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Database: UniProt
Entry: J3BXA4_FLASC
LinkDB: J3BXA4_FLASC
Original site: J3BXA4_FLASC 
ID   J3BXA4_FLASC            Unreviewed;       931 AA.
AC   J3BXA4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Family 31 glycosyl hydrolase, alpha-glucosidase {ECO:0000313|EMBL:EJL59629.1};
GN   ORFNames=PMI10_04048 {ECO:0000313|EMBL:EJL59629.1};
OS   Flavobacterium sp. (strain CF136).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1144313 {ECO:0000313|EMBL:EJL59629.1, ECO:0000313|Proteomes:UP000007287};
RN   [1] {ECO:0000313|EMBL:EJL59629.1, ECO:0000313|Proteomes:UP000007287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF136 {ECO:0000313|EMBL:EJL59629.1,
RC   ECO:0000313|Proteomes:UP000007287};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL59629.1}.
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DR   EMBL; AKJZ01000101; EJL59629.1; -; Genomic_DNA.
DR   AlphaFoldDB; J3BXA4; -.
DR   STRING; 1144313.PMI10_04048; -.
DR   PATRIC; fig|1144313.4.peg.4011; -.
DR   eggNOG; COG1501; Bacteria.
DR   Proteomes; UP000007287; 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; 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, ECO:0000313|EMBL:EJL59629.1}.
FT   DOMAIN          202..342
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   931 AA;  107556 MW;  7387C513F6D851E5 CRC64;
     MIDDGVVVNI KQKNQTDTRK VRLQVLRDEL IHITATPDKE FPKDSTLIIV PGIKNTPFTV
     DNSHKDSIML VTSRLKVIVS KLDGGVNFKD KDGKLILAEK KGGGKTFTPI EVEGTKGFSV
     RQIFNSPADE AFHGLGQHQA DEFNYKSKSE ELFQYNTKVS VPFIVSNKNY GLLWDSYSLS
     RFGDSRPYKQ LNSVFKLYDK KGNQGSLTGT YTSKDNGVET LVRSEESIFF EDIKSIKNLP
     KNFPLKNASV TYEGEIEAPE SGDFKFTLYY AGYVKVYLDN KLVVPERWRT AWNPNSYKFS
     MQLQEGKRVP LRIEWQPNGG TSYCGLRALT PQQADEKDNQ VWWSEMSKKL DYYFVYGSNA
     DEVIKGYRTL TGKSQIMPKW AMGYWQSRER YKTQDEILAN LKEFRKRKIP IDNIVLDWNY
     WEENEWGSHE FDKKRFPDPQ GMVDSIHAMN GKMMISVWPK FYKTTEHFKE FDKKGWMYQQ
     AIKDSVRDWV GPGYVGSFYD AYSGGARKLF WKQIYDNLYP LGIDAWWMDA SEPNVLDCTD
     MDYRKALCGP TALGTSTEYF NTYALMNAEA IYDGQRSVAT NKRVFLLTRS GFAGLQRYST
     ATWSGDIATR WEDMKAQISA GLNFAVSGIP YWTMDIGGFC VEDRYVSGQQ QYDKNGQENK
     DYKEWRELNT RWFQFGAFAP LYRAHGQFPY REPWNIAPEG HPAYTSIVYY TNLRYRLMPY
     IYTMAGMTYF NDYTIMRPLF MDFPADKKVE NISNQFMFGP AFMVCPVYSY EARERNVYFP
     TGSNWYDFYT GNYITGGKQV SVDAPYEHIP LFIKEGSIIP VGPELQYTGE KKADKIVLYV
     YKGKDGSFTL YEDEDNNYNY ESGKYANISF TYNNTSNTLT IGERKGQFDG MLKNRTFTIV
     TVSKDKPKAF NYDADGQNIS YDGKEQIVTL K
//
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