ID A0A0L0KP88_9ACTN Unreviewed; 493 AA.
AC A0A0L0KP88;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KND39653.1};
GN ORFNames=IQ63_02450 {ECO:0000313|EMBL:KND39653.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND39653.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KND39653.1}.
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DR EMBL; JPPY01000020; KND39653.1; -; Genomic_DNA.
DR RefSeq; WP_050369177.1; NZ_KQ257800.1.
DR AlphaFoldDB; A0A0L0KP88; -.
DR PATRIC; fig|42234.21.peg.508; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000037151; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037151}.
FT DOMAIN 300..474
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 126
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 493 AA; 52985 MW; 0F306786E4BE195C CRC64;
MPHNVTPIVP GFHPDPSVCR VGEDYYLVTS SFEYFPGIPV FHSRDLVRWE QIGNVLDRPS
QLNVRTGREG ASAGIYAPTI RHHDGEFWVV TTNRDDVMKG HLIVRASDPA GEWSDPVHTS
GAIGIDPDLA WDEDGTCYLT WSIPQGIVQV TVEPATGKVL SEPRVIWGGT ALAHTEGPHL
IRRGAYWYLL VAEGGTGPGH GVCVARSSSP SGPWEEHPAN PVLSHRGTDH PVQNTGHADL
VELPGGSWAL VHLGVRPLGT FPMSHVNGRE TFLAAVDWAD DWPVIVEDRY DVPPAPTAFT
DDFAARRLHP RWIAPGTDPR TFAVPTAGAG LRLLPGRAPA ARHAERLLAV RARDASWTAS
ATVPEGDVVL VVRIDDAHWA AVERRGATLS ARVVIGPLDQ VLATAEGIAA DSPLALRAVA
NTDEYSSKGP DEVHLGYLAD GRFETLATVD GRYVSTEVAG GFTGRVIGVE ALGTEAVLTR
FTYAPEALPA TES
//
