ID   XYND_PAEPO              Reviewed;         635 AA.
AC   P45796;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 121.
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;
OS   Paenibacillus polymyxa (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 /
RC   NCTC 10343 / NRRL B-4317 / VKM B-514;
RX   PubMed=1938968; DOI=10.1128/jb.173.23.7705-7710.1991;
RA   Gosalbes M.J., Perez-Gonzalez J.A., Gonzalez R., Navarro A.;
RT   "Two beta-glycanase genes are clustered in Bacillus polymyxa: molecular
RT   cloning, expression, and sequence analysis of genes encoding a xylanase and
RT   an endo-beta-(1,3)-(1,4)-glucanase.";
RL   J. Bacteriol. 173:7705-7710(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-46, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
RC   STRAIN=CECT 153 / NCTC 4747 / NRRL NRS-1237;
RX   PubMed=8579824; DOI=10.1007/bf00164489;
RA   Morales P., Sendra J.M., Perez-Gonzalez J.A.;
RT   "Purification and characterization of an arabinofuranosidase from Bacillus
RT   polymyxa expressed in Bacillus subtilis.";
RL   Appl. Microbiol. Biotechnol. 44:112-117(1995).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (0.8 ANGSTROMS) OF 505-635 IN COMPLEX WITH
RP   XYLOTRIOSE.
RC   STRAIN=ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 /
RC   NCTC 10343 / NRRL B-4317 / VKM B-514;
RX   PubMed=15242594; DOI=10.1016/j.str.2004.04.022;
RA   Jamal-Talabani S., Boraston A.B., Turkenburg J.P., Tarbouriech N.,
RA   Ducros V.M.-A., Davies G.J.;
RT   "Ab initio structure determination and functional characterization of
RT   CBM36; a new family of calcium-dependent carbohydrate binding modules.";
RL   Structure 12:1177-1187(2004).
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 (By similarity).
CC       Preferres wheat flour xylan over oat spelt xylan as substrate. Does not
CC       display endoxylanase activity. {ECO:0000250,
CC       ECO:0000269|PubMed:8579824}.
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   -!- ACTIVITY REGULATION: Activated by calcium and magnesium. Inhibited by
CC       copper. {ECO:0000269|PubMed:8579824}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:8579824};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:8579824};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: The C-terminal CBM6 domain shows calcium-dependent xylo-
CC       oligosaccharide and xylan binding. It binds, next to the structural
CC       calcium ion, a second calcium ion that, in addition to its coordination
CC       sites on the protein, completes its heptacoordination through
CC       coordination to the bound xylose moiety.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; X57094; CAA40378.1; -; Genomic_DNA.
DR   PIR; S19011; S19011.
DR   RefSeq; WP_019687278.1; NZ_UGSC01000001.1.
DR   PDB; 1UX7; X-ray; 1.50 A; A=516-635.
DR   PDB; 1W0N; X-ray; 0.80 A; A=505-635.
DR   PDBsum; 1UX7; -.
DR   PDBsum; 1W0N; -.
DR   AlphaFoldDB; P45796; -.
DR   SMR; P45796; -.
DR   CAZy; CBM36; Carbohydrate-Binding Module Family 36.
DR   CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   GeneID; 66577481; -.
DR   eggNOG; COG3507; Bacteria.
DR   BRENDA; 3.2.1.8; 683.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P45796; -.
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; cd04078; CBM36_xylanase-like; 1.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd09003; GH43_XynD-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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; 2.
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; 2.
DR   PROSITE; PS51175; CBM6; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Metal-binding; Polysaccharide degradation; Repeat;
KW   Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:8579824"
FT   CHAIN           27..635
FT                   /note="Arabinoxylan arabinofuranohydrolase"
FT                   /id="PRO_0000012202"
FT   DOMAIN          379..508
FT                   /note="CBM6 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          517..634
FT                   /note="CBM6 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q45071"
FT   ACT_SITE        248
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q45071"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         382
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         384
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         503
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         520
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT   BINDING         522
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT   BINDING         539
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT   BINDING         544
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="structural"
FT   BINDING         620
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="structural"
FT   BINDING         624
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="structural"
FT   BINDING         625
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="structural"
FT   BINDING         629
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="structural"
FT   SITE            188
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:0000250|UniProtKB:Q45071"
FT   STRAND          517..520
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   HELIX           521..523
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          524..530
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          532..534
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          536..543
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          549..581
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          584..595
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          597..605
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          609..618
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          620..623
FT                   /evidence="ECO:0007829|PDB:1W0N"
FT   STRAND          626..634
FT                   /evidence="ECO:0007829|PDB:1W0N"
SQ   SEQUENCE   635 AA;  67914 MW;  F9DEC69967323316 CRC64;
     MIRKCLVLFL SFALLLSVFP MLNVDAANRP LAKIPGNSNP LMDHKLGADP YSLVYDGRVY
     IFMSSDTYVY NKDGSIKEND FSALDRIQVI SSTDMVNWTD HGTIPVAGAN NKNSGRGIAK
     WASNSWAPAV AHKKINGRDK FFLYFANGGA GIGVLTADTP IGPWTDPLGK ALVTHSTPGM
     AGVTWLFDPA VLVDDDGTGY LYSGGGIPNE SDPASIANPK TARVIKLGAD MTSVIGSATT
     IDAPYLFEDS GIHKYNGKYY YSYCINFAGT HPQQYPAGEI GYMVSDNPMG PFTYKGHFLK
     NPYTFFGVGG NNHHAVFNFK NEWYVVYHAQ TVSKAQIGAG KGYRSPHINK LVHKEDGSIS
     EVQGNMTGIA QLSNMNPYTR VEAETIAWQA GVTTEPTQAS GGPISNLNVT NIHNGDWIAV
     GKADFGSAGA KTFKANVATN VGGNIEVRLD SETGPLVGSL KVPSTGGMQT WREVETTINN
     ATGVHNIYLV FTGSGSGNLL NLDAWQFTPN TGGNTITKVE AENMKIGGTY AGKISAPFDG
     VALYANADYV SYSQYFANST HNISVRGASS NAGTAKVDLV IGGVTVGSFN FTGKTPTVQT
     LSNITHATGD QEIKLALTSD DGTWDAYVDF IEFSL
//