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Database: UniProt
Entry: A0A0J7JQ46_9BURK
LinkDB: A0A0J7JQ46_9BURK
Original site: A0A0J7JQ46_9BURK 
ID   A0A0J7JQ46_9BURK        Unreviewed;       629 AA.
AC   A0A0J7JQ46;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-APR-2018, entry version 17.
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=BPMI_02310c {ECO:0000313|EMBL:KMQ80352.1};
OS   Candidatus Burkholderia pumila.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1090375 {ECO:0000313|EMBL:KMQ80352.1};
RN   [1] {ECO:0000313|EMBL:KMQ80352.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot3 {ECO:0000313|EMBL:KMQ80352.1};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-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:KMQ80352.1}.
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DR   EMBL; LELG01000103; KMQ80352.1; -; Genomic_DNA.
DR   EnsemblBacteria; KMQ80352; KMQ80352; BPMI_02310c.
DR   PATRIC; fig|1090375.4.peg.232; -.
DR   UniPathway; UPA00299; -.
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; 2.
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   Glycosidase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:KMQ80352.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:KMQ80352.1}.
FT   DOMAIN      110    463       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    276    276       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    309    309       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        400    400       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   629 AA;  70853 MW;  8047296FF884F1E5 CRC64;
     MSERPIDPHR HQHAYCLPFG AHLTGSKGES SCTHFRFWAP SRDKVQVELQ RTPGAEPELV
     DMQAAGDGWF EAEADAGAGT LYLYRLDEEL AVPDPASRFQ PKDVHGPSEV VDPRAFHWTH
     TDWHGRPWEE TVLYELHVGA MRGYAGVTAR LPELAQLGVT AIELMPLNDF SGTRNWGYDG
     VLPYAPDSAY GHPDELKKLI DAAHGLGLMV FLDVVYNHFG PDGNYLSTYA KTFFREGVNT
     PWGPAIDFER PQVRDFFFDN ALYWLNEYRF DGLRLDAVQA INDDEWLREL AQRIRSSVET
     GRHVHLVLEN EHNTANLLET HFEAQWSDDS HNTLHVLLTG EDESYYGAYS DKPVEKLARL
     LAEGFVYQGD PSPIHDGKPR GEKSSHLPPT CFIMFLQNHD QVGNRAMGDR LRSLTSDDAL
     RAATGLLLLS PQIPLLFMEE QYGSKQPFLF FTDYHDELAD AVREGRRKEF AKFSAFTDEK
     RRAQIPDPNS VKTFEMSSSR IDETKQDEED RLDWLRFYRS ALTVRAKLIA PRLKDAKALG
     AQVIGDKAVV ARWKLGNSET LGIALNLDDK PVALKNQPQG KVVFETPSRA QDGALKGEFG
     AHAFVAWITG DINEYAASPD ARNVEGKAK
//
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