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Database: UniProt
Entry: A0A0Q8BTA9_9RHIZ
LinkDB: A0A0Q8BTA9_9RHIZ
Original site: A0A0Q8BTA9_9RHIZ 
ID   A0A0Q8BTA9_9RHIZ        Unreviewed;       593 AA.
AC   A0A0Q8BTA9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   10-OCT-2018, entry version 18.
DE   RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
DE            Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE            EC=3.2.1.141 {ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
GN   ORFNames=ASD74_00075 {ECO:0000313|EMBL:KRA04960.1};
OS   Rhizobium sp. Root564.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1736563 {ECO:0000313|EMBL:KRA04960.1, ECO:0000313|Proteomes:UP000052141};
RN   [1] {ECO:0000313|EMBL:KRA04960.1, ECO:0000313|Proteomes:UP000052141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root564 {ECO:0000313|EMBL:KRA04960.1,
RC   ECO:0000313|Proteomes:UP000052141};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA04960.1, ECO:0000313|Proteomes:UP000052141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root564 {ECO:0000313|EMBL:KRA04960.1,
RC   ECO:0000313|Proteomes:UP000052141};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-alpha-D-glucosidic
CC       linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to
CC       yield trehalose and (1->4)-alpha-D-glucan.
CC       {ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRSR:PIRSR006337-1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|PIRNR:PIRNR006337, ECO:0000256|SAAS:SAAS00964676}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRA04960.1}.
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DR   EMBL; LMGN01000001; KRA04960.1; -; Genomic_DNA.
DR   RefSeq; WP_062423502.1; NZ_LMGN01000001.1.
DR   EnsemblBacteria; KRA04960; KRA04960; ASD74_00075.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000052141; 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   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR022567; DUF3459.
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   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF11941; DUF3459; 1.
DR   PIRSF; PIRSF006337; Trehalose_TreZ; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR02402; trehalose_TreZ; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000052141};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:KRA04960.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052141}.
FT   DOMAIN      114    458       Aamy. {ECO:0000259|SMART:SM00642}.
FT   REGION      321    325       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR006337-2}.
FT   ACT_SITE    260    260       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    295    295       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   BINDING     369    369       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006337-2}.
FT   SITE        391    391       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   593 AA;  67256 MW;  35CAA72077AE41B3 CRC64;
     MVYAFDFGPA ISDQDIEFRL WAPLHDEVLL NIEGATPEAM KRDDEGWHRL RKPRAEAALR
     YSFTLPDGLE VPDPASRFQP RDVHGQSEVV DLSSFPWKSA NWHGRPWEEI IIYELHIGTF
     SDEGTFQGAI AHLDHLRDLG VTAIQIMPVA DFPGGYNWGY DGVMPYAPDS SYGRPEDLMA
     LVDAAHERGL CVFLDVVYNH FGPDGNYMPN YAPLFSPHHE NPWGQGLNYD DEQSEHVREF
     IIQNAVYWVT QFRFDGLRLD AVHAIVDDSD EHLLSELARR VRAAVTDRHI HLIVENEEND
     SDLLSRDEEG RPERFTAQWN DDIHHVLHIA ATGETFGYYK AYSGDDDKIG RALAEGFAFQ
     GEHMPYRDEE RGKPSAHLPP TAFISFIQNH DQIGNRALGD RMQTYAPEAA LKAITAIYLL
     APQIPMLFMG EEWGSRDPFR YFCDFNEDLN QKVRDGRREE LSRLPGFDGE NVPDPTAKET
     FIASKLDWSK VEGDKATELL GFYKTLLDLR KRHIVPLLTK IVPDTTRYDV RDNLVTVDWG
     MEDGATLRLT ANLSEKNGET ETDATTGGEL FSLGTISAKA ISPWAVHWTL QPA
//
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