ID   D3HN54_LEGLN            Unreviewed;       512 AA.
AC   D3HN54;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Alpha,alpha-trehalase {ECO:0000313|EMBL:CBJ13904.1};
DE            EC=3.2.1.28 {ECO:0000313|EMBL:CBJ13904.1};
GN   Name=treF {ECO:0000313|EMBL:CBJ13904.1};
GN   OrderedLocusNames=LLO_3440 {ECO:0000313|EMBL:CBJ13904.1};
OS   Legionella longbeachae serogroup 1 (strain NSW150).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ13904.1, ECO:0000313|Proteomes:UP000001060};
RN   [1] {ECO:0000313|EMBL:CBJ13904.1, ECO:0000313|Proteomes:UP000001060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSW150 {ECO:0000313|EMBL:CBJ13904.1,
RC   ECO:0000313|Proteomes:UP000001060};
RX   PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA   Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA   Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA   Etienne J., Hartland E., Buchrieser C.;
RT   "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT   unique strategies to cause Legionnaires' disease.";
RL   PLoS Genet. 6:E1000851-E1000851(2010).
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};
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DR   EMBL; FN650140; CBJ13904.1; -; Genomic_DNA.
DR   RefSeq; WP_012979567.1; NC_013861.1.
DR   AlphaFoldDB; D3HN54; -.
DR   STRING; 661367.LLO_3440; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   KEGG; llo:LLO_3440; -.
DR   eggNOG; COG1626; Bacteria.
DR   HOGENOM; CLU_006451_3_3_6; -.
DR   OrthoDB; 106887at2; -.
DR   Proteomes; UP000001060; Chromosome.
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:SF6; CYTOSOLIC NEUTRAL TREHALASE-RELATED; 1.
DR   PANTHER; PTHR23403; 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, ECO:0000313|EMBL:CBJ13904.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBJ13904.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001060}.
SQ   SEQUENCE   512 AA;  59997 MW;  234D92CA3770F6EE CRC64;
     MDIQLLKIYK GQYVYCLLIS LVLFKNAFSS AREHLDLNVV QYIDKSWDVL VREDWLQSSF
     DPKLSTNESI VYLPQSENIE KIKSKNIKIS SKVQFEHLPK DPTSIKRHGL LYLPYPYVVP
     GGRFNEMYAW DSFFIELGLL ENRRFHLAKY MVDNLIYEVI NYGMILNANR TYYLGRTQPP
     LLTEMVLAYY EKDPNNIWLK STLPAVEKLY QFWTSPPHAI PNIGLSRYYS SGEGQTPEES
     PLYYKKVLNY FNTHPVTDYD KALFYDNKKN QLTNYFYIAD RTIRESGFDI TAKYGPFGAA
     ILDYAPVDLN VLLYQMECDI QRIYELLGNN KEANKWQRRA KNRANHINFY LWDEATGYYL
     DYNFKKKERK YYPFATTFYP IWAGVASKEQ AAAVVKHLPD LLMKGGIVTS TNYSGLQWDA
     PFGWAPMQYF AVFGLDRYGY NQFAREVATK FIHTINRGFQ KDHAIFEKYD VNIISTQTDN
     KIKYSYTSNE IGFGWTNGVY LILSKYLEES ET
//