ID   IABF1_BACSU             Reviewed;         500 AA.
AC   P94531; O05096;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Intracellular exo-alpha-(1->5)-L-arabinofuranosidase 1;
DE            Short=ABF;
DE            EC=3.2.1.55;
DE   AltName: Full=Intracellular arabinan exo-alpha-(1->5)-L-arabinosidase;
DE            Short=Arabinosidase;
GN   Name=abfA; OrderedLocusNames=BSU28720;
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=9084180; DOI=10.1099/00221287-143-3-957;
RA   Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H.;
RT   "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence,
RT   genetic organization and expression.";
RL   Microbiology 143:957-969(1997).
RN   [2]
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   [3]
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   [4]
RP   SEQUENCE REVISION TO 114.
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).
RN   [5]
RP   TRANSCRIPTIONAL REGULATION.
RX   PubMed=10417639; DOI=10.1046/j.1365-2958.1999.01484.x;
RA   Mota L.J., Tavares P., Sa-Nogueira I.M.G.;
RT   "Mode of action of AraR, the key regulator of L-arabinose metabolism in
RT   Bacillus subtilis.";
RL   Mol. Microbiol. 33:476-489(1999).
RN   [6]
RP   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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE, AND SUBUNIT.
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).
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-(1->5)-arabinofuranosyl bonds in different
CC       hemicellulosic homopolysaccharides (branched and debranched arabinans).
CC       It acts preferentially on arabinotriose, arabinobiose and linear alpha-
CC       (1->5)-L-arabinan, and is much less effective on branched sugar beet
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=0.36 mM for linear alpha-1,5-L-arabinan (at pH 6.6 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:18757805};
CC         KM=0.49 mM for p-nitrophenyl-alpha-L-arabinofuranoside (pNP-Araf) (at
CC         pH 6.6 and 37 degrees Celsius) {ECO:0000269|PubMed:18757805};
CC         KM=0.78 mM for arabinobiose (at pH 6.6 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:18757805};
CC         KM=1.1 mM for arabinotriose (at pH 6.6 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:18757805};
CC         KM=4.4 mM for sugar beet arabinan (branched) (at pH 6.6 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:18757805};
CC         Vmax=317 umol/min/mg enzyme with pNP-Araf as substrate (at pH 6.6 and
CC         37 degrees Celsius) {ECO:0000269|PubMed:18757805};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:18757805};
CC       Temperature dependence:
CC         Optimum temperature is 50 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 (Probable). {ECO:0000305|PubMed:10417639,
CC       ECO:0000305|PubMed:14973026}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene retain 38% 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; X89810; CAA61937.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99595.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14832.2; -; Genomic_DNA.
DR   PIR; C69580; C69580.
DR   RefSeq; NP_390750.2; NC_000964.3.
DR   RefSeq; WP_004398747.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P94531; -.
DR   SMR; P94531; -.
DR   STRING; 224308.BSU28720; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   PaxDb; 224308-BSU28720; -.
DR   EnsemblBacteria; CAB14832; CAB14832; BSU_28720.
DR   GeneID; 937509; -.
DR   KEGG; bsu:BSU28720; -.
DR   PATRIC; fig|224308.179.peg.3120; -.
DR   eggNOG; COG3534; Bacteria.
DR   InParanoid; P94531; -.
DR   OrthoDB; 9758333at2; -.
DR   PhylomeDB; P94531; -.
DR   BioCyc; BSUB:BSU28720-MONOMER; -.
DR   BioCyc; MetaCyc:BSU28720-MONOMER; -.
DR   BRENDA; 3.2.1.55; 658.
DR   SABIO-RK; P94531; -.
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:SF3; ALPHA-L-ARABINOFURANOSIDASE C; 1.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 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; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..500
FT                   /note="Intracellular exo-alpha-(1->5)-L-arabinofuranosidase
FT                   1"
FT                   /id="PRO_0000057701"
FT   ACT_SITE        173
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        292
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         172..173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            296
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            349
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        114
FT                   /note="A -> P (in Ref. 2; CAA99595)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  57034 MW;  3EEA8F8ADA3D705A CRC64;
     MKKARMIVDK EYKIGEVDKR IYGSFIEHMG RAVYEGIYEP DHPEADEDGF RKDVQSLIKE
     LQVPIIRYPG GNFLSGYNWE DGVGPVENRP RRLDLAWQTT ETNEVGTNEF LSWAKKVNTE
     VNMAVNLGTR GIDAARNLVE YCNHPKGSYW SDLRRSHGYE QPYGIKTWCL GNEMDGPWQI
     GHKTADEYGR LAAETAKVMK WVDPSIELVA CGSSNSGMPT FIDWEAKVLE HTYEHVDYIS
     LHTYYGNRDN NLPNYLARSM DLDHFIKSVA ATCDYVKAKT RSKKTINLSL DEWNVWYHSN
     EADKKVEPWI TARPILEDIY NFEDALLVGS LLITMLQHAD RVKIACLAQL VNVIAPIMTE
     KGGEAWRQPI FYPYMHASVY GRGESLKPLI SSPKYDCSDF TDVPYVDAAV VYSEEEETLT
     IFAVNKAEDQ METEISLRGF ESYQIAEHIV LEHQDIKATN QHNRKNVVPH SNGSSSVSEN
     GLTAHFTPLS WNVIRLKKQS
//