAPVQGAG NPGSESTWQL
TVDDTSSGHK QTIVGFGAAV TDATVTSFNT LSASVLQDLL NKLMTPAGAN FALMRHTIGA
SDLSGDPAYT YDDNGGKADP SLSGFNLGDR GTAMAKMLAT MKSLQPNLKI LGSPWSAPGW
MKLNGVLDGN TNNNNLNDGY LTSGGTGSTG YASQFAQYFV KYIQAYKNLG AHVDAITIQN
EPLFSSAGYP TMYVYDYESA QLIQNYIGPA LASAGLDTEI WAYDHNTDVP SYPQTVLNQA
GQYVKSVAWH CYAPNVDWTV LSQFHNTNPG VKQYMTECWT PASGAWHQAA DFTMGPLQNW
ASGVAAWTLG TNAQDGPHLS TGGCATCQGL VTINNGGYTL NTAYYMMAQF SKFMPPGAIV
LNGSGSYTYS GGGGIQSVAS LNPDGTRTVV IENTFGNDVY VTVTMKSGQK WSGNAPSQSV
TTWVLPSA
