ID G7XTQ2_ASPKW Unreviewed; 330 AA.
AC G7XTQ2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Endo-arabinase {ECO:0000313|EMBL:GAA90311.1};
GN ORFNames=AKAW_08425 {ECO:0000313|EMBL:GAA90311.1};
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 {ECO:0000313|EMBL:GAA90311.1};
RN [1] {ECO:0000313|EMBL:GAA90311.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA90311.1};
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).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; DF126473; GAA90311.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XTQ2; -.
DR SMR; G7XTQ2; -.
DR STRING; 1033177.G7XTQ2; -.
DR VEuPathDB; FungiDB:AKAW_08425; -.
DR eggNOG; ENOG502S9PF; Eukaryota.
DR InParanoid; G7XTQ2; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08999; GH43_ABN-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..330
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003505880"
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 160
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 330 AA; 35995 MW; D7477379FDEE1A90 CRC64;
MLWTHHLPTL WALTLPLLTS VLSSPIDIRA TAGPWLALDT DFPDPGFVQA DDGTWYAFGT
NGNNRTVQVA KSSDFKTWTL LDKEALPTLA GWETQIDHWA PDVVRRNDGK YILYYSGEAQ
SDLRHHCIGT AISTTTDPSG PYIPNPTPLS CRLDQGGSID ASGFLDKDGT RYVVFKVDGN
SIGNGGDCNN GIAPLKPTPI LLQKVDTDGF TPVGDAVQIL DRDDSDGPLV EAPNLILHGD
TYFLFYSTHC YTDEKYDVRW ATAPEITGPY TKTGKQLVKS GDYGLVSPGG GTVCGCGDRM
LFHGFCAQGD SRRCMYAAEV RIQGVEFEFV
//
