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Database: UniProt
Entry: A6EDC6_9SPHI
LinkDB: A6EDC6_9SPHI
Original site: A6EDC6_9SPHI 
ID   A6EDC6_9SPHI            Unreviewed;       619 AA.
AC   A6EDC6;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   08-NOV-2023, entry version 78.
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=PBAL39_25540 {ECO:0000313|EMBL:EDM36694.1};
OS   Pedobacter sp. BAL39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM36694.1, ECO:0000313|Proteomes:UP000003664};
RN   [1] {ECO:0000313|EMBL:EDM36694.1, ECO:0000313|Proteomes:UP000003664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL39 {ECO:0000313|EMBL:EDM36694.1,
RC   ECO:0000313|Proteomes:UP000003664};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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}.
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:EDM36694.1}.
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DR   EMBL; ABCM01000007; EDM36694.1; -; Genomic_DNA.
DR   RefSeq; WP_008241597.1; NZ_ABCM01000007.1.
DR   AlphaFoldDB; A6EDC6; -.
DR   STRING; 391596.PBAL39_25540; -.
DR   eggNOG; COG0296; Bacteria.
DR   OrthoDB; 9761875at2; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000003664; 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.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
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:UP000003664}.
FT   DOMAIN          124..468
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        270
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT   ACT_SITE        307
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT   BINDING         268..273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   BINDING         332..336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   BINDING         400..405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   SITE            401
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ   SEQUENCE   619 AA;  70365 MW;  AD0D16BDBACE665C CRC64;
     MSTIDLSKRR IGVNFSEQQA EVLVWAPQAS GLSLLIAQDP DQPLPLTQQE HGYWYLETDQ
     LKPGDAYQLL IHQQQGERLK RPDPASLSQH EGVHGASTAY DLSAFQWTDA TWKGIPLEAY
     ILYELHVGTF SAAGDFAGLE HQLDHLVSLG ITAIELMPVA QFPGNRNWGY DGVYPFAVQS
     SYGGPQGLQH LVGCCHAKGL AVVLDVVYNH MGPEGNYFDD FGPYFTEKYH TPWGNAINFD
     DEWSDGVRHY FIENVLMWFR DFHIDALRMD AVHAIKDFGS LHILEEIKSY TRKLSVKTGR
     QHYLIVESDL NDPKYIDPEH HYGYGMDAQW IDEFHHALRV TAGQEPTGYY SDFNGLAHLE
     KSFHDAYVYD GIYSPHRKKT FGRPATENPG KQFVVFSQNH DQVGNRMLGE RSANLLDFSM
     LKVLAGAVLC SPYLPMLFMG EEWAESNPFL YFVSHGDESL VTAVREGRKA EFASFHASGA
     APDPQSEETF MRSKLQWELL KKGDHACLFS FYQSLIAIRK KSAAIYELNR KHLKTETVPD
     ARCLMLHRWH EEQHILCFLN FSDDEQQMRM PSEKPYWKKL MDSNAPEWGG NKASPQSLEA
     GNLLQVPASS FLLYTSKHV
//
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