ID B8GCD5_CHLAD Unreviewed; 592 AA.
AC B8GCD5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
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 OrderedLocusNames=Cagg_2092 {ECO:0000313|EMBL:ACL24979.1};
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL24979.1, ECO:0000313|Proteomes:UP000002508};
RN [1] {ECO:0000313|Proteomes:UP000002508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485 {ECO:0000313|Proteomes:UP000002508};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) 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|PIRNR:PIRNR006337}.
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DR EMBL; CP001337; ACL24979.1; -; Genomic_DNA.
DR RefSeq; WP_015940837.1; NC_011831.1.
DR AlphaFoldDB; B8GCD5; -.
DR STRING; 326427.Cagg_2092; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; cag:Cagg_2092; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_020726_2_0_0; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000002508; 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 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; 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; 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 Glycosidase {ECO:0000256|PIRNR:PIRNR006337, ECO:0000313|EMBL:ACL24979.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006337, ECO:0000313|EMBL:ACL24979.1}.
FT DOMAIN 115..460
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 299
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 260..265
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 324..328
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 392..397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 393
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 592 AA; 66620 MW; 7BB7F68B62F09F58 CRC64;
MFNLPQPGAV YRSDGTTAFT LWAPTAATVE LIVLDPKPRT VTMKPIGYDC WHVVTEAPPG
TRYRYRLDGQ RERPDPASRC QPEGVHGPSA VVDHHFDWSD AAWRGVPLTD LVIYELHVGT
FTPEGTFTAI IPHLPILRDL GVTAIELMPV AHFPGQRNWG YDGVYLYAPH TVYGGVKGLK
QLVDAAHAHG IAVILDVVYN HFGPEGNYLW DIAPPAFTDR YRTPWGSAIN YDGPDSDLVR
WLIIENALEW LREYHIDGLR LDATHAIFDV SPYHVLEELA DRVREQAIRL GRPAYLFAEH
PLNDPRFARP KVLGGYGLSG IWSDDFHHAL HSFLTGEQNG YYAGFGSLAQ IATAIERSFV
FAGEYSPHAR RRFGRDPSEL APEQFVVFLQ NHDQVGNRAI GDRLGATLSE AQLRVAAATV
LLSPYTPLIF MGEEYNEPAP FQYFTDHSDP ALITGVREGR KREFAYFLRP GQEVPDPQDP
TTFTRSKLNH ALRTVGRHAA HQAFYRELLR LRRELPGLRQ RPRTRVQGQT IVVEWPRIRL
LLNFGPDPIR IELPVASWQI RLDSGDPPAT ILDGMRVTCS GYSAVLLTTH NE
//
