ID W0I3C6_9GAMM Unreviewed; 598 AA.
AC W0I3C6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:AHF79262.1};
GN ORFNames=Sant_P0217 {ECO:0000313|EMBL:AHF79262.1};
OS Sodalis praecaptivus.
OG Plasmid pHS1 {ECO:0000313|EMBL:AHF79262.1,
OG ECO:0000313|Proteomes:UP000019028}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF79262.1, ECO:0000313|Proteomes:UP000019028};
RN [1] {ECO:0000313|EMBL:AHF79262.1, ECO:0000313|Proteomes:UP000019028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AHF79262.1,
RC ECO:0000313|Proteomes:UP000019028};
RC PLASMID=Plasmid pHS1 {ECO:0000313|Proteomes:UP000019028};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(2014).
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|PIRNR:PIRNR006337}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006570; AHF79262.1; -; Genomic_DNA.
DR RefSeq; WP_025424391.1; NZ_CP006570.1.
DR AlphaFoldDB; W0I3C6; -.
DR KEGG; sod:Sant_P0217; -.
DR PATRIC; fig|1239307.3.peg.4758; -.
DR HOGENOM; CLU_020726_0_0_6; -.
DR OrthoDB; 3236218at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000019028; Plasmid pHS1.
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; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
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 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 Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006337, ECO:0000313|EMBL:AHF79262.1};
KW Plasmid {ECO:0000313|EMBL:AHF79262.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019028}.
FT DOMAIN 92..512
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 261
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 296
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT SITE 393
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 598 AA; 66154 MW; 6846D3BECC56D81A CRC64;
MESRSFSKSW GAEYVAEGQV RFRLWASGQD SVALRLSGED TAMTPCGAGW FEALASDVAP
GAEYHFVLAD GTAVPDPASR AQKADVNGPS LVIDPTRYAW RNTSWRGRPW EETVVYEMHV
GTFTPEGTFQ AAIEKLPYLA ALGITMIELL PLAQFGGNRG WGYDGVLLYA PHSAYGTPED
VKAFVDAAHG HGLSVVLDIV LNHFGPEGNY LPLLAPDFFN NKRSTPWGAG IAYDIEAARR
YIVEAPLYWL QEYYLDGLRF DAIDQIEDNA AKHVLIEIAE RIRAEITHRP IHLTTEDSRN
VICLHPREAN GAVPLYSGEW NDDFHNAIHV FATGETHAYY QDFANEPEQH IARVWAEGFA
YQGGVSQQTG KKRGVKSAGQ PPVAFVDFIQ NHDQVGNRAQ GERLITLAGV ERTKILLIAL
LFSPHIPLLF MGEEYGETRP FLFFTDFHGD LAKAVREGRA KEFAGHAGHE GEKVPDPNAR
QTFERSKLDW DKLRSHEGNE WLTLTRTLLA LRQKYIVPLL ASSGGEVGKV LRTAEGFIAV
SWRLPKGTLS LALNIGATPQ PLPYLQGETI YAWPKVTDEA DGLPPNGLLV RLASGDKP
//
