ID E3FVI8_STIAD Unreviewed; 537 AA.
AC E3FVI8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Beta-xylosidase (1,4-beta-D-xylan xylosidase) {ECO:0000313|EMBL:ADO72202.1};
GN OrderedLocusNames=STAUR_4422 {ECO:0000313|EMBL:ADO72202.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO72202.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO72202.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO72202.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP002271; ADO72202.1; -; Genomic_DNA.
DR RefSeq; WP_013376240.1; NZ_AAMD01000194.1.
DR AlphaFoldDB; E3FVI8; -.
DR STRING; 378806.STAUR_4422; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; sur:STAUR_4422; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_543697_0_0_7; -.
DR OrthoDB; 9760116at2; -.
DR Proteomes; UP000001351; 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; cd08999; GH43_ABN-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:SF5; ENDO-ARABINASE; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003169988"
FT DOMAIN 352..506
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 24..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 227
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 167
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 537 AA; 57205 MW; 32E38155ED8A91DC CRC64;
MRSRGVFLSA ALLSLTVLAA LTAPGCSSDE PKPPENPPEN PPPPPPALDI TNPVLSGDYP
DPSILRVEDT YWATATSSEW APHFPLLRST DLLHWELVGP VFESEPTWSE GNYWAPELAT
DNGRYFIFYT AKKKGGPLCV AVATASQVSG PYTDRGPLVC QALGSIDGAL IRDENNVLYL
VWKEDGNSQG LPTPLWAQPL SEEGTQLIGE KKQILLNDTP WEGQVVEGPY LLRRNGWFYL
FYAGAGCCGR ACNYGVGVAR SKTLLSGWEK HPLNPIVKNN ASWKCPGHGS VVTDPLGRDY
LLYHAYSTTD SVYVGRQGVL DAIQWGEDEW PSINSRRGTG GKVLATPPAF FDDFTATALV
PGWQWPKSRA PSTALTGGVL TLAPPTAQAA DPIGATLARS TNTGTYTAEA ILEVGDLSAE
TSAGLAASGD PENGLGIALQ AGKVALWIRK GNTHAVDAST SREAPVANGK LHLRMTARSG
HLYRFAVSGD GASWTDVGGE LNGDFLPPWD RGVRVALTGG GGAGAAARFD SLRITPE
//
