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Database: UniProt
Entry: A0A0Q8R659_9BURK
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Original site: A0A0Q8R659_9BURK 
ID   A0A0Q8R659_9BURK        Unreviewed;       987 AA.
AC   A0A0Q8R659;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KRB92417.1};
GN   ORFNames=ASE26_05430 {ECO:0000313|EMBL:KRB92417.1};
OS   Duganella sp. Root198D2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRB92417.1, ECO:0000313|Proteomes:UP000051728};
RN   [1] {ECO:0000313|EMBL:KRB92417.1, ECO:0000313|Proteomes:UP000051728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root198D2 {ECO:0000313|EMBL:KRB92417.1,
RC   ECO:0000313|Proteomes:UP000051728};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB92417.1, ECO:0000313|Proteomes:UP000051728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root198D2 {ECO:0000313|EMBL:KRB92417.1,
RC   ECO:0000313|Proteomes:UP000051728};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRB92417.1}.
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DR   EMBL; LMIC01000023; KRB92417.1; -; Genomic_DNA.
DR   RefSeq; WP_057246687.1; NZ_LMIC01000023.1.
DR   AlphaFoldDB; A0A0Q8R659; -.
DR   Proteomes; UP000051728; 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   Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
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; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 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; 2.
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; 2.
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:KRB92417.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051728};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..987
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006354214"
FT   DOMAIN          683..827
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   987 AA;  109578 MW;  7251DF11DE21D93B CRC64;
     MKHLPETVLA ASLALAAVWG APAHAACKQA PCTKAAAAAG SGLDKNGHSL ALPIAARDGF
     GYVRLQHGVQ FRVGGITKNV IFYGPGTVRV NANLGENHWT SPSIVVVGKP ARVAFELQES
     ADTLVISSAQ LRISIDRKTG ALRFMDGAGR EYTHEAEQPQ SVRAVEISGA PSYEVENRFI
     LKPDEAIFGF GYTDSDAVNR RKQDLLLVQT NLGIIIPVMM SSERYGILWD TYSRMRFQDG
     AEGARLWAES APGGVDYYFM GGRSMDGVVG EYRRLTGAAP MYPKQAFGLF MSKERYPTQQ
     RIVEVAETFR KERFPLDYIV QDWQYWGSDK DGSWSGMTWD PVRFPDPAGM ADSLHGLNLK
     LMVSIWPSVG NDTALARELD QYGLRFEPLH WISQKARVYD AYSPKARQIY FKHAKSGLFD
     KGVDALWMDG TEVEVGSAAW DAGKNEADIK ALGKNALGDF ARYLNPYTLL TTQGTYDGQR
     ATSDKRVFTL TRSAWAGAQR TAAASWSGDI FSSWDTLRKQ VSGGVNVTIT GNPYWTQDTG
     GFFVARDFPG GEKDPAYREL FARWFQYGAF NPIMRVHGTD IEREPYIFKT LDPEVYKSLL
     DTVHLRYRLL PYIYGLSAKV TSDHYTLMRA LPMDFADDKA TYGINDAFMF GPSLLVHPVT
     RPMYRIQPPP PATIPADYLR TPDGQPGLAG QYFEGRNFDT PKGQVIDKVI DHSWPAPPLA
     TIPAGLSRLD DFSARWNGTL EAPEDGEYEI GIEGDDGYRL FLDGALVLQR WENGGKRLAS
     SRQVLRKGQR VKLTLEYYQA TSDRSLRLAW RTPSAIRALA ESRPVSDAGM RTYLPKGTAW
     YDFWSNQRHE GGQAVVREVP LDIVPLYVRA GAILPMGPVL QYATEQPDAP YEIRIYPGAD
     GSFTLYEDDN QTYAYERGQA ARVQLGWNDK AKVLTIGARK GSFPGMVKAR TLNLVLVDPA
     NGKGVGMAQA ARAVRYDGKA MAVRFSQ
//
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