BTGC_ASPNC
ID BTGC_ASPNC Reviewed; 684 AA.
AC A2QN74;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Putative glucan endo-1,3-beta-glucosidase btgC;
DE EC=3.2.1.39;
DE AltName: Full=Endo-1,3-beta-glucanase btgC;
DE AltName: Full=Laminarinase btgC;
GN Name=btgC; ORFNames=An07g04650;
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: Glucanases play a role in cell expansion during growth, in
CC cell-cell fusion during mating, and in spore release during
CC sporulation. This enzyme may be involved in beta-glucan degradation.
CC Active on laminarin and lichenan (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Glu residue in position 619 essential for
CC glucanase activity. Its enzyme activity is therefore unsure.
CC {ECO:0000305}.
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DR EMBL; AM270130; CAK39383.1; -; Genomic_DNA.
DR RefSeq; XP_001391547.2; XM_001391510.2.
DR AlphaFoldDB; A2QN74; -.
DR SMR; A2QN74; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; A2QN74; -.
DR EnsemblFungi; CAK39383; CAK39383; An07g04650.
DR GeneID; 4981731; -.
DR KEGG; ang:ANI_1_1742064; -.
DR Proteomes; UP000006706; Chromosome 4L.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Cell wall biogenesis/degradation;
KW Glycoprotein; Hydrolase; Membrane; Polysaccharide degradation;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..684
FT /note="Putative glucan endo-1,3-beta-glucosidase btgC"
FT /id="PRO_0000395125"
FT TOPO_DOM 1..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..684
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 487
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 586
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 684 AA; 73248 MW; 5CB65C56222424D0 CRC64;
MAGVNRSFSY SRGDDALLRD DEREISPLRS AEDGLYSTSY GDVSPLSAGV QAQNRPFDRG
LVSVPEGQTL ERHMTSTPGM DNLGPASVGG GISGIALGVA NSHNRQSGVD AFRETDVPVR
NLPAERDFNT TGSDNPYIPA PPDGDIYPSS EAVRYRDSYS SHTGLGAGAP FAEHSTPGTT
PSQRSFFDSP YQGVDAGPYQ RHSAYSSHDY PLVINPDDIA DDGDDGFPVH PKGAADYRSN
ANVPGTGVAG AAAAGGFLGK FRALFKREEP SPFYDSDIGG GLGGAEKAQG GRHIIGGGSR
KRGWIVGLIL AAVIVAAIVG GAVGGILGHQ EHDGDTSSSS SSSSSSGTGS GGSDKGDGLL
DKDSDEIKAL MNNKNLHKVF PGVDYTPWGV QYPLCLQYPP SQNNVTRDLA VLTQLTNTIR
LYGTDCNQTE MVLEAIDRLQ LTNMKLWLGV WIDTNTTTTD RQISQLYKIV ENANDTSIFK
GAIVGNEALY RAGSDVASAE TNLIGYINDV KDHFKDKNID LPVGTSDLGD NWNAQLVSAA
DFVMSNIHPF FGGVEIDDAA SWTWTFWQTH DTPLTAGTNK QQIISEVGWP TGGGNDCGSD
NKCQNDKQGA VAGIDELNQF LSEWVCQALD NGTEYFWFEA FDEPWKVQYN TPGQEWEDKW
GLMDSARNLK PGVKIPDCGG KTIT
