ID   A0A1V9ENY8_9BACT        Unreviewed;       950 AA.
AC   A0A1V9ENY8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   SubName: Full=Alpha-xylosidase {ECO:0000313|EMBL:OQP47752.1};
GN   ORFNames=A4H97_30780 {ECO:0000313|EMBL:OQP47752.1};
OS   Niastella yeongjuensis.
OC   Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Niastella.
OX   NCBI_TaxID=354355 {ECO:0000313|EMBL:OQP47752.1, ECO:0000313|Proteomes:UP000192610};
RN   [1] {ECO:0000313|Proteomes:UP000192610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17621 {ECO:0000313|Proteomes:UP000192610};
RA   Chen L., Zhuang W., Wang G.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQP47752.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LVXG01000022; OQP47752.1; -; Genomic_DNA.
DR   RefSeq; WP_081200760.1; NZ_FOCZ01000019.1.
DR   AlphaFoldDB; A0A1V9ENY8; -.
DR   STRING; 354355.SAMN05660816_06349; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000192610; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd14752; GH31_N; 1.
DR   CDD; cd06591; GH31_xylosidase_XylS; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR017853; GH.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR051816; Glycosyl_Hydrolase_31.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR   PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   Pfam; PF07691; PA14; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192610}.
FT   DOMAIN          234..380
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   950 AA;  108393 MW;  0811FD99A8909BD5 CRC64;
     MKTPFKRLLV GIVALVLIGL IVIISSQRPA FNDYIRLEDG VIVKVEKPRA GGAGNVKLQV
     VNDKIIHVTA AAGDSFAAAP SLMTGDQKGH PEWKLEEQGD QLVLQTASLR AIVSRLTGQV
     QFTDLKGKAI LKETAITGKS FVAKGLENRS TYTITQSFES PVGEAWYGLG QHQQGLFNYR
     GTQVSLLQQN TEVAIPFMVS NRNYGLLWDN YSISRFGDCR PFEPLHSLSL TGTDGAAGVL
     TATYFSGKKQ DSVFLKRGEK EIDYEFIQSL QKLPQGFPLQ KGRVQWEGNV SSGFSGEHSF
     LFSSGGYLKY WFNGKLLVDK WRQCWNPITT LVKVDLEKGK QYPVKIEWVP DGGESYVAMK
     WLGPIPENNR NTFSFWSEAG DNINYYFVYG NNMDEVISGY RELTGNATML PRWALGFWQS
     RERYKTQNEL LSVVKEFRER KIPLDNIVLD WFYWKPDQWG SHEFDASRFP NAEAMIKDLH
     EKYNTHFMIS VWPKFYTGTK NYDLFNEKGW LYKQNVLNNQ KDWVGYVSTF YDAYNPQARE
     LFWKLMNEKL YSKGVDAWWM DATEPDILSN TSIDERKKLI GPVARGSSTS YFNDFAVENA
     KGVYEGQRRT NSLDRVFILT RSAYAGLQKY GAVTWSGDIG ARWNDLQNQV AGGINFSLSG
     LPYWTTDIGG FAVEKRFEKA TGNDLDEWRE LMTRWYQFGA FCPIFRVHGQ YPYREIFNVA
     PANHPAYKSM LYYDQLRYRL MPYIYTLAGQ VYHHDYTMMR ALVMDFAADK AVENIGDQYM
     FGPSLLINPV YEYKARSRWV YLPAGTGWYN FYTGAYQAGG LRINATAGYE QIPLFVKEGS
     IIPLGPDMQY TSEKTADPIT LYVYTGKDAT FTLYEDEGTN YNYEKGFFTN IPITWNEAAK
     TLTIGKRTGN YAGMLNQRSF NIVWITPARH DNKPAATVTY LGEQVTVTGK
//