ID S9TB39_9RALS Unreviewed; 649 AA.
AC S9TB39;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ORFNames=C404_02510 {ECO:0000313|EMBL:EPX99440.1};
OS Ralstonia sp. AU12-08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1235457 {ECO:0000313|EMBL:EPX99440.1, ECO:0000313|Proteomes:UP000015343};
RN [1] {ECO:0000313|EMBL:EPX99440.1, ECO:0000313|Proteomes:UP000015343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU12-08 {ECO:0000313|EMBL:EPX99440.1,
RC ECO:0000313|Proteomes:UP000015343};
RX PubMed=24503988;
RA Zhang L., Morrison M., Rickard C.M.;
RT "Draft Genome Sequence of Ralstonia pickettii AU12-08, Isolated from an
RT Intravascular Catheter in Australia.";
RL Genome Announc. 2:e00027-14(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|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR006337}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPX99440.1}.
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DR EMBL; ASZV01000005; EPX99440.1; -; Genomic_DNA.
DR AlphaFoldDB; S9TB39; -.
DR PATRIC; fig|1235457.3.peg.510; -.
DR eggNOG; COG0296; Bacteria.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000015343; Unassembled WGS sequence.
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 149..519
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 327
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT SITE 435
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 649 AA; 70985 MW; 6C5DFCA445DB0002 CRC64;
MTAAAVPTPT SHPLHATQHA ACFTHDLPFG ATCLGPERTR FRLWAPDATE AWVEIDAGHE
RNGGNGGNTI RMDAEPDGWY AAIAPIGAGL GYRYRVTDRN GVTLTVPDPA ARAQWQDLYG
PSLVVDPARY LWRHADWQGR PWHETVLYEL HVGAMGGAMG GFRGVRARLP ELARLGVTAI
ELMPLAEFPG ARNWGYDGVL PFAPDASYGS PDELKALIDT AHGLGLMVFL DVVYNHFGPD
GNYLAHYARR FFHEGTHTPW GAAFDFREPV VREFFIQNAL MWLMEYRFDG LRLDAVQAIG
ERDWLGELAA RVRQAVEPGR YVHLVLENEN NAASLLRGAT TLAAGPADHA AATAGAFEAQ
WNDDGHHALH ALLTGEHEAY YAAYADAPAK RLARVLQEGF CYQGEPSPLH NGAPRGEPSG
TLPPTAFVLY LQNHDQVGNR PLGERLTRLA HPEALHAAQA LLLLCPQIPL LFMGEEWGSL
RPFHYFTSHH GALADAVREG RRREFGRFSA FADPLKRERI PDPNDERTYQ ASWPGEAELT
NPEHLAWLNR THRLLALRQA QIVPRLVGAR ALDAVPLGTT GALARWRLGD GSVLTLAVNL
GAQPVSVPTA LAGNPSDLLY ESRDGAAATL ATHHVPAHAC IALLTLPAD
//
