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
//