IABF2_BACSU
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 03-AUG-2022, entry version 122.
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; Firmicutes; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; P94552; -.
DR PRIDE; P94552; -.
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 OMA; EPYICGN; -.
DR PhylomeDB; P94552; -.
DR BioCyc; BSUB:BSU28510-MON; -.
DR BioCyc; MetaCyc:BSU28510-MON; -.
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; 2.60.40.1180; -; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; SSF51445; 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
