ID B8MLF1_TALSN Unreviewed; 492 AA.
AC B8MLF1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Xylosidase, putative {ECO:0000313|EMBL:EED15484.1};
GN ORFNames=TSTA_049230 {ECO:0000313|EMBL:EED15484.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED15484.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; EQ962657; EED15484.1; -; Genomic_DNA.
DR RefSeq; XP_002485437.1; XM_002485392.1.
DR AlphaFoldDB; B8MLF1; -.
DR STRING; 441959.B8MLF1; -.
DR GeneID; 8100639; -.
DR VEuPathDB; FungiDB:TSTA_049230; -.
DR eggNOG; ENOG502SHWK; Eukaryota.
DR HOGENOM; CLU_009397_11_2_1; -.
DR InParanoid; B8MLF1; -.
DR OMA; FNFNWWQ; -.
DR OrthoDB; 5470935at2759; -.
DR PhylomeDB; B8MLF1; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd18618; GH43_Xsa43E-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF6; -; 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 366..492
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 251
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 190
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 492 AA; 53839 MW; 7A694442DF21A7FE CRC64;
MACIKEVNRT WVTNSAMLSP LLRPHPDRTD NMKQIKPTPL LRHLRSSFLL LGVLLNDIGI
GIAKADNPFV QSMYTADPAP LIYNDRLYVF MDHDENGATT YEMKDWRLFS TTDMANWQDH
GSPMSLANFS WANANAWAPQ IIARNNQFYF YAPVRHSTGS MAIGVGVSDT ITGPYHDALG
KPLVENNEID PTVFVDDDGQ AYLYWGNPDL WYVKLNQDMI SYSGSPIQIP LTTAGFGTRS
NNAQRPTTFE EAPWVYKRNG IYYIAYAADC CSEDIRYSTG TGPTGPWTYR GVIMPTQGGS
FTNHEGIIDY KNNSYFFYHN AALPGGSGYQ RSVCVERFVY NSDGTIPTIQ MTTAGPPQLG
TLNPYVRQEA ETAAWSSGIQ TEVCSEGGID VAFINNGDYI KVKGVAFGAS PGAHSFSARV
ASGASGGSIQ IHLGSTSGTL VGSCSVPGTG GWQTWTTVTC SVSGAVGTQD VYFVFQGSGS
GYLFNFDYWQ FS
//
