ID W8FA72_9BACT Unreviewed; 566 AA.
AC W8FA72;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:AHJ99521.1};
GN ORFNames=Hsw_3926 {ECO:0000313|EMBL:AHJ99521.1};
OS Hymenobacter swuensis DY53.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ99521.1, ECO:0000313|Proteomes:UP000019423};
RN [1] {ECO:0000313|EMBL:AHJ99521.1, ECO:0000313|Proteomes:UP000019423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ99521.1,
RC ECO:0000313|Proteomes:UP000019423};
RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT "Complete genome sequence of ionizing-radiation resistance bacterium
RT Hymenobacter swuensis DY53.";
RL Submitted (JAN-2014) 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; CP007145; AHJ99521.1; -; Genomic_DNA.
DR AlphaFoldDB; W8FA72; -.
DR STRING; 1227739.Hsw_3926; -.
DR KEGG; hsw:Hsw_3926; -.
DR PATRIC; fig|1227739.3.peg.4077; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016508_2_2_10; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000019423; 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; IPR033379; Acid_Pase_AS.
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.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 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:UP000019423};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004908357"
FT DOMAIN 364..555
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 151
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 566 AA; 62722 MW; EF9408D71B52E87D CRC64;
MKVKNTKRSL WLTAALAGAL LGAPAASAQS ITLTNPILTG FYPDPSVVKV GPDYYLVTST
FSYFPGIPVF HSQDLKNWRQ VGNVISRPSQ MNFLGDRMTR GLFAPAIDYH NGTYYLTCTL
IDRKGNFVVT AKNPAGPWSD PIWLPEVKGI DPSLFFDNDK VYVIYNSDPP DNKPLYDGHR
SIKIMELDPV KLQSIGEARM LVNGGVDLSK KPVWIEAPHL LKRNGWYYLY AAEGGTSVNH
TEVVFRAKSV QGPFVPYEHN PILTQRTLPP DRKNPITSAG HAQFVEGPDG QTYAIFLAVR
PYEANYYNTG RETFIAPVVW KDDWPIVNTG PQGVQYSYNA NYREVKQPGA RPQSGNFRYT
LTFEKQLDPA LLFLRTHDST LYSLSKAAGL TLKLRPETCA GLGNPAFIGK RQQHMYCTTE
TELNFTAKSA SEKAGLVVFQ DEKHYYYLCK TLADGKPVLQ LLKSRPEAAE PELLAQAPLK
SATGKVQLRI TAAADAYGFQ FSENAKTWTS LKEKVDGKFL STQVAGGFIG CLIGMYATSS
GQPTTSTAAF QWLKYAGNDP VYTPAK
//