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Database: UniProt
Entry: A0A098U507_9BURK
LinkDB: A0A098U507_9BURK
Original site: A0A098U507_9BURK 
ID   A0A098U507_9BURK        Unreviewed;       780 AA.
AC   A0A098U507;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:KGF79372.1};
GN   ORFNames=IA69_24725 {ECO:0000313|EMBL:KGF79372.1};
OS   Massilia sp. JS1662.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF79372.1, ECO:0000313|Proteomes:UP000029701};
RN   [1] {ECO:0000313|EMBL:KGF79372.1, ECO:0000313|Proteomes:UP000029701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS1662 {ECO:0000313|EMBL:KGF79372.1,
RC   ECO:0000313|Proteomes:UP000029701};
RA   Fida T.T., Spain J.C.;
RT   "Identification of Arachidin-3 degrading bacteria in the peanut
RT   rhizosphere.";
RL   Submitted (JUL-2014) 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:KGF79372.1}.
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DR   EMBL; JPQD01000034; KGF79372.1; -; Genomic_DNA.
DR   RefSeq; WP_036238385.1; NZ_JPQD01000034.1.
DR   AlphaFoldDB; A0A098U507; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000029701; 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; 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   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   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..780
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001949627"
FT   DOMAIN          37..221
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          263..604
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          612..699
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          717..759
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
SQ   SEQUENCE   780 AA;  86493 MW;  10E0E6E64A5E618E CRC64;
     MRLTLHRTLI ALTSALAFVP AAFAAPLTTL DRNGAWVSVE AYGPNIVHVT IAVDKDEVLK
     GPGYGILKKN ADNAAFRHTA GNDGDTFTSN GMTVHVNAAP PARTPSQPEK YFAPSLAPVG
     LQVKNAKGES ILEMHGWEMS PQTVNGEKTY QVGATFAAGR DEHYYGMGQN QESTGPLDLR
     GRTLDCKHWY DAPTGESVCV PFMVSSKGYG IVWDNPSATR FNAAIHGRTS FQSNVGERVS
     FFVITGKTTD EIYSGYARLT GKTPIPPKAA FGLIQSKARY DSQQEVLRVA NTYRQKKYPL
     DVMVVDWFYW TRMGQMDINP AEFPDPDGMN KQLHDMGMQS IVSIWPRYET AGRYFNELDA
     KGYLLKDKDG KTVDGLPFRS DRTGGLIDAT NPKARQWFWE KSRDNILSHG FDYPWLDETE
     PDLVPDGYFY SIGSGDRYHN LFPLLHVEGF ADNMRTWKPN KRVLILSRAA YLGSQRTGAL
     FWSSDVNATW EALQRQIPTG LNMTASGIAL WGNDIGGWQS IPGTSDGTKT PLVDPSDARD
     VVGQNNDYPE LLTRWFQYGT FLPTLRLHGQ HKHTDIWSFG KQAETIMARY DTLRYQLIPY
     IYSQAKFTHD TGAPFMRALW MDFPNDPNVA NIGTQYMFGP AFLVAPVTEQ GQTEKNVYLP
     AGTDWYNFWT DEKVAGGQWV KVAAPIDQIP VFVKAGSIVP FGADIQSTAT KQAIASVKVY
     PGRDASFNLY DDDGVSYDYE KGKGTTTRLQ WNDGAGKLTA SGGDANLAKN LASIVKVAGK
//
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