ID A0A117E189_ASPNG Unreviewed; 1587 AA.
AC A0A117E189;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE AltName: Full=Exo-1,3-beta-glucanase D {ECO:0000256|ARBA:ARBA00041260};
GN ORFNames=ABL_05191 {ECO:0000313|EMBL:GAQ42530.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ42530.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan. {ECO:0000256|ARBA:ARBA00037126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ42530.1}.
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DR EMBL; BCMY01000007; GAQ42530.1; -; Genomic_DNA.
DR PaxDb; 5061-CADANGAP00008917; -.
DR VEuPathDB; FungiDB:An11g07650; -.
DR VEuPathDB; FungiDB:An11g07660; -.
DR VEuPathDB; FungiDB:An11g07670; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1127838; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1127841; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1147158; -.
DR VEuPathDB; FungiDB:ATCC64974_92850; -.
DR VEuPathDB; FungiDB:ATCC64974_92860; -.
DR VEuPathDB; FungiDB:ATCC64974_92870; -.
DR VEuPathDB; FungiDB:M747DRAFT_286902; -.
DR VEuPathDB; FungiDB:M747DRAFT_325558; -.
DR VEuPathDB; FungiDB:M747DRAFT_334460; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR021858; Fun_TF.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF11951; Fungal_trans_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..218
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 271..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1587 AA; 179347 MW; D24B9B580C0849B1 CRC64;
MASILPRVGF RALTALPRAT PLPRVSFTQL PRVQPRVQPL TRRFLATIPQ EQPRLRLGST
APNFKALTTH GEIDFHEFIG NSWAILFSHP ADFTPVCTTE LGAFAKMKDE FEKRGVKMIG
LSANDLSSHD QWIDDINEVA NTNVQFPIIA DADRKVAFLY DMVDQRDLDN IAEKGIPFTI
RSVFIIDPEK KIRLTMSYPA STGRNSAEVL RVIDSLQTAD RKGIATPIDW QVGEDVIVPP
SVSTEDAKKK FGEVRELKPY LRYTNSRLHC MPSHSRSRDR LSPSSELDDA DPVYSPSVYQ
REHYNNNDSL FDSTEEDYAR APRNVYSYET HDEYHDDDDD DDDDDNVHED DHDREYDDKF
GEPWVPLRAQ VEGDQWREGF ETAIPKEEDV TQAKEYQYQM SGALGDDGPP LPSGSLGKGK
GKKRLDRETR RQRRKERLAA FFKHKNGDAS AGLVSGDALA KLLGSQDGDE DCLSHLGSER
ADSMSQKNLE GGRQRKLPVL SEEPMMLRPF PAVAPTGQTQ GRVVSGAQLE QGGPGIEMRH
RGGGGPPTEA LLQKEGDWDG STKGSSASAR PSFWKRYHKT FIFFAILIIM AAIAIPVGII
EARRLHGTNG GDNTSNSNLK GISRDSIPAY ARGTYLDPFT WYDTTDFNVT FTNATVGGLS
IMGLNSTWND SAQANENVPP LDEKFPYGSQ PIRGVNLGGW LSIEPFIVPS LFDTYTSSEG
IIDEWTLSKK LGDSAASVIE KHYATFITEQ DFADIRDAGL DHVRIQFSYW AIKTYDGDPY
VPKIAWRYLL RAIEYCRKYG LRVNLDPHGI PGSQNGWNHS GRQGTIGWLN GTDGELNRQR
SLEMHDQLSQ FFAQDRYKNV VTIYGLVNEP LMLSLPVEKV LNWTVEATNL VQKNGIKAWV
TAHDGFLNLA KWDKMLKTRP SNMMLDTHQY TVFNTGEIVL NHTRRVELIC ESWYSMIQQI
NITSTGWGPT ICGEWSQADT DCAQYVNNVG RGTRWEGTFS LTDSTQYCPT ASEGTCSCTQ
ANAVPGVYSE GYKTFLQTYA EAQMSAFETA MGWFYWTWAT ESAAQWSYRT AWKNGYMPKK
AYSPAFKGVN VRFRNGLDIF GDDDTLFPER DLWPYLMGPL RFVDETVIIK RLYEVEEPEH
NGPTEQSHGV NDAPITPVGV VEYYGLEQYT SPLTDDTPPI QTLCHDDRSS ELELLVGNAL
KPSDKYYGRE LQAGGLVQEQ RYSFNEREAK LMRNYVENMA LWADITDPHR HFEIEVPVRA
MQDPVLRYAI FAFSSRHVER QRKGNEAEAL QYHNHCLQLL IPTLSGIGGD LTDVVLATVA
ILRQHEEMEY DDNQFHLTGA TRIMNTVSSF GSSGGLGEAA AWLCLREDIH VSLISQKPLR
TNLESFHRSD IFLRNDDFAW AARMVFLLAK VLKCAFNQMS SPEYTALQSI AQEVEDWNAR
KPPSFQPLRE LPRGKDVSCR FPEMWMLLPV HVVGTQYYHI AKIVLAFACC PSPPLAYESF
RNSRNIEKTI RYHLFMVLGL AKSNPKAENT LFTARHSLVA WGWVIRQKAD QQAAEILLRE
MWTRTGWDVT ASIQSLREQW ADEETDS
//
