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
//