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Database: UniProt
Entry: U3U6U4_9ENTR
LinkDB: U3U6U4_9ENTR
Original site: U3U6U4_9ENTR 
ID   U3U6U4_9ENTR            Unreviewed;       470 AA.
AC   U3U6U4;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00015938};
DE            EC=3.2.1.141 {ECO:0000256|ARBA:ARBA00012268};
DE   AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00033284};
DE   AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00032057};
GN   Name=treZ {ECO:0000313|EMBL:BAN99152.1};
GN   ORFNames=E05_43860 {ECO:0000313|EMBL:BAN99152.1};
OS   Plautia stali symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN99152.1, ECO:0000313|Proteomes:UP000016901};
RN   [1] {ECO:0000313|EMBL:BAN99152.1, ECO:0000313|Proteomes:UP000016901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA   Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT   "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT   lipopolysaccharide.";
RL   Microbiol. Res. 167:48-54(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-
CC         [(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-
CC         alpha-D-glucan.; EC=3.2.1.141;
CC         Evidence={ECO:0000256|ARBA:ARBA00034013};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005199}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; AP012551; BAN99152.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3U6U4; -.
DR   KEGG; psts:E05_43860; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_020726_2_0_6; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000016901; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033942; F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd11325; AmyAc_GTHase; 1.
DR   Gene3D; 1.10.10.760; E-set domains of sugar-utilizing enzymes; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR012768; Trehalose_TreZ.
DR   InterPro; IPR044901; Trehalose_TreZ_E-set_sf.
DR   NCBIfam; TIGR02402; trehalose_TreZ; 1.
DR   PANTHER; PTHR43002:SF10; 1,4-ALPHA-GLUCAN BRANCHING ENZYME GLGB; 1.
DR   PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAN99152.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016901}.
FT   DOMAIN          75..417
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   470 AA;  52470 MW;  946E894361BD3CD9 CRC64;
     MQPQQDGWFS LTLRGPGHGS EYHDELADGS TVPDPAARAQ RADVNGPSLV IDPHHYAWQQ
     RDWQGRPWHE TVVYELHIGT FTAEGTFHAA IEKLPALADL GITMSEVLPV SQFGGTRGWG
     YDGVLLYAPH SAYGSPDDFK AFVDAAHALG LSVVLDIVLN HFGPEGNYLP LLAPAFFHEE
     RMTPWGAGIA YDVDAARRYI VEAPLYWLKE FNLDGLRFDA IDQIEDTSSK HVLIEIAERI
     REEIHHRPIH LTTEDSRNVI FLHPRDADCN APLFSGEWND DFHNAIHVFA TGETHAYYQD
     FADVPEKLIA RILTEGFAYQ GELSPQSGQR RGVPSAGQPP VAFVDFIQNH DQVGNRAQGE
     RLISLAGAER TKVLLATLLL SPHIPLLFMG EEYGETNPFL FFTDFHGDLA KAVREGRARE
     FTGHAGHDDT VPDPNAEETF TRSKLDWSKV DHPAGQAWLT LTHQLLALRQ
//
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