BTGC_ASPOR
ID BTGC_ASPOR Reviewed; 685 AA.
AC Q2U492;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Probable 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=AO090020000436;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
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DR EMBL; AP007167; BAE63623.1; -; Genomic_DNA.
DR RefSeq; XP_001824756.1; XM_001824704.2.
DR AlphaFoldDB; Q2U492; -.
DR SMR; Q2U492; -.
DR STRING; 510516.Q2U492; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR EnsemblFungi; BAE63623; BAE63623; AO090020000436.
DR GeneID; 5997083; -.
DR KEGG; aor:AO090020000436; -.
DR HOGENOM; CLU_011476_0_1_1; -.
DR Proteomes; UP000006564; Chromosome 6.
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..685
FT /note="Probable glucan endo-1,3-beta-glucosidase btgC"
FT /id="PRO_0000395126"
FT TOPO_DOM 1..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 587
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 685 AA; 72800 MW; CBCDFB8987DF725B CRC64;
MSGPHRSFSF NQGDDGAGDA GDVSPIRSQE GHFMNSPPRH NDVSPVSARS QAMGSSPSSG
FLSAHEHGDR GWGQNSGHTQ AMRTNSTTPG MDNLGPAAVG GGISGIALGV ANSHNRQSGI
DAFRDTDGRN LPAERGYNTT GSDNPYVPTP PGGGSHGSAE NLRPRDSYGS NVALGAAAAP
AGQLTPGGSN PSQRSLFDSP YQGVGAMDAG PYQRQSAYSA AGDYPLVINP DEIADDGDDG
FTPVPNGKSA SSNARAIPAA AAGGAAGGGL FGLFKSKKAD NPSYGPVPGA GLEAGEKSRW
VKPTPGGGSR KRGWIVGLAL AFIVVGAIVG GAVGGTLGNR ENEAPDTTKS ASSDTESNGD
LNKDSSEIKD LMNNPDLHKV FPGMDYTPWG VQYPLCLKYP PSQNNVTRDV AVLSQLTNTV
RLYGTDCNQT EMVLHAIDRL ELKDMKVWLG VWIDSNDTTN DRQIKQLYKV LDDTKDISIF
KGAIVGNEAL YRAGNDIASA KKKLISYMDD VRNHFKEKNY DLPIATSDLG DNWKEDLVTA
TDLVMSNVHP FFAGVTAKEA AGWTWNFWNQ NDVPLTKGTN KKQVISEVGW PSGGGNDCGS
NNKCTDDTSG SVAGIDEMNQ FMSDWICQAL ENGTDYFWFE AFDEPWKVQY NTKDENWEDK
WGLMDAARKL KPGLKIPDCG GKTAA
