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Database: UniProt
Entry: A0A0K2DKF2_9RHIZ
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Original site: A0A0K2DKF2_9RHIZ 
ID   A0A0K2DKF2_9RHIZ        Unreviewed;       604 AA.
AC   A0A0K2DKF2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   20-DEC-2017, 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=AL346_23250 {ECO:0000313|EMBL:ALA20334.1};
OS   Chelatococcus sp. CO-6.
OG   Plasmid pCO-6 {ECO:0000313|EMBL:ALA20334.1,
OG   ECO:0000313|Proteomes:UP000065824}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Chelatococcaceae; Chelatococcus.
OX   NCBI_TaxID=1702325 {ECO:0000313|EMBL:ALA20334.1, ECO:0000313|Proteomes:UP000065824};
RN   [1] {ECO:0000313|EMBL:ALA20334.1, ECO:0000313|Proteomes:UP000065824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-6 {ECO:0000313|EMBL:ALA20334.1,
RC   ECO:0000313|Proteomes:UP000065824};
RC   PLASMID=Plasmid pCO-6 {ECO:0000313|Proteomes:UP000065824};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M.,
RA   Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J.,
RA   Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L.,
RA   Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J.,
RA   Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L.,
RA   Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z.,
RA   Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J.,
RA   Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA   Hatfull G.F.;
RL   Submitted (AUG-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}.
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DR   EMBL; CP012399; ALA20334.1; -; Genomic_DNA.
DR   RefSeq; WP_019401932.1; NZ_CP012399.1.
DR   EnsemblBacteria; ALA20334; ALA20334; AL346_23250.
DR   KEGG; chel:AL346_23250; -.
DR   PATRIC; fig|1702325.3.peg.4852; -.
DR   KO; K01236; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000065824; Plasmid pCO-6.
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; 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   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; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR02402; trehalose_TreZ; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000065824};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337};
KW   Plasmid {ECO:0000313|EMBL:ALA20334.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065824}.
FT   DOMAIN       90    461       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    261    261       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    296    296       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        393    393       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   604 AA;  67284 MW;  A74631574C5B339F CRC64;
     MRRRHPMPFG TELSDEGTTF SLWAPTARSV ALDLQGRRVD LPEAGDGWRR LLVPEARAGT
     RYRYFIDGTL VVPDPASRRQ PDGVHGSSLV VDPQAFDWRD GGWRGRPWEE AVLYEAHVGT
     ATPDGTFAAL AGQLPDLAGL GITAVELMPV AQCPGLRNWG YDGVLPFAPH HAYGTPDDLK
     RLVETAHSLG LMVLLDVVYN HFGPSGNYLH AYAAPFFTDR HATPWGQAID FEGGNAPVRD
     FFIHNALYWL EEFHLDGLRL DAVHAIADDS DPHILDDIAR AVRESFPDRH VHLVLENDAN
     EARYLERSGG VARRYTAQWD DDLHHAWHVV LTGESSGYYA DYGDAPLRAL GRALVEGFVY
     QGEPSRFRKG APRGEPSRHL PPVAFVAFLQ NHDQIGNRAF GERLTTLVPE QRLAAARAAL
     LLSPQVPMLF MGEEWASTSP FLYFVDYAEE PDIARAVREG RRREFAEGAG FSDPARAETI
     PDPNAQDTFV RSRIDWNERE HPPHAPILGQ VRRLLALREA HVLPLLRSGF RDARWDLPTP
     YCLDVSWHFE AGTLRFILNV GDAPLTLSGV DQSTAISMSE PARLEGDECI LPAWCAAFFA
     SPRP
//
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