ID A0A0Q9MGF2_9BACL Unreviewed; 525 AA.
AC A0A0Q9MGF2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KRE60276.1};
GN ORFNames=ASL11_24575 {ECO:0000313|EMBL:KRE60276.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE60276.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE60276.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE60276.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE60276.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE60276.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRE60276.1}.
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DR EMBL; LMSD01000033; KRE60276.1; -; Genomic_DNA.
DR RefSeq; WP_056620762.1; NZ_LMSD01000033.1.
DR AlphaFoldDB; A0A0Q9MGF2; -.
DR STRING; 1736398.ASL11_24575; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000051252; 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; cd09000; GH43_SXA-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 323..522
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 187
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 128
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 525 AA; 60148 MW; 34597C7F0775FE63 CRC64;
MSYITNPILP GFNPDPSILR VEDNYYIATS TFEWFPGVQI HHSKDLVHWQ LLPHPLTRTS
QINMEGNLDS CGIWAPCLSY DKGIYYLIYT DVKSRIGAYK DTHNYLVTAT DIKGPWSEPI
YLNSSGFDPS LFHDDDGRKW LVNMLWDSRK GHNRFAGIVL QEYSIEEQKL VGPISNIFKG
TELKLTEGPH LYKHNGYYYL LTAEGGTQYN HAATMARSRH IQGPYKVDPQ NPILTSAGRP
DLPLQKSGHA SLVTTPAGEW YMAHLCARPV KDKYCNLGRE TAIQRCEWSE DGWLRLAGGS
RYPLLHVPAP DLQPFPFESE PEKDDFDGGE LSVHWSTLRI PADPTWLSLK DRPGYLRLRG
MESMISMHRQ SLVARRQQAF RCEAETCLEF DPDHFQQMAG LILYYDTKDY VYLRLTHHEE
SGICLGILQS KNGVQDELLD QDVSMNGNSR FRLKVVVDRE NAQFYYVNSD EQWTAIGVAI
DISHLSDDFP DYIRFTGTFI GMCVQDLGGT QKHADFDYFI YKEIE
//
