EABN1_BACSU
ID EABN1_BACSU Reviewed; 323 AA.
AC P94522; Q5MPF4; Q795W7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Extracellular endo-alpha-(1->5)-L-arabinanase 1;
DE Short=ABN;
DE EC=3.2.1.99;
DE AltName: Full=Endo-1,5-alpha-L-arabinanase;
DE Flags: Precursor;
GN Name=abnA; OrderedLocusNames=BSU28810;
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], PROTEIN SEQUENCE OF 33-37, FUNCTION,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-215, DISRUPTION PHENOTYPE,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=168;
RX PubMed=15556708; DOI=10.1016/j.femsle.2004.10.003;
RA Leal T.F., de Sa-Nogueira I.;
RT "Purification, characterization and functional analysis of an endo-
RT arabinanase (AbnA) from Bacillus subtilis.";
RL FEMS Microbiol. Lett. 241:41-48(2004).
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 172 AND C-TERMINUS.
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 FUNCTION, DISRUPTION PHENOTYPE, 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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 31-323 IN COMPLEX WITH CALCIUM
RP IONS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-43;
RP ASP-44; TRP-104; PHE-124; ASP-163; PHE-181; TRP-182 AND GLU-215, COFACTOR,
RP AND SUBSTRATE SPECIFICITY.
RX PubMed=15708971; DOI=10.1073/pnas.0500051102;
RA Proctor M.R., Taylor E.J., Nurizzo D., Turkenburg J.P., Lloyd R.M.,
RA Vardakou M., Davies G.J., Gilbert H.J.;
RT "Tailored catalysts for plant cell-wall degradation: redesigning the
RT exo/endo preference of Cellvibrio japonicus arabinanase 43A.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2697-2702(2005).
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 internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear
CC 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays
CC no activity against heavily substituted arabinans or a range of other
CC polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p-
CC nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is
CC progressively reduced as alpha-(1->5)-chains become shorter or more
CC highly substituted. {ECO:0000269|PubMed:14973026,
CC ECO:0000269|PubMed:15556708, ECO:0000269|PubMed:15708971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC (1->5)-arabinans.; EC=3.2.1.99;
CC Evidence={ECO:0000269|PubMed:15556708};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 mM for arabinotetraose (at 27 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:15556708, ECO:0000269|PubMed:15708971};
CC KM=5.92 mM for linear 1,5-alpha-L-arabinan (at 37 degrees Celsius and
CC pH 6.6) {ECO:0000269|PubMed:15556708, ECO:0000269|PubMed:15708971};
CC Vmax=1.31 mmol/min/mg enzyme (at 37 degrees Celsius and pH 6.6)
CC {ECO:0000269|PubMed:15556708, ECO:0000269|PubMed:15708971};
CC pH dependence:
CC Optimum pH is 6.0. At pH 4.0 the arabinosidase retains about 8% of
CC activity. {ECO:0000269|PubMed:15556708, ECO:0000269|PubMed:15708971};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. At 80 degrees Celsius
CC retains about 2% of activity. {ECO:0000269|PubMed:15556708,
CC ECO:0000269|PubMed:15708971};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15556708}.
CC -!- INDUCTION: Induced by arabinose and arabina,n and repressed by glucose.
CC {ECO:0000269|PubMed:14973026}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene retains about 40% of the
CC capacity to hydrolyze linear arabinan compared to the wild-type.
CC {ECO:0000269|PubMed:14973026, ECO:0000269|PubMed:15556708}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA99586.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z75208; CAA99586.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY669857; AAV87172.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14841.2; -; Genomic_DNA.
DR PIR; E69580; E69580.
DR RefSeq; NP_390759.2; NC_000964.3.
DR PDB; 1UV4; X-ray; 1.50 A; A=31-323.
DR PDBsum; 1UV4; -.
DR AlphaFoldDB; P94522; -.
DR SMR; P94522; -.
DR STRING; 224308.BSU28810; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR PaxDb; P94522; -.
DR PRIDE; P94522; -.
DR EnsemblBacteria; CAB14841; CAB14841; BSU_28810.
DR GeneID; 937430; -.
DR KEGG; bsu:BSU28810; -.
DR PATRIC; fig|224308.179.peg.3129; -.
DR eggNOG; COG3507; Bacteria.
DR InParanoid; P94522; -.
DR OMA; RYDNGWP; -.
DR PhylomeDB; P94522; -.
DR BioCyc; BSUB:BSU28810-MON; -.
DR BioCyc; MetaCyc:BSU28810-MON; -.
DR SABIO-RK; P94522; -.
DR UniPathway; UPA00667; -.
DR EvolutionaryTrace; P94522; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:15556708"
FT CHAIN 33..323
FT /note="Extracellular endo-alpha-(1->5)-L-arabinanase 1"
FT /id="PRO_0000360437"
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15708971"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15708971"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160..163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 180..182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT SITE 163
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:0000305|PubMed:15708971"
FT MUTAGEN 43
FT /note="H->A: Decrease in binding affinity."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 44
FT /note="D->A: Loss of arabinanase activity."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 104
FT /note="W->A: Significantly less active (10000-fold) than
FT the wild-type arabinanase against both linear arabinan and
FT arabinooligosaccharides."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 124
FT /note="F->A: Increase in binding affinity."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 163
FT /note="D->A: Loss of arabinanase activity."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 181
FT /note="F->A: Significantly less active than the wild-type
FT arabinanase against both linear arabinan (50-fold) and the
FT arabinooligosaccharides (1000-fold)."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 182
FT /note="W->A: Same binding affinity as wild-type."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 215
FT /note="E->A: Loss of arabinanase activity."
FT /evidence="ECO:0000269|PubMed:15556708,
FT ECO:0000269|PubMed:15708971"
FT CONFLICT 172
FT /note="G -> D (in Ref. 1; CAA99586)"
FT /evidence="ECO:0000305"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 64..77
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1UV4"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:1UV4"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:1UV4"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:1UV4"
FT TURN 208..212
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:1UV4"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 278..289
FT /evidence="ECO:0007829|PDB:1UV4"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:1UV4"
FT TURN 301..305
FT /evidence="ECO:0007829|PDB:1UV4"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1UV4"
SQ SEQUENCE 323 AA; 35446 MW; 0105FB280E83BC69 CRC64;
MKKKKTWKRF LHFSSAALAA GLIFTSAAPA EAAFWGASNE LLHDPTMIKE GSSWYALGTG
LTEERGLRVL KSSDAKNWTV QKSIFTTPLS WWSNYVPNYG QNQWAPDIQY YNGKYWLYYS
VSSFGSNTSA IGLASSTSIS SGGWKDEGLV IRSTSSNNYN AIDPELTFDK DGNPWLAFGS
FWSGIKLTKL DKSTMKPTGS LYSIAARPNN GGALEAPTLT YQNGYYYLMV SFDKCCDGVN
STYKIAYGRS KSITGPYLDK SGKSMLEGGG TILDSGNDQW KGPGGQDIVN GNILVRHAYD
ANDNGIPKLL INDLNWSSGW PSY
