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Database: UniProt
Entry: A0A1W6YZR2_9BORD
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ID   A0A1W6YZR2_9BORD        Unreviewed;       611 AA.
AC   A0A1W6YZR2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00015938, ECO:0000256|PIRNR:PIRNR006337};
DE            Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE            EC=3.2.1.141 {ECO:0000256|ARBA:ARBA00012268, ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00033284, ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00032057, ECO:0000256|PIRNR:PIRNR006337};
GN   ORFNames=CAL13_09650 {ECO:0000313|EMBL:ARP86434.1};
OS   Bordetella genomosp. 9.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416803 {ECO:0000313|EMBL:ARP86434.1, ECO:0000313|Proteomes:UP000194139};
RN   [1] {ECO:0000313|EMBL:ARP86434.1, ECO:0000313|Proteomes:UP000194139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17164 {ECO:0000313|EMBL:ARP86434.1,
RC   ECO:0000313|Proteomes:UP000194139};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-
CC         [(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-
CC         alpha-D-glucan.; EC=3.2.1.141;
CC         Evidence={ECO:0000256|ARBA:ARBA00034013,
CC         ECO:0000256|PIRNR:PIRNR006337};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005199, ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRSR:PIRSR006337-1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR006337}.
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DR   EMBL; CP021109; ARP86434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6YZR2; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000194139; Chromosome.
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   CDD; cd11325; AmyAc_GTHase; 1.
DR   CDD; cd02853; E_set_MTHase_like_N; 1.
DR   Gene3D; 1.10.10.760; E-set domains of sugar-utilizing enzymes; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   InterPro; IPR044901; Trehalose_TreZ_E-set_sf.
DR   NCBIfam; TIGR02402; trehalose_TreZ; 1.
DR   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006337};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194139}.
FT   DOMAIN          133..520
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          482..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        274
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT   ACT_SITE        307
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT   BINDING         272..277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   BINDING         326..330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   BINDING         397..402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   SITE            398
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ   SEQUENCE   611 AA;  68408 MW;  8341DCD074B254BE CRC64;
     MTDTPSSNPT EQSARAETGR TFMPSFGACH LPSGLTRFRL WAPNAEHGVT LEIAGAEPQP
     MTDVGDGYYE IETPCPPGTR YRYRVSPDLS VPDPASRLQA GDVHDDSVVT SSSYTWRNDG
     WRGRPWREAV FYEIHPGIAG GFAGIEARLP ELADLGFTAI ELMPIADFPG PRNWGYDGVL
     PYAPDCAYGT PEELKRLIDT AHGLGLMVFL DVVYNHFGPD GNYLSAYASD FFRDDLHTPW
     GVAIDFRRRP VRQFFTENAL YWLTEYRFDG LRLDAVHAIR DVGWLEEMAG YVRAHLPADR
     HVHLVLENDD NQVHPLEHGY QAQWNDDGHH VLHQLLTGES EGYYGDYAVH PAQRLTRALA
     DGFIYQGEPS AHRNGARRGE PSAHLPPTSF VLFLQNHDQI GNRAMGDRLI SLLRNDTRAL
     RAAVALLLLC PQIPLVFMGE ERGATAPFLY FTSHTNPELA QAVRDGRRKE FEKFRAFANP
     ATRDRIPDPN DPETFAQSDP YREPANESWL SYYRDLLQVR HRMIAPRLEG ARALGAHILG
     LRAVVAQWLL SDGAILSLYV NLGTVDLRPD WLQDDHRGET LLYESEAGAG AALYEGMLQN
     GVTVALLKEP A
//
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