ID A0A085EQH1_9BURK Unreviewed; 529 AA.
AC A0A085EQH1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KFC61466.1};
DE EC=3.2.1.37 {ECO:0000313|EMBL:KFC61466.1};
GN Name=xynB_3 {ECO:0000313|EMBL:KFC61466.1};
GN ORFNames=FG94_05107 {ECO:0000313|EMBL:KFC61466.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC61466.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC61466.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC61466.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-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:KFC61466.1}.
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DR EMBL; JNNN01000083; KFC61466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085EQH1; -.
DR STRING; 1502852.FG94_05107; -.
DR PATRIC; fig|1502852.3.peg.5023; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 8866236at2; -.
DR Proteomes; UP000028601; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..529
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001788969"
FT DOMAIN 330..523
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 195
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 142
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 529 AA; 57402 MW; FCB229F1CB9CF868 CRC64;
MRFGLAAWAA LGLSCAINAA AGEYRNPVIP GFNPDPSICR DGEDYYVATS TFEYFPGVPI
YHSKDLVNWR LLGHALERPS QLPLAGQKSS MGIFAPTLRC GNGHFYMITT NVAGGGNFIV
HATNPAGPWS EPVWIKDVQG IDPSLFFDDD GKVYLTYQDG GERGGIGQVE IDVATGQLKG
EPRRIWNGTG GVWPEGPHLY KINGWYYLLH AEGGTSYGHV VILARSRSPW GPFEGAPDNP
ILTHRDRPDL LLQALGHADL VQTPEGKWFM VLLGVRHLKH KHHLGRETLL APVEWTQDGW
LKINGGAPLL EKVEAAGLPA PHPWPASAAR EEFGARKLGG EWIFLRGPAQ DLWSLSERPG
FLRLKGSKLS LADIGTPAFV GKRQAHLDLR ASTLLDFTPR AKGQQAGLAL RMNEDNHYQL
LVAGTGKGRV IRLVTRVKGV STVVREAPLG AGKVELSVRA SPERYVFGYR IGGREVADFG
SAPTAPLSSE DAGGFTGVVL GMVANSGDGA PMPPADFDWF DYRPSDGKK
//
