ID A1A2Q1_BIFAA Unreviewed; 548 AA.
AC A1A2Q1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Xylan beta-1,4-xylosidase {ECO:0000313|EMBL:BAF39984.1};
GN Name=xynB {ECO:0000313|EMBL:BAF39984.1};
GN OrderedLocusNames=BAD_1203 {ECO:0000313|EMBL:BAF39984.1};
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF39984.1, ECO:0000313|Proteomes:UP000008702};
RN [1] {ECO:0000313|EMBL:BAF39984.1, ECO:0000313|Proteomes:UP000008702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC {ECO:0000313|Proteomes:UP000008702};
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) 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; AP009256; BAF39984.1; -; Genomic_DNA.
DR RefSeq; WP_011743526.1; NC_008618.1.
DR AlphaFoldDB; A1A2Q1; -.
DR STRING; 367928.BAD_1203; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; bad:BAD_1203; -.
DR HOGENOM; CLU_016508_2_1_11; -.
DR Proteomes; UP000008702; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008702}.
FT DOMAIN 343..540
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 224..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 188
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 548 AA; 62642 MW; 3EFD8AA9E83FF23A CRC64;
MLHNPIFKGF NPDPAICRKG DDYYVAVSTF EWFPGIPIYH SKDMKHWELL THVLTDDTKP
NLTKLPSAKG IWAPCLTYCE EEDMFYVIYG VMNSMNARYF DVNNYLIKSK SIEGPWSEPV
YLTSSGFDAS ILHDDNGKKY IVSLEWETRE GYEKPGVICC VEYDPETKHV VGYPKRIWRG
ATDRGCIEAP HLTKRDGWYY IMCAEGGTGY NHAVTMGRSR NVWGPYEPDP NGPLVTSQPK
ESNERADDDH LKPRYFNPDS VLQKSGHGSY VDLPNGETYL VHLTSRPFVP ELRCTLGRET
AIQKMTWTND GWLRMADGSN LAKLEVEEPD LPDAPMPEIP GHDDFDGGAI GNWYYSPRQM
PTTFANVTER PGWLRIRGEE SLASLNRTSL IARKLTSVYA TVTTKMEFEP EVYQHSAGLT
IYYDNMNNIF LRKYYSQTLG GSAISIVRLE NGEKTEMLDT RVAVEDKPIY FRLNIEGRRT
WFEWGYDGEN WTKIGPDFDT TTFSDEYCKY GEFTGTMVGI AITDAALHEK TADFDFFDYE
ADETKPVD
//
