ID E8NDD9_MICTS Unreviewed; 507 AA.
AC E8NDD9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:BAJ74997.1};
GN OrderedLocusNames=MTES_2033 {ECO:0000313|EMBL:BAJ74997.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ74997.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ74997.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ74997.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; AP012052; BAJ74997.1; -; Genomic_DNA.
DR RefSeq; WP_013585122.1; NC_015125.1.
DR AlphaFoldDB; E8NDD9; -.
DR STRING; 979556.MTES_2033; -.
DR KEGG; mts:MTES_2033; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016508_2_0_11; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000008975; Chromosome.
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 322..492
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 216..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 18
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 191
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 507 AA; 54062 MW; 66108315C38CF23F CRC64;
MTTTAPLPNP LIAGFHPDPS AVRVGDTWYL ATSTFEYLPG IPIHRSTDFV EWELIGHVAT
RPGQLAVEDV PTAGGAWAPT LRHRDGIFHV VVTDAMGRGM LHFTATDPAG PWSDGDLLTV
PDGSRSLDGI DPDIAWDAAG TAYITYSGLI LGGPDAGTHT GIQQARVDLE THRALEEPRS
LWSGVGGMFP EAPHLYEIDG RWYLLIAEGG TERGHGVSLA RADSPEGPFE AAPGNPLVSA
RSTTRPVQNT GHGDLVTGPD GEWVCVLLGV RPRGMTRAFS ALGRETFVTR VAWQADGWPT
IEPVPLNPRP GTRVEVAFSP ETPLDGEWIA VRSLPTDHAD LTSRPGWMRL DADGSTLGDP
RPVFVGRRQV HLAQRTSVTV DVSAGVGGLA VRYDERFHVE VEAGAGEIVA RAVLGDVVQE
WRTPLTATTL TLHIDCGPGS SAVSFAPAIH ALHLGATVDG QRLALAEVDG RFLSSEVTES
FTGRVIGVYA REGRIDATAW VAEGDDA
//
