NEG1_NEUCR
ID NEG1_NEUCR Reviewed; 480 AA.
AC Q7M4T0; Q7RZ78; Q8NKJ2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Endo-1,6-beta-D-glucanase;
DE EC=3.2.1.75;
DE AltName: Full=Beta-1,6-glucanase Neg1;
DE AltName: Full=Glucan endo-1,6-beta-glucosidase;
DE Flags: Precursor;
GN Name=neg-1; ORFNames=29E8.200, NCU04395;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-35; 243-257; 323-330 AND
RP 426-435, AND CHARACTERIZATION.
RC STRAIN=ATCC 10336 / CBS 304.59 / FGSC 1757 / NBRC 6068 / IMI 53238;
RX PubMed=12162562; DOI=10.1271/bbb.66.1378;
RA Oyama S., Yamagata Y., Abe K., Nakajima T.;
RT "Cloning and expression of an endo-1,6-beta-D-glucanase gene (neg1) from
RT Neurospora crassa.";
RL Biosci. Biotechnol. Biochem. 66:1378-1381(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Partially degrades N.crassa cell wall beta-D-glucan,
CC liberating small amounts of oligosaccharides.
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.
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DR EMBL; AB073820; BAB91213.1; -; mRNA.
DR EMBL; BX908809; CAF06053.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA28236.1; -; Genomic_DNA.
DR PIR; JC7866; JC7866.
DR RefSeq; XP_957472.1; XM_952379.2.
DR AlphaFoldDB; Q7M4T0; -.
DR SMR; Q7M4T0; -.
DR STRING; 5141.EFNCRP00000005200; -.
DR CAZy; GH30; Glycoside Hydrolase Family 30.
DR EnsemblFungi; EAA28236; EAA28236; NCU04395.
DR GeneID; 3873626; -.
DR KEGG; ncr:NCU04395; -.
DR VEuPathDB; FungiDB:NCU04395; -.
DR HOGENOM; CLU_014379_3_1_1; -.
DR InParanoid; Q7M4T0; -.
DR OMA; FGGIAWH; -.
DR BRENDA; 3.2.1.75; 3627.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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: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; 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 PRINTS; PR00843; GLHYDRLASE30.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:12162562"
FT CHAIN 18..480
FT /note="Endo-1,6-beta-D-glucanase"
FT /id="PRO_0000012180"
FT ACT_SITE 225
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 101
FT /note="T -> P (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="G -> D (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="G -> D (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> V (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="T -> K (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="S -> A (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="S -> T (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="K -> R (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="T -> M (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="A -> T (in Ref. 1; BAB91213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 51353 MW; 9183B780A3B491F8 CRC64;
MYPPALTLLL TPGLVAAAIQ PQAYASSADG RYKLSSYSAP VRGTGTPGSN STWKLTIDDT
PSGRKQTIKG FGAAVTDSTV SVFNALPSAQ RTALLNTLMT TAGANFAMMR HTIASSDLSA
NPAYSYDDSN GQTDLSLSNF NLGGRGNAMA SLLAEMRRLQ PGLTILGSPW SPPGWMKLNR
AIQGTTVNNN LDHAYASQFA QYFVKYLQAY QAKGATIDAI TIQNEPLNSR AQMPTMYIYA
DEAGDLIQNN IGPALRNAGL DTKIWAYDHN TDQPSYPSTV LSRAGGYVPA VAWHCYASSL
DWSVLTTFHN AHPGVEQYMT ECWTSAKQPT PWNWAASFTM GPLQNWASGV TAWVLGTDTN
DGPHLTGSDA CDKCTGLVTV DAAAGTYNLR GDYYMMAQFS KFMKKGAVVM SGTGSWTYGD
GSGLESVAAT NADDGSRVVV IENKFGNEIY VTVEAKSGEV WSGLVYRNSV VTWVLPAAGA
