ID   IABF2_BACSU             Reviewed;         495 AA.
AC   P94552; B5KLN7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Intracellular exo-alpha-L-arabinofuranosidase 2;
DE            Short=ABF;
DE            EC=3.2.1.55;
DE   AltName: Full=Intracellular arabinan exo-alpha-L-arabinosidase;
DE            Short=Arabinosidase;
GN   Name=abf2; Synonyms=asd, xsa; OrderedLocusNames=BSU28510;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=14973026; DOI=10.1128/jb.186.5.1287-1296.2004;
RA   Raposo M.P., Inacio J.M., Mota L.J., de Sa-Nogueira I.;
RT   "Transcriptional regulation of genes encoding arabinan-degrading enzymes in
RT   Bacillus subtilis.";
RL   J. Bacteriol. 186:1287-1296(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RC   STRAIN=168;
RX   PubMed=18757805; DOI=10.1099/mic.0.2008/018978-0;
RA   Inacio J.M., Correia I.L., de Sa-Nogueira I.;
RT   "Two distinct arabinofuranosidases contribute to arabino-oligosaccharide
RT   degradation in Bacillus subtilis.";
RL   Microbiology 154:2719-2729(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [5]
RP   SEQUENCE REVISION TO 397.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Involved in the degradation of arabinan and is a key enzyme
CC       in the complete degradation of the plant cell wall. Catalyzes the
CC       cleavage of terminal alpha-L-arabinofuranosyl residues in different
CC       hemicellulosic homopolysaccharides (branched and debranched arabinans)
CC       and heteropolysaccharides (arabinoxylans). It is able to hydrolyze the
CC       alpha-(1->5)-glycosidic linkages of linear alpha-(1->5)-L-arabinan
CC       (debranched), sugar beet arabinan (branched) and wheat arabinoxylan.
CC       Moreover, it displays higher activity towards branched arabinan, a
CC       molecule comprising a backbone of alpha-(1->5)-linked L-
CC       arabinofuranosyl residues decorated with alpha-(1->2)-, and alpha-
CC       (1->3)-linked L-arabinofuranosyl units, than towards debranched
CC       arabinan. In addition, arabinoxylan, which has L-arabinofuranose
CC       residues attached to the main chain by alpha-(1->2)- and/or alpha-
CC       (1->3)-glycosidic linkages, is preferred to linear alpha-(1->5)-L-
CC       arabinan. {ECO:0000269|PubMed:18757805}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC         residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC         Evidence={ECO:0000269|PubMed:18757805};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.35 mM for sugar beet arabinan (branched)
CC         {ECO:0000269|PubMed:18757805};
CC         KM=0.42 mM for p-nitrophenyl-alpha-L-arabinofuranoside (pNP-Araf)
CC         {ECO:0000269|PubMed:18757805};
CC         KM=0.5 mM for linear alpha-1,5-L-arabinan
CC         {ECO:0000269|PubMed:18757805};
CC         KM=2.5 mM for arabinotriose {ECO:0000269|PubMed:18757805};
CC         Vmax=311 umol/min/mg enzyme with pNP-Araf as substrate
CC         {ECO:0000269|PubMed:18757805};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:18757805};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:18757805};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000305|PubMed:18757805}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18757805}.
CC   -!- INDUCTION: Transcription is repressed by glucose and by the binding of
CC       AraR to the operon promoter. L-arabinose acts as an inducer by
CC       inhibiting the binding of AraR to the DNA, thus allowing expression of
CC       the gene. {ECO:0000269|PubMed:14973026}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene retain 70% of
CC       arabinofuranosidase activity, and the double mutant abfA/abf2 is
CC       inactive. {ECO:0000269|PubMed:18757805}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR   EMBL; Z75208; CAA99576.1; -; Genomic_DNA.
DR   EMBL; EU073712; ABW70629.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14811.2; -; Genomic_DNA.
DR   PIR; G69734; G69734.
DR   RefSeq; NP_390729.2; NC_000964.3.
DR   RefSeq; WP_004398654.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P94552; -.
DR   SMR; P94552; -.
DR   STRING; 224308.BSU28510; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   PaxDb; 224308-BSU28510; -.
DR   EnsemblBacteria; CAB14811; CAB14811; BSU_28510.
DR   GeneID; 937449; -.
DR   KEGG; bsu:BSU28510; -.
DR   PATRIC; fig|224308.179.peg.3098; -.
DR   eggNOG; COG3534; Bacteria.
DR   InParanoid; P94552; -.
DR   OrthoDB; 9758333at2; -.
DR   PhylomeDB; P94552; -.
DR   BioCyc; BSUB:BSU28510-MONOMER; -.
DR   BioCyc; MetaCyc:BSU28510-MONOMER; -.
DR   SABIO-RK; P94552; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR   PANTHER; PTHR43576:SF2; INTRACELLULAR EXO-ALPHA-L-ARABINOFURANOSIDASE 2; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Disulfide bond; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..495
FT                   /note="Intracellular exo-alpha-L-arabinofuranosidase 2"
FT                   /id="PRO_0000057702"
FT   ACT_SITE        172
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        295
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171..172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            299
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            344
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..176
FT                   /evidence="ECO:0000250"
FT   CONFLICT        44
FT                   /note="D -> N (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="H -> N (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="S -> A (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="K -> T (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203..204
FT                   /note="DI -> EL (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="N -> H (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="E -> D (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340
FT                   /note="A -> T (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="N -> E (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="A -> D (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="M -> T (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="N -> K (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        407
FT                   /note="Q -> H (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="V -> I (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="E -> D (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        468
FT                   /note="R -> S (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="S -> N (in Ref. 2; ABW70629)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   495 AA;  56475 MW;  5D8F939DB55A6397 CRC64;
     MSEHQAVIQT DIAKGTINKN IYGHFAEHLG RGIYEGIWVG TDSDIPNING IRKDVLEALK
     QLHIPVLRWP GGCFADEYHW ANGVGDRKTM LNTHWGGTIE SNEFGTHEFM MLCELLECEP
     YICGNVGSGT VQEMSEWIEY MTFEEGTPMS DWRKQNGREE PWKLKYFGVG NENWGCGGNM
     HPEYYADLYR RFQTYVRNYS GNDIYKIAGG ANVDDFNWTD VLMKKAAGLM DGLSLHYYTI
     PGDFWKGKGS ATEFTEDEWF ITMKKAKYID ELIQKHGTIM DRYDPEQRVG LIIDEWGTWF
     DPEPGTNPGF LYQQNTIRDA LVAASHFHIF HQHCRRVQMA NIAQTVNVLQ AMILTEGERM
     LLTPTYHVFN MFKVHQDASL LATETMSADY EWNGETLPQI SISASKQAEG DINITICNID
     HQNKAEAEIE LRGLHKAADH SGVILTAEKM NAHNTFDDPH HVKPESFRQY TLSKNKLKVK
     LPPMSVVLLT LRADS
//