ID A0A0E3ZT21_9BACT Unreviewed; 560 AA.
AC A0A0E3ZT21;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:AKD53825.1};
GN ORFNames=SD10_01815 {ECO:0000313|EMBL:AKD53825.1};
OS Spirosoma radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD53825.1, ECO:0000313|Proteomes:UP000033054};
RN [1] {ECO:0000313|EMBL:AKD53825.1, ECO:0000313|Proteomes:UP000033054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5A {ECO:0000313|EMBL:AKD53825.1,
RC ECO:0000313|Proteomes:UP000033054};
RX PubMed=24748440; DOI=10.1007/s00284-014-0584-x;
RA Lee J.J., Srinivasan S., Lim S., Joe M., Im S., Bae S.I., Park K.R.,
RA Han J.H., Park S.H., Joo B.M., Park S.J., Kim M.K.;
RT "Spirosoma radiotolerans sp. nov., a gamma-radiation-resistant bacterium
RT isolated from gamma ray-irradiated soil.";
RL Curr. Microbiol. 69:286-291(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP010429; AKD53825.1; -; Genomic_DNA.
DR RefSeq; WP_046375419.1; NZ_CP010429.1.
DR AlphaFoldDB; A0A0E3ZT21; -.
DR STRING; 1379870.SD10_01815; -.
DR KEGG; srd:SD10_01815; -.
DR PATRIC; fig|1379870.5.peg.399; -.
DR HOGENOM; CLU_016508_2_2_10; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000033054; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033054};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..560
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002417208"
FT DOMAIN 361..552
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 145
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 560 AA; 63129 MW; A989866BA2FEAC57 CRC64;
MRNRLFTALF AILSLVLTHK LPAQTTLVNP ILTGFYPDPS IVRVGTDYYL VNSTFSYFPG
IPVLHSKDLK NWKQIGNVID RPSQMDFMGE RLTRGLFAPA IQYYKGTYYV TCTDIDHDGN
FIVTAKNPAG PWSNPVKLPQ VHGIDPSLYF DDATDKAYII YNSDAPDRKP LYSGHRTIRI
YELDYTNLKV VGEEKQLVNG GVDLSKKPVW IEAPHIMKVK DWYYLYAAEG GTSVNHTEVV
FRSKSVWGPF VPYENNPILT QRGLPADRKE PITSAGHAQF VEGPDGKWYA VFLAVRPYEG
DYYNTGRETF IAPVEWKNDW PIVDPANKVI QYTYPAAWKE VKQKDALPQS GNFAYTLRFD
KALDPALLFM RTMDKSAFSL SKKDGLTMKL KPETVMEMGN PAFIGKRQQH LNSMAETELS
FSPKSDKEKA GLLILQDEYH FYFLSKSTAQ GKDVLQLFKS DPKTKAMEVL AEVPLTAKTG
KVGLRIASQG GTYSFSFSED AKNWKLLKDN VDARFLSTKE AGGFIGCLYG MYATSSGEPT
TNSASFQYLS YKGDDPMYKK
//
