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Database: UniProt
Entry: A0A0D0Q6F3_9RHOB
LinkDB: A0A0D0Q6F3_9RHOB
Original site: A0A0D0Q6F3_9RHOB 
ID   A0A0D0Q6F3_9RHOB        Unreviewed;       586 AA.
AC   A0A0D0Q6F3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   20-DEC-2017, entry version 21.
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=Wenmar_01609 {ECO:0000313|EMBL:KIQ70039.1};
OS   Wenxinia marina DSM 24838.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Wenxinia.
OX   NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ70039.1, ECO:0000313|Proteomes:UP000035100};
RN   [1] {ECO:0000313|EMBL:KIQ70039.1, ECO:0000313|Proteomes:UP000035100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ70039.1,
RC   ECO:0000313|Proteomes:UP000035100};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (JAN-2013) 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}.
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:KIQ70039.1}.
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DR   EMBL; AONG01000008; KIQ70039.1; -; Genomic_DNA.
DR   RefSeq; WP_018301029.1; NZ_KN848372.1.
DR   EnsemblBacteria; KIQ70039; KIQ70039; Wenmar_01609.
DR   PATRIC; fig|1123501.6.peg.1702; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000035100; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000035100};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:KIQ70039.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:KIQ70039.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035100}.
FT   DOMAIN       63    453       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    257    257       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    292    292       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        387    387       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   586 AA;  64717 MW;  428D71ED9C4B328A CRC64;
     MTDRRPAWGA VPTRPGHWHL RLWAPGADSL SLRLGAADRP MEAEGDGWFG LEVEAEEGAP
     YSFVLPDGMA VPDPAARRQQ GDVHGPSLLT APPADDPWAG WSGRPWEEAA ILELHVGTFT
     GEGTFRAAID RLDHIAKAGF TAIEIMPVAQ FAGDRGWGYD GVLLYAPHPA YGTPDDLRAL
     VRAAHERGLM VLLDVVYNHF GPEGSYLHAY APDFFHDEKD TPWGGAIAFE RQPVRRFMIE
     NGLYWLREFG FDGLRLDAID HIDDPSDEEV LIEFARELRA ALPGRPVHLT TEDSRNVTHL
     HEREDGRVTL HTAEWNDDFH NVAHVIATGE TEAYYADFAQ KEWAHLARTL AEGFAYQGEP
     DRSGKVRGKT SGHQPPTAFV DFLQNHDQIG NRAFGERLCN LASPRMVDAL TAILLLSPHI
     PLMFMGEEYG ETRSFCFFAG FDGDLARAVT EGRRREFADF SAFTVADTSS IPDPIARSTF
     EASKLDWAKL SDDDHRATLD RTRHLLTLRR ERIVPLLAGA GPHCGTVLKA DEGAIAVDWR
     LGGGALLQLR ANLEDQPRDL PPATGEELHR VGAPGGPISA VHWLGT
//
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