ID A0A0S4IDL9_9PSED Unreviewed; 582 AA.
AC A0A0S4IDL9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00015938, ECO:0000256|PIRNR:PIRNR006337};
DE Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE EC=3.2.1.141 {ECO:0000256|ARBA:ARBA00012268, ECO:0000256|PIRNR:PIRNR006337};
DE AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00033284, ECO:0000256|PIRNR:PIRNR006337};
DE AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00032057, ECO:0000256|PIRNR:PIRNR006337};
GN Name=treZ {ECO:0000313|EMBL:CRN07796.1};
GN ORFNames=PYEL_36430 {ECO:0000313|EMBL:CRN07796.1};
OS Pseudomonas sp. URMO17WK12:I11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1283291 {ECO:0000313|EMBL:CRN07796.1, ECO:0000313|Proteomes:UP000062067};
RN [1] {ECO:0000313|Proteomes:UP000062067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Falquet L., Falquet L.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|PIRNR:PIRNR006337};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005199, ECO:0000256|PIRNR:PIRNR006337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRSR:PIRSR006337-1}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR006337}.
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DR EMBL; LN865164; CRN07796.1; -; Genomic_DNA.
DR RefSeq; WP_059183842.1; NZ_LN865164.1.
DR AlphaFoldDB; A0A0S4IDL9; -.
DR PATRIC; fig|1283291.5.peg.3588; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000062067; Chromosome 1.
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 CDD; cd02853; E_set_MTHase_like_N; 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; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
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; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF11941; DUF3459; 1.
DR PIRSF; PIRSF006337; Trehalose_TreZ; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR006337};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006337}.
FT DOMAIN 107..438
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 286
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT SITE 375
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 582 AA; 64871 MW; EF1FC298B46AD260 CRC64;
MQRHGAHVED ATSARFALWA PDARSVSLEL QHQDAVDLVP DDDDDGWFIG TAPAKPGDLY
RYCINGELRV ADPASRFQPE GVHGPSQVVD LAGYTWQHPW QGRPWHEAVI QELHVGVLGG
YEGVSSHLHR IASTGITAIE LMPISQFPGT RNWGYDGVLP YAAQHNYGTP EQLCSLVDQA
HGHGLMVMLD VVYNHFGPDG NFLHEYASSF FREDRQTPWG AAIDFRRPEV REYFIQNALM
WICDYRIDGL RLDAVHAIDQ PDFLKELAKR VREAVEPGRH VWLVLENEHN QAFLLEQGFD
AQWNDDGHNA LHVLLTDETE GYYEDYKDDP IGKLARCLGE GFVFQGQLNR HGEPRGEPSG
HLPPSAFVLF LQNHDQIGNR AMGERLTRLT SPAALRAATG LLLLSPMIPL LFMGDDDGSR
APFLFFTDFH DELADAVREG RRGEFEHFAA FADPEKRARI PDPNAEQTFH ASRPDPQDVI
AGWHGLYQQL LTTRRQHLVP RLPGTRSLGA EVLADKALTA RWQLGDGSTL RIDLNLGDQA
QHLAAAPAGT CLFDSGDKAH AGSTLSPFSC VVTLLPPNQE MP
//
