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Database: UniProt
Entry: A0A0Q6L2J1_9SPHN
LinkDB: A0A0Q6L2J1_9SPHN
Original site: A0A0Q6L2J1_9SPHN 
ID   A0A0Q6L2J1_9SPHN        Unreviewed;       511 AA.
AC   A0A0Q6L2J1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Trehalase {ECO:0000313|EMBL:KQU61809.1};
GN   ORFNames=ASG67_01100 {ECO:0000313|EMBL:KQU61809.1};
OS   Sphingomonas sp. Leaf339.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU61809.1, ECO:0000313|Proteomes:UP000051371};
RN   [1] {ECO:0000313|EMBL:KQU61809.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU61809.1,
RC   ECO:0000313|Proteomes:UP000051371};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU61809.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU61809.1,
RC   ECO:0000313|Proteomes:UP000051371};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC         glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001576};
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:KQU61809.1}.
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DR   EMBL; LMRS01000001; KQU61809.1; -; Genomic_DNA.
DR   RefSeq; WP_056524105.1; NZ_LMRS01000001.1.
DR   AlphaFoldDB; A0A0Q6L2J1; -.
DR   STRING; 1736343.ASG67_01100; -.
DR   OrthoDB; 106887at2; -.
DR   Proteomes; UP000051371; Unassembled WGS sequence.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   InterPro; IPR018232; Glyco_hydro_37_CS.
DR   PANTHER; PTHR23403; TREHALASE; 1.
DR   PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00928; TREHALASE_2; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051371};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..511
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006282538"
SQ   SEQUENCE   511 AA;  56957 MW;  88239F5A62426163 CRC64;
     MIARLLFAAT AVLTVAATPL SPAQRFGKLY HDVQMRRLFP DGKTFADAVP KRPDSRIVAA
     YRVCKCGTDA TLRRFVLANF TLPEAPITRP QPCRSLTEHI DQLWSQLTRT TTTVPAGSSA
     LTLPRRYVVP GGRFREMYYW DSWFSMLGLP TARRQDLVED MVVDFGSLID RYGHIPNGTR
     TYYLSRSQPP FFYLIAGMSR DAATLATLTR QLRAEHAYWM QGAATLVPGH ESARVVRLPD
     GALLNRYWDD RADARDESYR EDTELANTTP GRPRAELMRD LRAAAESGWD FSSRWLADGR
     SLATIRTTRL VPVDLNSLMV GMEQAIAANC RVLQDMPCAT SFTARVEART QAIRRHLWNG
     RFFADYDLDT GQPNAVATAA MTFPLFTGVA TADQARATAR AFAPFVGEGG VRTTLTASGQ
     QWDDPNGWAP LQWIAIQGLR RYGEQALAAR IRTAWLATVT REYDASGKLL EKYDVVERRP
     GGGGEYPNQD GFGWTNGVTR ALLAEKPDSG R
//
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