ID   EGLX_ASPNC              Reviewed;         739 AA.
AC   A2QBQ3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Probable endo-1,3(4)-beta-glucanase An02g00850;
DE            EC=3.2.1.6;
DE   AltName: Full=Mixed-linked glucanase An02g00850;
DE   Flags: Precursor;
GN   ORFNames=An02g00850;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Mixed-linked glucanase involved in the degradation of complex
CC       natural cellulosic substrates. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans
CC         when the glucose residue whose reducing group is involved in the
CC         linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; AM269996; CAK96300.1; -; Genomic_DNA.
DR   RefSeq; XP_001399223.1; XM_001399186.1.
DR   AlphaFoldDB; A2QBQ3; -.
DR   SMR; A2QBQ3; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   EnsemblFungi; CAK96300; CAK96300; An02g00850.
DR   GeneID; 4978566; -.
DR   KEGG; ang:An02g00850; -.
DR   VEuPathDB; FungiDB:An02g00850; -.
DR   HOGENOM; CLU_016972_4_0_1; -.
DR   OrthoDB; 1932445at2759; -.
DR   Proteomes; UP000006706; Chromosome 4R.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR   GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02181; GH16_fungal_Lam16A_glucanase; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   PANTHER; PTHR10963:SF58; ENDO-1,3(4)-BETA-GLUCANASE XGEA; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Cellulose degradation;
KW   Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..717
FT                   /note="Probable endo-1,3(4)-beta-glucanase An02g00850"
FT                   /id="PRO_5000219530"
FT   PROPEP          718..739
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395090"
FT   DOMAIN          31..283
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          431..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        145
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   LIPID           717
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        526
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        537
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        581
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   739 AA;  72556 MW;  7640750996F31B92 CRC64;
     MPTSTLLWSV GSLALSSMVL PAAASSYELV ETWKGEDFLT AFDFYTGADP TNGFVTYANQ
     SYAESTGLVK VNSNGTFYMG VDHTTKLSTN GPGRESVRIG SNKYYDEGLF IIDLQHMPGS
     VCGTWPAFWS TGKNWPTDGE IDIIEGVNKN EANEIVLHTS GTCQVSSQKM SGTLTSTECG
     EDAGTTGCVV EGTQGSSGTP FNENGGGVYA MQWTDEFLKF WFFPRGSIPS SITKGDPDVA
     AFGTPMAHME GSCSIAEHFK AQQFIFDTTF CGDWAGGVYS TSGCPVSDSS SSFKSCVAYV
     AENPTAFAES YWEINYIKIY QTGVAASASA SASHVESAAS VAETISAVRE GTNSVVATTT
     AATIAVTSTA DAETATTMAG ATTVAASTET SAADENGSSA STSTHYVTMT TTICPIAESS
     SAAAALAGGS SEATEASNSE GSPAAATPSS VTGASAEANE SESTSAAVTT PSTSTGASAE
     ANGSESSSAS EAGSVAGATP SSVSTTGASG EADSSEGASA AATPSNVSST GASAEANGSE
     DSSASSEAKT VAPSIPSSVT GASAEANGND SASSNAATAS NVSGASAQAG DNESTPASAG
     ANAGSSAAPS SVSGASAEAN GSEGSSSHSS GSQAGAHSYG SVPSSAAAYG RPAPSSSSHA
     FATAPSSTGS SRVPTSAAAA NNAAAATQGS SASGSNSGSS GHGSSSATTP STPVFTGGAN
     KLTLGASSVL SVLAFALLA
//