ID G7Y008_ASPKW Unreviewed; 527 AA.
AC G7Y008;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:GAA92503.1};
GN ORFNames=AKAW_10617 {ECO:0000313|EMBL:GAA92503.1};
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:GAA92503.1};
RN [1] {ECO:0000313|EMBL:GAA92503.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA92503.1};
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; DF126495; GAA92503.1; -; Genomic_DNA.
DR AlphaFoldDB; G7Y008; -.
DR SMR; G7Y008; -.
DR STRING; 1033177.G7Y008; -.
DR VEuPathDB; FungiDB:AKAW_10617; -.
DR eggNOG; ENOG502QQH8; Eukaryota.
DR InParanoid; G7Y008; -.
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; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT DOMAIN 328..526
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 131
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 527 AA; 60209 MW; B4BE010D98637FFA CRC64;
MYINPILPGF NPDPSIIRVG KDFFLVTSSF EYFPGAPIYH STDLIQWTLI GHALTRSSQL
QIQTPEPGGG VWATTLRYHD GVFYILAACF QRYRPQEDDR VWPRGFYVKT TDIWDSKSWS
DPVYFDQVGF DQDLFWDDDG TVYLSSTYRK LERTPGANLK DFAVHIVTVD LETGASTSEP
KLIRESSSGV AEGSHIFKRG KYYYLFTAEG GTESGHCEWV SRSTTGPFGP WEAGPHNPLW
RNGVDDDVQN TGHADLVEDV QGQWWAVLLG VRPVWKDGQW EESVFGRETF LAPVDWKDDW
PIVNSGQKIP LHSKSPHLYE LSVLVAWRDD FSDSELQLGW YRKNTPVVRD YCLTERPGFL
RLYGGPYDLS VPACPTLFLR KQTHRFCTWE TRLSFHPRNQ VCEAGAVVWW TYFTYSRIGL
RLGKDGQRIV RLRFPGGEVV DFGLRHSQSN VRLVIECGDS YRFGFQELSD IESDDALIEW
IGEVDNSSMT AAPPVGVAFT GMMLGLYAFG ERQRCLDPAD FHYAQWK
//
