ID G4HDU2_9BACL Unreviewed; 519 AA.
AC G4HDU2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:EHB65011.1};
DE EC=3.2.1.37 {ECO:0000313|EMBL:EHB65011.1};
GN ORFNames=PaelaDRAFT_2153 {ECO:0000313|EMBL:EHB65011.1};
OS Paenibacillus lactis 154.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB65011.1, ECO:0000313|Proteomes:UP000003891};
RN [1] {ECO:0000313|EMBL:EHB65011.1, ECO:0000313|Proteomes:UP000003891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154 {ECO:0000313|EMBL:EHB65011.1,
RC ECO:0000313|Proteomes:UP000003891};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA Allgaier M., Woyke T.J.;
RT "The draft genome of Paenibacillus lactis 154.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; AGIP01000004; EHB65011.1; -; Genomic_DNA.
DR RefSeq; WP_007129325.1; NZ_AGIP01000004.1.
DR AlphaFoldDB; G4HDU2; -.
DR STRING; 743719.PaelaDRAFT_2153; -.
DR PATRIC; fig|743719.3.peg.2177; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000003891; 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; cd09002; GH43_XYL-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:SF2; XYLOSIDASE_ARABINOSIDASE; 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 343..511
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 160
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 519 AA; 57420 MW; 39D348FD54952BBE CRC64;
MTHAEAESRD EGYGLNRPAR SELDDASGQD AALQDSVPQA PVHEDAVLQD SDAGLYAPII
AGNYADPSII RVGDDYYMTH SSYKLTPGLI IWHSRDLRNW RRVGAALTRY AGDVWAPDFV
MHNDRFYIYY PAGGTNWVVT ASNPAGPWSE PACLGIRGID PGHTVGPDGK RYLHMSGGAF
AALSDDGLSV IGEVKQVYDG WRYPQDWVVE AYSLEGPKVT YHNGYYYLTV AVGGTAGPPT
SHMAVSSRSR TPWGPWEHSP YNPIIRTWSK EEPWWSKGHA SLIDTPDGEW WMVYHAYRNG
YHTLGRQTLL ERVEWSADGW FRVAGRGRGV NSPPQEVLLD SLNEAELGLH WQCEGCAPSS
RFRTGPNGLT AEGTAEGAER SPLFFMPGHE RYTAQVEIAV EGDAEGRLLL YYNDSAYLGI
GISAKGVRHF RSFKSYAAIP TGGGRAFLRI VNDEHIVSFY FSSDGAEWFR YDKTVEVSGM
HHNTLGGFQS LRIGLDVAGA GKAIFRNFSY EAEAWTAGQ
//
