XYN3_ASPKW
ID XYN3_ASPKW Reviewed; 211 AA.
AC P33557; G7XQI2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Endo-1,4-beta-xylanase 3;
DE Short=Xylanase 3;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase 3;
DE AltName: Full=Xylanase C;
DE Flags: Precursor;
GN Name=xynC; ORFNames=AKAW_07136;
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-34.
RC STRAIN=NBRC 4308;
RX PubMed=1368843; DOI=10.1271/bbb.56.1338;
RA Ito K., Iwashita K., Iwano K.;
RT "Cloning and sequencing of the xynC gene encoding acid xylanase of
RT Aspergillus kawachii.";
RL Biosci. Biotechnol. Biochem. 56:1338-1340(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 4308;
RX PubMed=22045919; DOI=10.1128/ec.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-210.
RC STRAIN=NBRC 4308;
RX PubMed=9930661; DOI=10.1093/protein/11.12.1121;
RA Fushinobu S., Ito K., Konno M., Wakagi T., Matsuzawa H.;
RT "Crystallographic and mutational analyses of an extremely acidophilic and
RT acid-stable xylanase: biased distribution of acidic residues and importance
RT of Asp-37 for catalysis at low pH.";
RL Protein Eng. 11:1121-1128(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; S45138; AAC60542.1; -; Genomic_DNA.
DR EMBL; D14848; BAA03576.1; -; Genomic_DNA.
DR EMBL; DF126466; GAA89022.1; -; Genomic_DNA.
DR PDB; 1BK1; X-ray; 2.00 A; A=28-211.
DR PDB; 3RI8; X-ray; 2.00 A; A=28-211.
DR PDB; 3RI9; X-ray; 2.00 A; A=28-211.
DR PDBsum; 1BK1; -.
DR PDBsum; 3RI8; -.
DR PDBsum; 3RI9; -.
DR AlphaFoldDB; P33557; -.
DR SMR; P33557; -.
DR STRING; 40384.P33557; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR VEuPathDB; FungiDB:AKAW_07136; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR InParanoid; P33557; -.
DR BRENDA; 3.2.1.8; 514.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P33557; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033119; GH11_AS_2.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Secreted; Signal; Xylan degradation.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:1368843"
FT CHAIN 28..211
FT /note="Endo-1,4-beta-xylanase 3"
FT /id="PRO_0000007991"
FT DOMAIN 28..210
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 197
FT /note="Proton donor"
FT DISULFID 119..138
FT CONFLICT 7
FT /note="F -> S (in Ref. 1; AAC60542/BAA03576)"
FT /evidence="ECO:0000305"
FT CONFLICT 12..13
FT /note="VT -> GH (in Ref. 1; AAC60542/BAA03576)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="E -> Q (in Ref. 1; AAC60542/BAA03576)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="G -> A (in Ref. 1; AAC60542/BAA03576)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="T -> S (in Ref. 1; AAC60542/BAA03576)"
FT /evidence="ECO:0000305"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1BK1"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1BK1"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 52..63
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:1BK1"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1BK1"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 133..147
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 150..163
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1BK1"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:1BK1"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1BK1"
FT STRAND 187..210
FT /evidence="ECO:0007829|PDB:1BK1"
SQ SEQUENCE 211 AA; 22627 MW; 86EFBEE12A869022 CRC64;
MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG
VSSDFVVGLG WTTGSSNAIT YSAEYSASGS SSYLAVYGWV NYPQAEYYIV EDYGDYNPCS
SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA
QHGFGNSDFN YQVMAVEAWS GAGSASVTIS S
