ID   XYNC_CELJU              Reviewed;         619 AA.
AC   P23031; B3PEH9;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Alpha-L-arabinofuranosidase C;
DE            EC=3.2.1.55;
DE   AltName: Full=Xylanase C;
DE   Flags: Precursor;
GN   Name=xynC; Synonyms=abf62A; OrderedLocusNames=CJA_3281;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-46.
RX   PubMed=2125205; DOI=10.1042/bj2720369;
RA   Kellett L.E., Poole D.M., Ferreira L.M.A., Durrant A.J., Hazlewood G.P.,
RA   Gilbert H.J.;
RT   "Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp.
RT   cellulosa contain identical cellulose-binding domains and are encoded by
RT   adjacent genes.";
RL   Biochem. J. 272:369-376(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
CC   -!- FUNCTION: Xylanase C contributes to hydrolyse hemicellulose, the major
CC       component of plant cell-walls.
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   -!- PATHWAY: Glycan metabolism; hemicellulose degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Acts only on high MW substrates, in which arabinose is
CC       linked to a polymeric backbone.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA38390.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X54523; CAA38390.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP000934; ACE85320.1; -; Genomic_DNA.
DR   RefSeq; WP_012488857.1; NC_010995.1.
DR   AlphaFoldDB; P23031; -.
DR   SMR; P23031; -.
DR   STRING; 498211.CJA_3281; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH62; Glycoside Hydrolase Family 62.
DR   EnsemblBacteria; ACE85320; ACE85320; CJA_3281.
DR   KEGG; cja:CJA_3281; -.
DR   eggNOG; COG3509; Bacteria.
DR   eggNOG; COG3693; Bacteria.
DR   HOGENOM; CLU_418515_0_0_6; -.
DR   OMA; WYLITQW; -.
DR   OrthoDB; 1622507at2; -.
DR   UniPathway; UPA00697; -.
DR   Proteomes; UP000001036; 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:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   CDD; cd08987; GH62; 1.
DR   Gene3D; 2.115.10.20; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR005193; GH62_arabinosidase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR40631; PTHR40631; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF03664; Glyco_hydro_62; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS51175; CBM6; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000269|PubMed:2125205"
FT   CHAIN           38..619
FT                   /note="Alpha-L-arabinofuranosidase C"
FT                   /id="PRO_0000008033"
FT   DOMAIN          38..136
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   DOMAIN          163..289
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   REGION          300..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        39..133
FT                   /evidence="ECO:0000250"
FT   CONFLICT        556..590
FT                   /note="NNNVEWSTGKWADGISHGELIRSGHDEKMTVDPCN -> MMFCFTMASSLKV
FT                   YTCY (in Ref. 1; CAA38390)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   619 AA;  66440 MW;  9CA48261A2D0FD0F CRC64;
     MINHNKTPNI LAKVFKRTCG LVSTGAALAI LSQAASAACT YTIDSEWSTG FTANITLKND
     TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW NGSIAPGQSI SFGLQGEKNG
     STAERPTVTG AACNSATTSS VASSSSTPTT SSSSASSVAS ALLLQEAQAG FCRVDGTIDN
     NHTGFTGSGF ANTNNAQGAA VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN
     YTVSLPTTGA WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS
     VSSSSSVQSS SSSSSTPSQT CELKAPLRWT STGPLISPKN PGWISIKDPS IVKYNDTYHV
     YATYYDTAYR SMYTSFTDWN TAQQAPHISM NGSRVGNTVA PQVFYFRPHN KWYLITQWAG
     AYATTDDIRN PNWSAKQKLL QGEPNGALDF WVICNDTHCY LYFSRDDGVL YVSKTTLANF
     PNFSGYSIVM EDHRGNGNSY LFEAANVYKL DGQNRYLLMV EAYISGPRFF RSWTATSLDG
     PWTPLADTEA NPFAGNNNVE WSTGKWADGI SHGELIRSGH DEKMTVDPCN LEFLYQGASG
     PGSTYNTIPY KLGLLRLKK