ID   XYNC_BACIU              Reviewed;         423 AA.
AC   Q6YK37;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Glucuronoxylanase XynC;
DE            EC=3.2.1.136;
DE   AltName: Full=Endoxylanase XynC;
DE   AltName: Full=Glucuronoxylan xylanohydrolase;
DE   Flags: Precursor;
GN   Name=xynC; Synonyms=ynfF;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AU195;
RX   PubMed=15109718; DOI=10.1111/j.1574-6968.2004.tb09511.x;
RA   Moyne A.-L., Cleveland T.E., Tuzun S.;
RT   "Molecular characterization and analysis of the operon encoding the
RT   antifungal lipopeptide bacillomycin D.";
RL   FEMS Microbiol. Lett. 234:43-49(2004).
CC   -!- FUNCTION: Catalyzes the depolymerization of methylglucuronoxylan
CC       (MeGAXn). It cleaves the beta-1,4-xylosidic bond penultimate to that
CC       linking carbon one of the xylose residue substituted with alpha-1,2-
CC       linked 4-O-methyl-D-glucuronate (MeGA) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosyl links in some
CC         glucuronoarabinoxylans.; EC=3.2.1.136;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN07016.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY137375; AAN07016.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q6YK37; -.
DR   SMR; Q6YK37; -.
DR   CAZy; GH30; Glycoside Hydrolase Family 30.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR   GO; GO:0033940; F:glucuronoarabinoxylan endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR033452; GH30_C.
DR   InterPro; IPR001139; Glyco_hydro_30.
DR   InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11069; PTHR11069; 1.
DR   Pfam; PF02055; Glyco_hydro_30; 1.
DR   Pfam; PF17189; Glyco_hydro_30C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..423
FT                   /note="Glucuronoxylanase XynC"
FT                   /id="PRO_0000278647"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   423 AA;  47840 MW;  3B4C45E656C18EDA CRC64;
     MMSSVKKTIC VLLVCFTMMS VMLLGPGVTE VSAASDAKVN ISADRQVIRG FGGMNHPAWI
     GDLTAAQRET AFGNGQNQLG FSVLRIHVDE NRNNWYKEVE TAKSAIKHGA IVFASPWNPP
     NDMVETFNHN GDTSAKRLRY DKYAAYAQHL NDFVNFMKSN GVNLYAISMQ NEPDYAHEWT
     WWTPQEILRF MRENAGSINA RVIAPESFQY LKNISDPILN DPQALRNMDI LGTHLYGTQV
     SQFPYPLFKQ KGGGKELWMT EVYYPNSDNN SADRWPEALG VSEHIHHSMV EGDFQAYVWW
     YIRRSYGPMK EDGMISKRGY NMAHFSKFVR PGYVRIDATK NPEPNVYVSA YKGDNKVVIV
     AINKNNTGVN QNFVLQNGTA SQVSRWITSS SSNLQPGTDL KVTDNHFWAH LPAQSVTTFV
     VKR