ID G3YFQ1_ASPNA Unreviewed; 386 AA.
AC G3YFQ1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 1 {ECO:0000256|ARBA:ARBA00041265};
DE AltName: Full=Exo-1,3-beta-glucanase A {ECO:0000256|ARBA:ARBA00041261};
GN ORFNames=ASPNIDRAFT_52811 {ECO:0000313|EMBL:EHA17789.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA17789.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA17789.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
RN [2] {ECO:0007829|PDB:6I1A}
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 18-386, AND DISULFIDE BONDS.
RX PubMed=31943739; DOI=10.1111/febs.15208;
RA Pachl P., Kapesova J., Brynda J., Biedermannova L., Pelantova H.,
RA Bojarova P., Kren V., Rezacova P., Kotik M.;
RT "Rutinosidase from Aspergillus niger: crystal structure and insight into
RT the enzymatic activity.";
RL FEBS J. 287:3315-3327(2020).
CC -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC the main structural component of the cell wall. It could also function
CC biosynthetically as a transglycosylase.
CC {ECO:0000256|ARBA:ARBA00037254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:EHA17789.1}.
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DR EMBL; ACJE01000021; EHA17789.1; -; Genomic_DNA.
DR PDB; 6I1A; X-ray; 1.27 A; A/B=18-386.
DR AlphaFoldDB; G3YFQ1; -.
DR SMR; G3YFQ1; -.
DR STRING; 380704.G3YFQ1; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1188538; -.
DR HOGENOM; CLU_004624_2_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6I1A};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..386
FT /note="glucan 1,3-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003460546"
FT DOMAIN 91..330
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT CARBOHYD 128
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 176
FT /note="N-acetyl-D-glucosamine 3"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 177
FT /note="N-acetyl-D-glucosamine 4"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 178
FT /note="N-acetyl-D-glucosamine 3"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 181
FT /note="N-acetyl-D-glucosamine 4"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 214
FT /note="N-acetyl-D-glucosamine 5"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 361
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:6I1A"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6I1A"
FT DISULFID 72..79
FT /evidence="ECO:0007829|PDB:6I1A"
SQ SEQUENCE 386 AA; 43102 MW; DA0CFE399B2E6386 CRC64;
MYSLLGLLAA LGCAQSALAA PLASPPNSSY IDWRTFKGNG VNLGGWLEQE STIDSLFWDK
YSGGASDEWG LCEHLGSQCG PVLEHRYATW ITKADIDKLA SGGITVLRIP TTYAAWIDLP
SSQLYSGNQT AYLKEIADYA IKTYNMHIII DTHSLPGGVN GLTIGEATGH WYWFYNETNF
NYSMQVIDQV INFIQTSGSP QSYTLEPINE PADNNTNMVV FGTPLALTDH GAAWVLKYIR
AVVQRVESVN PNIPVMFQGS FKYPQYWEGD FPASTNLVFD THHYYYEHMD SSSENLPEYI
LADAREKSGT GKFPVFVGEW AIQATYNNTL ALRKRNVLAG LETWSSFSQG SSYWTAKFTG
NTSVAGQGEQ KDYWCYETFI DEGYFN
//
