ID A0A0B8T2H6_9SPHI Unreviewed; 605 AA.
AC A0A0B8T2H6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=DI53_3265 {ECO:0000313|EMBL:KGE13048.1};
OS Sphingobacterium deserti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE13048.1, ECO:0000313|Proteomes:UP000031802};
RN [1] {ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RA Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C.,
RA Zhang W.;
RT "Whole-Genome optical mapping and complete genome sequence of
RT Sphingobacterium deserti sp. nov., a new spaces isolated from desert in the
RT west of China.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGE13048.1, ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RX PubMed=25830331;
RA Teng C., Zhou Z., Molnar I., Li X., Tang R., Chen M., Wang L., Su S.,
RA Zhang W., Lin M.;
RT "Whole-Genome Optical Mapping and Finished Genome Sequence of
RT Sphingobacterium deserti sp. nov., a New Species Isolated from the Western
RT Desert of China.";
RL PLoS ONE 10:E0122254-E0122254(2015).
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:KGE13048.1}.
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DR EMBL; JJMU01000061; KGE13048.1; -; Genomic_DNA.
DR RefSeq; WP_037501963.1; NZ_JJMU01000061.1.
DR AlphaFoldDB; A0A0B8T2H6; -.
DR STRING; 1229276.DI53_3265; -.
DR PATRIC; fig|1229276.3.peg.3374; -.
DR eggNOG; COG0296; Bacteria.
DR OrthoDB; 9761875at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000031802; 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; 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; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031802}.
FT DOMAIN 115..459
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 298
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 259..264
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 323..327
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 391..396
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 392
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 605 AA; 68019 MW; 12C459080D015D0D CRC64;
MFETGVNNIG VSLRNGTAHI NVWAPDAKSV ICRVEKRGAD IPLAIGKYGY WYAESDALKE
GDSYRFQIDG EPYPDPASLA QPEGVHGASQ IVDLQYPWRD ENYHPPALDK LIIYELHVGT
FTASHDFSGV IERIPHLLKL GINAIEIMPV AQFPGDRNWG YDGVFLFAVQ HSYGGAKGLQ
QLVDACHEAG IAVILDVVYN HFGPEGNYLP NFGPYFTEKY STPWGKAINY DDAYSHGVRD
FVLANIRMWF EDFHIDGLRL DAVHAIKDFS PKHILQEVRQ LTDDIIAARK KPHYLIVECD
LNDRRYLDPL QNNAFAMDAQ WIDEFHHALR VAAGEEKKGY YKDFNGLEDL AKAYEKAYVF
DGNYSTHREK FFGTSAAGLS GERFIVFSQN HDQVGNRMLG ERSAALYSKS VQRLMAMAVI
LSPYTPMLFM GEEWGTEKPF QYFVSHGDEE LIEAVREGRK AEFADFQSEG TPPDPQATAT
FNTCVLDWNE VEADTQQKML NYYTKLIKLR RELQASGSFG REQLAVEHDK EKDSILLTMG
SGKNQMLAIL NFSAETQSYE VDGQWKIMLD SNDRQWAGDS NMGDAVDSSV TVASTSGILL
ALVSA
//
