ID K4IP53_BIFAP Unreviewed; 309 AA.
AC K4IP53;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Endo-1,4-beta-xylanase {ECO:0000313|EMBL:AFU70816.1};
DE EC=3.2.1.55 {ECO:0000313|EMBL:AFU70816.1};
GN OrderedLocusNames=BAST_0219 {ECO:0000313|EMBL:AFU70816.1};
OS Bifidobacterium asteroides (strain PRL2011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU70816.1, ECO:0000313|Proteomes:UP000007006};
RN [1] {ECO:0000313|EMBL:AFU70816.1, ECO:0000313|Proteomes:UP000007006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRL2011 {ECO:0000313|EMBL:AFU70816.1,
RC ECO:0000313|Proteomes:UP000007006};
RX PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA Ventura M.;
RT "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT colonization of the insect gut.";
RL PLoS ONE 7:E44229-E44229(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP003325; AFU70816.1; -; Genomic_DNA.
DR RefSeq; WP_015021255.1; NC_018720.1.
DR AlphaFoldDB; K4IP53; -.
DR STRING; 1147128.BAST_0219; -.
DR GeneID; 41009501; -.
DR KEGG; bast:BAST_0219; -.
DR PATRIC; fig|1147128.3.peg.231; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_2_11; -.
DR Proteomes; UP000007006; Chromosome.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd09004; GH43_bXyl-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:AFU70816.1};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:AFU70816.1}.
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 185
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 138
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 309 AA; 34747 MW; 0B77A0FC98760C5D CRC64;
MEEFASAHQG SKGTGLASNP LHRYCADPDL VMIGDRWYLY CTEDGLAGWS SHAFYVYESG
DLCHWTRRKI LDLDQVPWWH GRQGAWAPCL LVRQGRCILY FVADGQIGQA VAPGPTGPFR
VAQEPFIARG DYDCVPIDPS VFVDDDDIPY LLWGNGRAYM ARLSSDGMCL EDGSVRSAVP
DNFREAITVC RRGDTYYASW SENDTRDPNY RIRWSNAPSL DGPWTAPQIL VKADYDKGIL
ATGHHCITRV PGRDDWIVAY HRFARDGQGD GCHREIVFAP LDFADDGAMV QVRPQVGSYW
YPARDQVTP
//
