ID A0A0A2TUT3_9BACL Unreviewed; 503 AA.
AC A0A0A2TUT3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:KGP79787.1};
GN ORFNames=P364_0122465 {ECO:0000313|EMBL:KGP79787.1};
OS Paenibacillus sp. MAEPY2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP79787.1, ECO:0000313|Proteomes:UP000030061};
RN [1] {ECO:0000313|EMBL:KGP79787.1, ECO:0000313|Proteomes:UP000030061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP79787.1,
RC ECO:0000313|Proteomes:UP000030061};
RX PubMed=24526641;
RA Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL Genome Announc. 2:0-0(2014).
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:KGP79787.1}.
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DR EMBL; AWUK01000031; KGP79787.1; -; Genomic_DNA.
DR RefSeq; WP_024632450.1; NZ_AWUK01000031.1.
DR AlphaFoldDB; A0A0A2TUT3; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000030061; 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}.
FT DOMAIN 309..500
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 120
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 503 AA; 55728 MW; D31F522814BBCA9D CRC64;
MNYTNPVISG FYPDPSICRV DDDYYLVTST FEYFPGVPIF HSKDLVNWRQ IGHVLTSAKQ
LPLANAGSSG GIYAPTLRHH DGWFYMTTTN VSGGGNFFVR SRAAEGPWSD PIFVAQDGID
PSLLFDEDGR IYFQTACNGD KGEGIYQCEI DISTGHKLTE SQFIWSGTGG AAPEAPHLYR
INDFYYLMIA EGGTEYGHME TIARSTNPYG PFDPCPHNPI LSNRSIKSSI HATGHADLIQ
AQDGSWWAVC LGIRPAAYPM RHHLGRETFL APVTWTSDGW PIIGHDGHIE PVMTGPQLAE
VHWPRNAIRD DFDGSTLGLD WIFLRNPAPG SWSLTEYPGH LVLRGNPVSL NDGRNPAFVG
RRLSHFLCNV AAKLNFEPIH DGDESGLTVF MNERYHYDLA IKRINGQKKI IFRRTIASLR
TEEIQDCEAG PVILQIQAQR DLFTFSIQQG STIGTVLGSG DTHLLSTEVA GGFTGVILAM
YAYSPSGEGA PSQFDWFDYE PLD
//
