IABF1_BACSU
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 03-AUG-2022, entry version 127.
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; Firmicutes; 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 AlphaFoldDB; P94531; -.
DR SMR; P94531; -.
DR STRING; 224308.BSU28720; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR PaxDb; P94531; -.
DR PRIDE; P94531; -.
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 OMA; SKYMRGW; -.
DR PhylomeDB; P94531; -.
DR BioCyc; BSUB:BSU28720-MON; -.
DR BioCyc; MetaCyc:BSU28720-MON; -.
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; 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; 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
