ID I4EXS3_9ACTN Unreviewed; 499 AA.
AC I4EXS3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:CCH88186.1};
GN OrderedLocusNames=MODMU_2757 {ECO:0000313|EMBL:CCH88186.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88186.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH88186.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88186.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FO203431; CCH88186.1; -; Genomic_DNA.
DR RefSeq; WP_014740778.1; NC_017955.1.
DR AlphaFoldDB; I4EXS3; -.
DR STRING; 477641.MODMU_2757; -.
DR KEGG; mmar:MODMU_2757; -.
DR PATRIC; fig|477641.3.peg.2614; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016508_2_0_11; -.
DR OMA; FAIHICT; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000006461; 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; 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; 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:UP000006461}.
FT REGION 207..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 13
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 121
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 499 AA; 52912 MW; 2318A1C7A0F33E82 CRC64;
MTQRPVLPGF HPDPSTCRVG ETYLLATSSF EYAPGVPLFS STDLRSWEQI GNVLDRPSQL
DVSKAGPSGG IFAPTLRHHD GRFWMITTNW SDDGGQLLVH AEDPAGPWSE PVRIPSAIGI
DPDLAWDDEG TCLMTYAGFG PHGGEGIVQS AIDPLTGEVL TERRQIWNGT GGKFPEGPHL
YRIGEWWYLL IAEGGTERGH AVTIARSRTP HGPFEGDPAN PLLTSRGTDS PVQNTGHADL
VQRPDGSWAI VYHGVRARGS SPEWHVLGRE TFADEVTWTD GWPVLTGHVE PAAGTGAVVE
TVEGSDLPVS WVGASCHLGE VVTGEDGGWR LTASGDGPVF VGRRQEHLFA VVRARLAVTG
TGGLSLRIDP RHALDLEVSD GTVRAVWAVG DVRHELGRAE LTGEAELELR ALPSQGHEFS
TARGPDRVVA GVVVDGGFTA LGEVDGRYLS TEVAGGMTGR MAGVVSSSGS VLVRSFSYLG
ADDPAVVGGG AADPQPWAS
//
