(data stored in ACNUC7421 zone)

SWISSPROT: B2UHI9_RALPJ

ID   B2UHI9_RALPJ            Unreviewed;       613 AA.
AC   B2UHI9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 87.
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   OrderedLocusNames=Rpic_3935 {ECO:0000313|EMBL:ACD29040.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29040.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-
CC         alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield
CC         trehalose and (1->4)-alpha-D-glucan.; EC=3.2.1.141;
CC         Evidence={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; CP001069; ACD29040.1; -; Genomic_DNA.
DR   RefSeq; WP_012430070.1; NC_010678.1.
DR   STRING; 402626.Rpic_3935; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ACD29040; ACD29040; Rpic_3935.
DR   GeneID; 6285119; -.
DR   KEGG; rpi:Rpic_3935; -.
DR   PATRIC; fig|402626.5.peg.174; -.
DR   eggNOG; ENOG4105C9C; Bacteria.
DR   eggNOG; COG0296; LUCA.
DR   HOGENOM; HOG000155668; -.
DR   KO; K01236; -.
DR   OMA; FTPMLFM; -.
DR   OrthoDB; 148706at2; -.
DR   BioCyc; RPIC402626:GH94-3936-MONOMER; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000002566; Chromosome 2.
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;
DR   PRODOM; B2UHI9.
DR   SWISS-2DPAGE; B2UHI9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:ACD29040.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   DOMAIN      103    465       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    269    269       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    302    302       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        398    398       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   613 AA;  68079 MW;  DB258FFA36D91D1A CRC64;
     MTAPAPRFAH DMPFGATVLA DGNTRFRLWA PDATAAWIDI DDTRGNESIR MDAEPDGWYA
     AVAPVGSGTC YRYRLTNRDG VTLSVPDPAA RAQWQDIPGP SLVVDPQRYR WQHADWQGRP
     WHETVLYELH VGALGGFKGV RGRLPELARL GITAIELMPV AEFPGARNWG YDGVLPFAPD
     ASYGTPDDLK ALIDTAHGLG MMVFLDVVYN HFGPDGNYLH HYARSFFRDD VHTPWGAAID
     FRKPQVREFF IQNALMWLME YRFDGLRLDA VHAITERDWL GELAARVRLS AEPGRHVHLV
     LENEHNAASL LRDGNTHGDF DAQWNDDGHN VLHVLLTGER EAYYAAYADA PAQRLARVLQ
     DGFCYQGEPS PIHDNAPRGE PSAHLPPTAF VLFLQNHDQI GNRAFGERLT QLAHPDALHA
     AQVLLLLSPQ IPMLFMGEEW GSTCPFQYFT SHHGMLAEAV REGRRREFAK FEAFADPHQR
     ERIPDPNEEL TYLASCPGEA NLAEPAQLNT LNRMHRLLAL RHAEIIPRLP HARALDAVAL
     GHAGAIARWR MGDGSVLTLM LNLADQPVAV PTVLAGSPAD LLHESREGAA AALITHRLPE
     RACVALLHTP SPG
//

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