ID A0A0D0WU82_9ACTN Unreviewed; 496 AA.
AC A0A0D0WU82;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KIR62199.1};
GN ORFNames=TK50_27895 {ECO:0000313|EMBL:KIR62199.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR62199.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR62199.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR62199.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-2015) 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:KIR62199.1}.
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DR EMBL; JXSX01000003; KIR62199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0WU82; -.
DR PATRIC; fig|47853.6.peg.5852; -.
DR Proteomes; UP000032254; 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:UP000032254}.
FT DOMAIN 288..493
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 182..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 105
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 496 AA; 53451 MW; 5D8E7AE3ABE97AAA CRC64;
MCRVGDDYYL VCSSFEYFPG VPLLHSRDLV NWRQVGNVLD RPSQLELPAD TPASQGVYAP
TIRHHDGRFW VVTTNVSLGR HLIVTAQDPA GPWSDPVYLD LPHVDPSLAW DDEGNCWLTT
SGVKSYRIDP DTGRVLEGPI PLWSGTGGQY PEAPHLYRID GWWYLLLSEG GTHTGHAVSV
ARSRSPRGPF APAPTNPILT HRGSNLPVQA TGHADLVQSP DGSWWMVLLG IRAKGQWPPY
HVLGRETFLV PVRWVDGWPV VDPVEEVTAA PAGSAPALAA PAEAGAYRDD FDAAVLAPGW
VSPRSRPDAA WSLTARPGWL TLNATGATLD RAGATIVATR QRHHDCRASA RLDPGGGTAG
LTIRIDEAHH YDLEVSAGRV RVVGRVGPFR QVFAELAVPP GPLVLTIATR THDLRPPTVT
CAADLSAGAA PFGVRAAACD MVAFEVQTSD GPRVLAELDG RYLSTEVAAG FTGRVIGMYV
TEGSAAFDWF DYRPAG
//