ID   XYND_BACSU              Reviewed;         513 AA.
AC   Q45071;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Arabinoxylan arabinofuranohydrolase;
DE            Short=AXH;
DE            EC=3.2.1.55;
DE   AltName: Full=AXH-m2,3;
DE            Short=AXH-m23;
DE   AltName: Full=Alpha-L-arabinofuranosidase;
DE            Short=AF;
DE   Flags: Precursor;
GN   Name=xynD; OrderedLocusNames=BSU18160;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
RP   PROTEIN SEQUENCE OF 27-37, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA   Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT   "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT   dimensional protein electrophoretic study.";
RL   Microbiology 146:65-75(2000).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=17426966; DOI=10.1007/s00253-007-0956-2;
RA   Bourgois T.M., Van Craeyveld V., Van Campenhout S., Courtin C.M.,
RA   Delcour J.A., Robben J., Volckaert G.;
RT   "Recombinant expression and characterization of XynD from Bacillus subtilis
RT   subsp. subtilis ATCC 6051: a GH 43 arabinoxylan arabinofuranohydrolase.";
RL   Appl. Microbiol. Biotechnol. 75:1309-1317(2007).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 27-513 IN COMPLEXES WITH
RP   XYLOTRIOSE; XYLOTETRAOSE; ARABINOXYLO-OLIGOSACCHARIDES AND CELLOTETRAOSE,
RP   AND ACTIVE SITE.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=18980579; DOI=10.1042/bj20081256;
RA   Vandermarliere E., Bourgois T.M., Winn M.D., van Campenhout S.,
RA   Volckaert G., Delcour J.A., Strelkov S.V., Rabijns A., Courtin C.M.;
RT   "Structural analysis of a glycoside hydrolase family 43 arabinoxylan
RT   arabinofuranohydrolase in complex with xylotetraose reveals a different
RT   binding mechanism compared with other members of the same family.";
RL   Biochem. J. 418:39-47(2009).
CC   -!- FUNCTION: Cleaves arabinose units from O-2- or O-3-monosubstituted
CC       xylose residues, thereby assisting in arabinoxylan (AX) and short-chain
CC       arabinoxylo-oligosaccharide (AXOS) degradation. Is more active on wheat
CC       bran AXOS than on wheat water-extractable AX and rye water-extractable
CC       AX. Does not display endoxylanase, xylosidase or arabinanase activity.
CC       {ECO:0000269|PubMed:17426966}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.6. Stable from pH 4.4 to 7.6.
CC         {ECO:0000269|PubMed:17426966};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. Thermostable for 40 min
CC         from 4 to 45 degrees Celsius. {ECO:0000269|PubMed:17426966};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10658653}.
CC   -!- DOMAIN: The CBM6 domain lost its carbohydrate binding capacity.
CC   -!- MASS SPECTROMETRY: Mass=52080; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17426966};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB13699.1; -; Genomic_DNA.
DR   PIR; H69735; H69735.
DR   RefSeq; NP_389698.1; NC_000964.3.
DR   RefSeq; WP_003245027.1; NZ_JNCM01000035.1.
DR   PDB; 3C7E; X-ray; 2.00 A; A=27-513.
DR   PDB; 3C7F; X-ray; 1.55 A; A=27-513.
DR   PDB; 3C7G; X-ray; 2.02 A; A=27-513.
DR   PDB; 3C7H; X-ray; 2.00 A; A=27-513.
DR   PDB; 3C7O; X-ray; 1.80 A; A=27-513.
DR   PDBsum; 3C7E; -.
DR   PDBsum; 3C7F; -.
DR   PDBsum; 3C7G; -.
DR   PDBsum; 3C7H; -.
DR   PDBsum; 3C7O; -.
DR   AlphaFoldDB; Q45071; -.
DR   SMR; Q45071; -.
DR   STRING; 224308.BSU18160; -.
DR   CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   PaxDb; 224308-BSU18160; -.
DR   EnsemblBacteria; CAB13699; CAB13699; BSU_18160.
DR   GeneID; 936433; -.
DR   KEGG; bsu:BSU18160; -.
DR   PATRIC; fig|224308.179.peg.1980; -.
DR   eggNOG; COG3507; Bacteria.
DR   InParanoid; Q45071; -.
DR   OrthoDB; 9801455at2; -.
DR   PhylomeDB; Q45071; -.
DR   BioCyc; BSUB:BSU18160-MONOMER; -.
DR   BioCyc; MetaCyc:BSU18160-MONOMER; -.
DR   BRENDA; 3.2.1.55; 658.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; Q45071; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd09003; GH43_XynD-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51175; CBM6; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Metal-binding; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:10658653"
FT   CHAIN           27..513
FT                   /note="Arabinoxylan arabinofuranohydrolase"
FT                   /id="PRO_0000360828"
FT   DOMAIN          382..511
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   ACT_SITE        50
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:18980579"
FT   ACT_SITE        251
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:18980579"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:18980579"
FT   BINDING         385
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:18980579"
FT   BINDING         387
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:18980579"
FT   BINDING         409
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:18980579"
FT   BINDING         410
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:18980579"
FT   BINDING         506
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:18980579"
FT   SITE            189
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:18980579"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          49..56
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          59..65
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          87..105
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:3C7G"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          127..136
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          139..148
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          153..160
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          200..205
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   HELIX           216..220
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          225..230
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          234..244
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          249..258
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          261..268
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          270..272
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          282..290
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          296..302
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   HELIX           305..309
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          317..322
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          325..333
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   HELIX           334..340
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          348..353
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          388..394
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          396..399
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          410..413
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          420..427
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   TURN            429..431
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          433..441
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          446..454
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          459..465
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          475..480
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          486..495
FT                   /evidence="ECO:0007829|PDB:3C7F"
FT   STRAND          497..500
FT                   /evidence="ECO:0007829|PDB:3C7O"
FT   STRAND          504..512
FT                   /evidence="ECO:0007829|PDB:3C7F"
SQ   SEQUENCE   513 AA;  54498 MW;  1EBC94AB6CE1490F CRC64;
     MRKKCSVCLW ILVLLLSCLS GKSAYAATST TIAKHIGNSN PLIDHHLGAD PVALTYNGRV
     YIYMSSDDYE YNSNGTIKDN SFANLNRVFV ISSADMVNWT DHGAIPVAGA NGANGGRGIA
     KWAGASWAPS IAVKKINGKD KFFLYFANSG GGIGVLTADS PIGPWTDPIG KPLVTPSTPG
     MSGVVWLFDP AVFVDDDGTG YLYAGGGVPG VSNPTQGQWA NPKTARVIKL GPDMTSVVGS
     ASTIDAPFMF EDSGLHKYNG TYYYSYCINF GGTHPADKPP GEIGYMTSSS PMGPFTYRGH
     FLKNPGAFFG GGGNNHHAVF NFKNEWYVVY HAQTVSSALF GAGKGYRSPH INKLVHNADG
     SIQEVAANYA GVTQISNLNP YNRVEAETFA WNGRILTEKS TAPGGPVNNQ HVTSIQNGDW
     IAVGNADFGA GGARSFKANV ASTLGGKIEV RLDSADGKLV GTLNVPSTGG AQTWREIETA
     VSGATGVHKV FFVFTGTGTG NLFNFDYWQF TQR
//