EGLX_ASPOR
ID EGLX_ASPOR Reviewed; 667 AA.
AC Q2UIE6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Probable endo-1,3(4)-beta-glucanase AO090023000083;
DE EC=3.2.1.6;
DE AltName: Full=Mixed-linked glucanase AO090023000083;
DE Flags: Precursor;
GN ORFNames=AO090023000083;
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: 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; AP007157; BAE58669.1; -; Genomic_DNA.
DR RefSeq; XP_001820671.1; XM_001820619.1.
DR AlphaFoldDB; Q2UIE6; -.
DR SMR; Q2UIE6; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblFungi; BAE58669; BAE58669; AO090023000083.
DR GeneID; 5992673; -.
DR KEGG; aor:AO090023000083; -.
DR VEuPathDB; FungiDB:AO090023000083; -.
DR HOGENOM; CLU_016972_4_0_1; -.
DR OMA; ILNINFC; -.
DR Proteomes; UP000006564; Chromosome 3.
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..643
FT /note="Probable endo-1,3(4)-beta-glucanase AO090023000083"
FT /id="PRO_0000395091"
FT PROPEP 644..667
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395092"
FT DOMAIN 25..288
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 361..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 643
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 667 AA; 68301 MW; A37D2DC90AF23769 CRC64;
MSSSSFVWTV GSIALSSLIT PTIADGSGSR YQLTEAWQGE KFLDHFKFFS GSDPTNGFVT
YANQSYAESS GLIEVTESGS FYMGVDYKTK LSPNGPGRDS VRIESKEYYD EGLYIIDLQH
MPGSVCGTWP AFWSVGPNWP YDGEIDIIEG VNKHEANEIV LHTSGSCSLS SENDMSGTMT
SSECGESSGT IGCVVKGQDG TSGAPFNEKN GGVYAMEWTS SFVKIWYFAR SEIPQSITEG
NPDTTAFGTP MAHLQGTCDF GERFKSQKFI LDTTFCGDWA GGVFGDSGCP VSDPSNPIQS
CVNYVAENPA AFKEAYWEIN YIKLFQTGTG HSTASVASQA ETATAVASNT VDSIPSVTST
AIPETTAPAP ETVSAEAPAT SSAVPEPANP QTSVAGAETT AAPAPSPETT AAPASPSLDD
SDGADAVSET TIYVTETTTI CGASTQKGTI QTIGGGETEV SPASSTVESA ATPAAPTPTS
QKPVASLPGT TVNGGTPVPT DVSPETPAEE TAGESGAPTP SAEQPEQPQP AATSIETGTV
PPAVSNPAPT EQGTPEGASP VDATESRHDS DEPAPTSAAP IRSPSPSSWT ISSSSRVASS
SSFASTTSSA SRTTSATKEA TAPTETDSGA STGTNPESPV FTAGASKSVG ISGLTGIVCG
IAMAMLA
