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Database: UniProt
Entry: A0A087EAU8_9BIFI
LinkDB: A0A087EAU8_9BIFI
Original site: A0A087EAU8_9BIFI 
ID   A0A087EAU8_9BIFI        Unreviewed;       533 AA.
AC   A0A087EAU8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Glycoside hydrolase family 43 protein {ECO:0000313|EMBL:MSS13404.1};
DE   SubName: Full=Xylosidase {ECO:0000313|EMBL:KFJ04899.1};
DE            EC=3.2.1.37 {ECO:0000313|EMBL:KFJ04899.1};
DE            EC=3.2.1.55 {ECO:0000313|EMBL:KFJ04899.1};
GN   ORFNames=BITS_1417 {ECO:0000313|EMBL:KFJ04899.1}, FYJ32_08160
GN   {ECO:0000313|EMBL:MSS13404.1};
OS   Bifidobacterium tsurumiense.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=356829 {ECO:0000313|EMBL:KFJ04899.1, ECO:0000313|Proteomes:UP000029080};
RN   [1] {ECO:0000313|EMBL:KFJ04899.1, ECO:0000313|Proteomes:UP000029080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13495 {ECO:0000313|EMBL:KFJ04899.1,
RC   ECO:0000313|Proteomes:UP000029080};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MSS13404.1, ECO:0000313|Proteomes:UP000482439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSM-380-WT-2B {ECO:0000313|EMBL:MSS13404.1,
RC   ECO:0000313|Proteomes:UP000482439};
RA   Wylensek D., Hitch T.C.A., Clavel T.;
RT   "In-depth cultivation of the pig gut microbiome towards novel bacterial
RT   diversity and tailored functional studies.";
RL   Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
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:KFJ04899.1}.
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DR   EMBL; JGZU01000017; KFJ04899.1; -; Genomic_DNA.
DR   EMBL; VULW01000005; MSS13404.1; -; Genomic_DNA.
DR   RefSeq; WP_026642428.1; NZ_VULW01000005.1.
DR   AlphaFoldDB; A0A087EAU8; -.
DR   STRING; 356829.BITS_1417; -.
DR   eggNOG; COG3507; Bacteria.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000029080; Unassembled WGS sequence.
DR   Proteomes; UP000482439; Unassembled WGS sequence.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
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; 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:UP000029080}.
FT   DOMAIN          365..526
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   REGION          412..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        19
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            126
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   533 AA;  57729 MW;  9BAE60060630AECB CRC64;
     MTLFNCKPAK RIASGFHPDP SICEKPDGGY VMVNSSFEFM PGLPVFESED GEHWTKVGHA
     LSRPSQFPYE SMGNSQGIYA PTIRYHDGLY YLIVTNVNVG NMLLTASDPS GEWSDPIWIP
     DWPGIDPSLF FDDDGTVYIC GNESGCVDED GNHEEAGIYL SRLDVTTGEV LDKRKRICGG
     ITGSNPEGPH MLKRGDMYYL MWAEGGTESG HMENIARSNK ADGPYEMYSG NPLITNRSTH
     LTLQAIGHCD CAHFEDERTL MVFHGTRNND EYPAQGWIGR EPYAVWFTWK DGWPQLADQS
     YDCTLNGNGD ALEHDVEWIT PGRDDYGRYS VSPNQGVADS DESVFDIEVS ASGNDFDLPN
     DGAPLIGTRQ TDMDCLFEAA VVPGVSCETA VAGIAAYGND KHVITVSIER GAAKDSESAE
     NAPNKQGGKD STSAEQYTVS AQVNNAGLRS TVGSIAMDGS QPVTLRLLGT NAGYVCSVQT
     ADGLVHELGP VPGKVLSFTN AGGFTGTLLG VFAHGTGQVK FSQVRYQPLM ASR
//
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