XGEA_ASPAC
ID XGEA_ASPAC Reviewed; 238 AA.
AC O94218; Q6YBY2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Xyloglucan-specific endo-beta-1,4-glucanase A;
DE EC=3.2.1.151;
DE AltName: Full=Xyloglucanase A;
DE AltName: Full=Xyloglucanendohydrolase A;
DE Flags: Precursor;
GN Name=xgeA;
OS Aspergillus aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=KSM 510;
RX PubMed=9884411; DOI=10.1093/glycob/9.1.93;
RA Pauly M., Andersen L.N., Kauppinen S., Kofod L.V., York W.S.,
RA Albersheim P., Darvill A.;
RT "A xyloglucan-specific endo-beta-1,4-glucanase from Aspergillus aculeatus:
RT expression cloning in yeast, purification and characterization of the
RT recombinant enzyme.";
RL Glycobiology 9:93-100(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-238, AND FUNCTION.
RX PubMed=15094064; DOI=10.1016/s0014-5793(04)00346-1;
RA Park Y.W., Baba K., Furuta Y., Iida I., Sameshima K., Arai M., Hayashi T.;
RT "Enhancement of growth and cellulose accumulation by overexpression of
RT xyloglucanase in poplar.";
RL FEBS Lett. 564:183-187(2004).
CC -!- FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in
CC xyloglucan with retention of the beta-configuration of the glycosyl
CC residues. Specific for xyloglucan and does not hydrolyze other cell
CC wall components. {ECO:0000269|PubMed:15094064,
CC ECO:0000269|PubMed:9884411}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.4. Stability declines sharply below pH 2.8 and above
CC pH 5.0. {ECO:0000269|PubMed:9884411};
CC Temperature dependence:
CC Optimum temperature is below 30 degrees Celsius. Is very stable below
CC 35 degrees Celsius, but at 50 degrees Celsius, it loses 80 percent of
CC its activity within 2 h. {ECO:0000269|PubMed:9884411};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC {ECO:0000305}.
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DR EMBL; AF043595; AAD02275.1; -; mRNA.
DR EMBL; AY160774; AAO20340.1; -; mRNA.
DR PDB; 3VL8; X-ray; 1.90 A; A=15-238.
DR PDB; 3VL9; X-ray; 1.20 A; A/B=15-238.
DR PDB; 3VLB; X-ray; 2.70 A; B/D=21-238.
DR PDBsum; 3VL8; -.
DR PDBsum; 3VL9; -.
DR PDBsum; 3VLB; -.
DR AlphaFoldDB; O94218; -.
DR SMR; O94218; -.
DR CAZy; GH12; Glycoside Hydrolase Family 12.
DR CLAE; XEG12A_ASPAC; -.
DR KEGG; ag:AAD02275; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_77812; -.
DR BioCyc; MetaCyc:MON-16602; -.
DR BRENDA; 3.2.1.151; 488.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase 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 Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR002594; GH12.
DR PANTHER; PTHR34002; PTHR34002; 1.
DR Pfam; PF01670; Glyco_hydro_12; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..238
FT /note="Xyloglucan-specific endo-beta-1,4-glucanase A"
FT /id="PRO_5000054062"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3VLB"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3VL9"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 47..59
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 62..73
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3VLB"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3VL9"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 100..125
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 130..141
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3VL9"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:3VL9"
FT STRAND 209..235
FT /evidence="ECO:0007829|PDB:3VL9"
SQ SEQUENCE 238 AA; 25159 MW; FCCA6746D9AEC1B1 CRC64;
MKLSLLSLAT LASAASLQRR SDFCGQWDTA TAGDFTLYND LWGESAGTGS QCTGVDSYSG
DTIAWHTSWS WSGGSSSVKS YVNAALTFTP TQLNCISSIP TTWKWSYSGS SIVADVAYDT
FLAETASGSS KYEIMVWLAA LGGAGPISST GSTIATPTIA GVNWKLYSGP NGDTTVYSFV
ADSTTESFSG DLNDFFTYLV DNEGVSDELY LTTLEAGTEP FTGSNAKLTV SEYSISIE
