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Database: UniProt
Entry: A0A087M3Q3_9RHIZ
LinkDB: A0A087M3Q3_9RHIZ
Original site: A0A087M3Q3_9RHIZ 
ID   A0A087M3Q3_9RHIZ        Unreviewed;       598 AA.
AC   A0A087M3Q3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   12-SEP-2018, entry version 22.
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=JP75_08215 {ECO:0000313|EMBL:KFL31506.1};
OS   Devosia riboflavina.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Hyphomicrobiaceae; Devosia.
OX   NCBI_TaxID=46914 {ECO:0000313|EMBL:KFL31506.1, ECO:0000313|Proteomes:UP000028981};
RN   [1] {ECO:0000313|EMBL:KFL31506.1, ECO:0000313|Proteomes:UP000028981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO13584 {ECO:0000313|EMBL:KFL31506.1,
RC   ECO:0000313|Proteomes:UP000028981};
RA   Hassan Y.I., Lepp D., Zhou T.;
RL   Submitted (AUG-2014) 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   -!- 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:KFL31506.1}.
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DR   EMBL; JQGC01000006; KFL31506.1; -; Genomic_DNA.
DR   RefSeq; WP_035081938.1; NZ_JQGC01000006.1.
DR   EnsemblBacteria; KFL31506; KFL31506; JP75_08215.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000028981; 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:UP000028981};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028981}.
FT   DOMAIN      111    454       Aamy. {ECO:0000259|SMART:SM00642}.
FT   REGION      318    322       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR006337-2}.
FT   ACT_SITE    257    257       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    292    292       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   BINDING     367    367       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006337-2}.
FT   SITE        391    391       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   598 AA;  67643 MW;  7985E6B5746358EE CRC64;
     MRFGAEVRKG STRFKLWAPK CKTLQLKLKG RRSLIEMDAI DDGWFRVDVE GVGAGALYKY
     VLPDGSAIPD PTSRHQPDDI AGFSEVIDPQ AFGWTDRGWR GRPWEEAIIY ELHIGTFTEE
     GTFAAAITKL DHLVALGVTA IQIMPVGEFY GKFNWGYDGA MWFAPSSNYG RPDDLKALID
     AAHRRSMMVF LDVVYNHFGP HGNYLPAIAP IFTKKHQSPW GEALNFDGRG ANVVRELVVE
     NALYWMSEFN LDGLRFDSVH TMVDDSSSHI LELLSARIRA SRPHRHTHLI IENSDNQEVW
     LRRNSDSEPV HYTAQWNDDV HHLLHAAATG ENTGYYADFD DSDGRSGRLG RALAEGFAYQ
     GEVKPHEAMK RGEPSGGLPA TSFVVYMQDH DQIGNRIKGD RITRVAHDDA VKALIAIYLL
     CPQIPMLFQG EEWASARPFP FFSDVPAEVR DAVRNGRQDD LRSTPEHEDQ DRPEVEEAVD
     PTSIRTFTSA KLDWSNLRKQ PHSNWLKHYR SLIDLRKMEI VPRLVGQQGF AGRYEPLGVK
     SVLVSWRMGD GSILRLYANL TDETQHDVQP IIGRKVYLHG FAEEGRLGPW SVLWTVEV
//
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