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Database: UniProt
Entry: A0A0S7ZPB7_9SPIR
LinkDB: A0A0S7ZPB7_9SPIR
Original site: A0A0S7ZPB7_9SPIR 
ID   A0A0S7ZPB7_9SPIR        Unreviewed;       612 AA.
AC   A0A0S7ZPB7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-APR-2018, entry version 15.
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=AMS17_04495 {ECO:0000313|EMBL:KPJ88707.1};
OS   Spirochaetes bacterium DG_61.
OC   Bacteria; Spirochaetes.
OX   NCBI_TaxID=1704237 {ECO:0000313|EMBL:KPJ88707.1};
RN   [1] {ECO:0000313|EMBL:KPJ88707.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_61 {ECO:0000313|EMBL:KPJ88707.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur
RT   cycling among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPJ88707.1}.
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DR   EMBL; LJNB01000042; KPJ88707.1; -; Genomic_DNA.
DR   PATRIC; fig|1704237.3.peg.2418; -.
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   Hydrolase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:KPJ88707.1}.
FT   DOMAIN      113    457       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    259    259       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    296    296       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        390    390       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   612 AA;  70458 MW;  4D5162F34686C25E CRC64;
     MEVGAIYRGN GRCSFTVWTP FKKDVSIRIL HPKKRTISME KDERGYWSVH AEGVYPGTQY
     VLELDHKQRR PDPASFYQPD GVHGPSEVID HKAFVWEDRS WNGVPLEEMV LYEIHTGTFT
     PEGSFEAIIP RLTSLKDLGI TTLEIMPVAQ FPGTRNWGYD GVYPFAVHSS YGGPYGLKSL
     VNACHSQGIA VVLDVVYNHL GPEGNFFQDY GPYFTEKYKT FWGKALNFYD EYSNEVRSYF
     IQNMRYWFLQ YHIDGLRLDA IHAIFDMSAK HFLQALSKTA DEVSGKQGRK YYLIAESNLN
     DVRIIRPRAQ NGYGIDAQWC DDFHHALHTL LTGEQNGYYC DFGSIDHLRV AMMEGFYYSW
     KYSRFRKKYF GSSTEGIRAS QFIVFSQNHD QIGNRVDGKR LSRLVSFEAL KLAAGTVMLS
     PFVPLLFMGE EYGEKAPFHY FVSHSDINLI KAVREGRRRE FKAFNLKENF PDSQDEKTFT
     SSKLTWEQRK EDPHKVLLSF YTKLMQLRTT IPVFKTLDKD SLDIRGEEGD KLLIYIRSHL
     KGKVLCIMNF CRETVQWTCD TGNGIWNKII NSADKSWLGP GSSDPQTLEQ GTTLTVPPLS
     FVVYIHHMEN TG
//
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