ID   A0A1M3HBQ8_9SPHI        Unreviewed;       944 AA.
AC   A0A1M3HBQ8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Alpha-xylosidase {ECO:0000313|EMBL:OJW55952.1};
GN   ORFNames=BGO55_04900 {ECO:0000313|EMBL:OJW55952.1};
OS   Sphingobacteriales bacterium 50-39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW55952.1, ECO:0000313|Proteomes:UP000184242};
RN   [1] {ECO:0000313|EMBL:OJW55952.1, ECO:0000313|Proteomes:UP000184242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=50-39 {ECO:0000313|EMBL:OJW55952.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJW55952.1}.
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; MKTZ01000015; OJW55952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3HBQ8; -.
DR   STRING; 1895841.BGO55_04900; -.
DR   Proteomes; UP000184242; 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; 2.
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; 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; IPR017853; Glycoside_hydrolase_SF.
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, INTESTINAL-LIKE; 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}.
FT   DOMAIN          227..370
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   944 AA;  107165 MW;  137B35B6307CBD49 CRC64;
     MKLRLVLSSL LTVAIVNVLL AAPPSYKTIP DGLIIFTDSL VTGTSNAVRL EVIADNIIRV
     TAAPAKEIVP LQSLVTLDKK RTDVFWEVIP SKESLTLRTK KLTAIVDLKT GAVSFRDPRG
     GKILEEKRPL GRSFQASVVD GKRCYKLAQT FQTTPGDAWY GLGQHQDGIY NYKGQQVTLF
     QNNTEVGIPF LISCRNYGVL WDNYSLTAAG DTRPLHDLSA LQLFSKTGDQ GWLTASYAND
     KRKSQEVVTE RAEGNIDMPF LGDSKIQLPP SFTPATGMVT WEGSVASYLS GVHQFRFTFG
     GSLKVWLDGK LVLDHWRKAW NPAPAMVPIQ LEKGAKVPVR IEWIPEGGES YLSLKWQEPL
     TPAEQNSFGF SSEAGQQIDY YFIYGRNMDG VIAGYRELTG KAPIVPKWAL GFWQSRERYK
     TQDEIINTID EFRKREIPID NIVLDWSYWK EAAWGSQEFD ETRFPSPDSM IDVLHKKYHT
     HLMISVWPKF YEGISSYDEF DKKGWLYKRN IADRQRDWIG KGYVSTFYDA FNADARKGFW
     DLIHKKIYSK GIDAWWMDAS EPDILSNVSP EKRKLQMTPT ALGSAAEYLN AYPLQNAKGI
     YEGQRADDPD RRVFLLTRSG FAGSQRYAAA IWSGDIGSTW RDMKNQIAAG VNFSMSGLPY
     WTMDIGGFVV PEKFEKPNAE SLEEWRELNT RWYQFGAFVP LFRAHGQFPY REIFNIAPPD
     HPAYQSILYY DKLRYRLLPY LYSLAGMVWH DDYTMMRGLV MDFGNDTAVR DIADEFMLGP
     SLLVNPVCTY KAQQREVYLP AGQGWYDLYS GKIVDGGQRI TAEAPYQRMP VYVKEGTILP
     MGPDLQYTGE RPADTITLYV YTGRDADFTL YEDEGTNYNY EKGSFSTIAL HYNEAARMLT
     IGERNGSFAG ALLQRTFRIE CIGGKSKPTA VVTYTGHEKR IDLK
//