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Database: UniProt
Entry: D6XWN8_BACIE
LinkDB: D6XWN8_BACIE
Original site: D6XWN8_BACIE 
ID   D6XWN8_BACIE            Unreviewed;       320 AA.
AC   D6XWN8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:ADH97880.1};
DE            EC=3.2.1.55 {ECO:0000313|EMBL:ADH97880.1};
GN   OrderedLocusNames=Bsel_0340 {ECO:0000313|EMBL:ADH97880.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Salisediminibacterium.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97880.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97880.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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; CP001791; ADH97880.1; -; Genomic_DNA.
DR   RefSeq; WP_013171309.1; NC_014219.1.
DR   AlphaFoldDB; D6XWN8; -.
DR   STRING; 439292.Bsel_0340; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   KEGG; bse:Bsel_0340; -.
DR   eggNOG; COG3940; Bacteria.
DR   HOGENOM; CLU_009397_2_1_9; -.
DR   OrthoDB; 177947at2; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18817; GH43f_LbAraf43-like; 1.
DR   InterPro; IPR016828; Alpha-L-arabinofuranosidase.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   PIRSF; PIRSF025414; Alpha-L-arabinofuranosidase; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:ADH97880.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:ADH97880.1}.
FT   ACT_SITE        17
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            136
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   320 AA;  37058 MW;  86FA28CAE6CB546F CRC64;
     MTQSYDYKNP VIEQRADPWM YKHTDGYYYF TASVPEYDRI EVRRAKTIEG LKGATPAVVW
     RKYDEGPLSA NIWAPEIHYI DGAWYIYFAA ARTTETDNGL FDHRMYALAC QSNNPVEGTW
     EEKGQVKSKW ESFCLDATVF EHKGDHYYVW AQKDPDIEGN SNMYIDKMVN PWTLKGDQVM
     ISQPEYEWEK VGFYVNEGAA VIKRNGKIFM TFSGSATDHN YRMGLLYADE ESDLLNPSSW
     HKLDKPVFAT SEENGQYGPG HNSFTTSEDG EKDLLVYHAR NYKEIDGDPL YDPNRHTRVQ
     AFEWDENGFP VFEKPVPDAD
//
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