EGLX_ASPNC
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 25-MAY-2022, entry version 67.
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 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=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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 PaxDb; A2QBQ3; -.
DR EnsemblFungi; CAK96300; CAK96300; An02g00850.
DR GeneID; 4978566; -.
DR KEGG; ang:ANI_1_2196024; -.
DR VEuPathDB; FungiDB:An02g00850; -.
DR HOGENOM; CLU_016972_4_0_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF49899; SSF49899; 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
