(data stored in SCRATCH zone)

SWISSPROT: Q13S09_PARXL

ID   Q13S09_PARXL            Unreviewed;       640 AA.
AC   Q13S09;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 96.
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=Bxe_B2865 {ECO:0000313|EMBL:ABE33130.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33130.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33130.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33130.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE33130.1; -; Genomic_DNA.
DR   RefSeq; WP_011490510.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2865; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABE33130; ABE33130; Bxe_B2865.
DR   GeneID; 4006770; -.
DR   KEGG; bxb:DR64_5194; -.
DR   KEGG; bxe:Bxe_B2865; -.
DR   PATRIC; fig|266265.5.peg.4826; -.
DR   eggNOG; ENOG4105C9C; Bacteria.
DR   eggNOG; COG0296; LUCA.
DR   HOGENOM; HOG000155668; -.
DR   KO; K01236; -.
DR   OMA; FTPMLFM; -.
DR   OrthoDB; 148706at2; -.
DR   BioCyc; BXEN266265:BXE_RS22875-MONOMER; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000001817; 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; 2.
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; Q13S09.
DR   SWISS-2DPAGE; Q13S09.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:ABE33130.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:ABE33130.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN      108    470       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    274    274       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    307    307       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        398    398       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   640 AA;  71418 MW;  AACF14CABF9227A7 CRC64;
     MSESPIDPHA HHHAHCLPFG AQLIGATGAK PRTRFRFWAP SCKHVQVEIE NGPAQGAHDM
     TPAGNGWFEA SVDSGAGTLY RFRLDGEHAV PDPTSRFQPQ DVHGPSEVID PRAYRWQQTN
     WHGRPWEETV LYELHVGALG GYAGVQKRLP ELAALGVTAI ELMPLNDFPG KHNWGYDGVL
     PYAPDSAYGR PEDLKALIDA AHGLGLMVFL DVVYNHFGPD GNYLHEYARS FFREGTHTPW
     GPAIDFERSE VSDFFTDNAV YWINEYRIDG LRFDAVHAID NHAWLRELSD HIRARVQHGR
     HVHLVLENEH NSANLLETHF DAQWNDDAHN TLHVLLTGET EGYYHAYEDQ PIRRLARVLS
     EGFAYQGDPS PIHDGKPRGE ASAHLPPTSF VMFLQNHDQV GNRAFGERLR KLTSDEALRA
     ATGLLLLSPQ IPLLFMGEEY GSTQPFLFFT DYTGDLADAV REGRRREFAR FSSFSDEKRR
     AQIPDPNDVK TFAASSPPAP DETSQHTDAE AKDRLDWMHF YKSALAVRAR LITPRLKHSK
     ACGATVLSAA NGGDANALIA RWKLGDGETL SIALNLSKEN VALADLPAGK VIFETPPRVR
     EQVDVKVLPA HAFVAWLTGD VSGYAIRHDA RIAGQQERHA
//

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