ID A0A0M2UT30_9BACT Unreviewed; 625 AA.
AC A0A0M2UT30;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=BROFUL_02516 {ECO:0000313|EMBL:KKO18775.1};
OS Candidatus Brocadia fulgida.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO18775.1, ECO:0000313|Proteomes:UP000034954};
RN [1] {ECO:0000313|EMBL:KKO18775.1, ECO:0000313|Proteomes:UP000034954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KKO18775.1};
RX PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA Keltjens J.T., Jetten M.S.;
RT "Identification of the type II cytochrome c maturation pathway in anammox
RT bacteria by comparative genomics.";
RL BMC Microbiol. 13:265-265(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKO18775.1}.
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DR EMBL; LAQJ01000236; KKO18775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2UT30; -.
DR PATRIC; fig|380242.3.peg.3124; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000034954; 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 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:UP000034954}.
FT DOMAIN 86..458
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 258
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 295
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 256..261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 320..324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 388..393
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 389
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 625 AA; 71202 MW; E1BCAD9F9FD78372 CRC64;
MHAINYISSG RCEFNVWAPF LSAVAVKILS PEERLVPMEK DMEGFWRATL TGITPAVRYL
YRLSDEKDRP DPASQYQPDG VHGPSQVIDH SAFRWSDENW RGISLSEMII YELHVGTFTP
DGTFKAIIPR LDEVRDTGIN TIELMPVSQF PGERNWGYDG VYPYAVQNSY GGPQGLKHLV
NECHRRGISV ILDVVYNHLG PEGNYLRDFG PYFTTTYLTP WGEAINFDSA YSREVRNYFI
ENALHWLRHY HVDALRIDAV HAIFDMKAKH FLSELSERVE EFSQEQGRKY YLIAESDLND
SRIVMPRESG GYGIDGVWCD DFHHSLHTLL TGENRGYYLD FGKIEHMVKS MKEGFVYSGE
YSEFRKRNHG NSSGDIPAQQ MVVFSQNHDQ TGNRMLGERL SALVSFEALK LAAGVVLLSP
YVPLIFMGEE YGEDTPFLYF VSHSDPGLIE AVQRGRMREF REFKWQGGLP DPQSTETFLK
SKIDWEKRRE GHHKVLLNFY RQLIGLRKTI PALSHPDKKN LCAEGNENQR ILFIMRRKDA
SQIMIALNFN GADVACVPPL SDGAWNKAID SAESIWRGPG SVLPYELVPG SEITVRGGSI
ALYIRKSPLL EENGGIQQSN PENHE
//
