ID J3ERK9_9PSED Unreviewed; 598 AA.
AC J3ERK9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=PMI21_02569 {ECO:0000313|EMBL:EJM17552.1};
OS Pseudomonas sp. GM18.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144324 {ECO:0000313|EMBL:EJM17552.1, ECO:0000313|Proteomes:UP000007280};
RN [1] {ECO:0000313|EMBL:EJM17552.1, ECO:0000313|Proteomes:UP000007280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM18 {ECO:0000313|EMBL:EJM17552.1,
RC ECO:0000313|Proteomes:UP000007280};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM17552.1}.
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DR EMBL; AKJT01000041; EJM17552.1; -; Genomic_DNA.
DR RefSeq; WP_007937872.1; NZ_AKJT01000041.1.
DR AlphaFoldDB; J3ERK9; -.
DR PATRIC; fig|1144324.3.peg.2522; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000007280; 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}.
FT DOMAIN 95..448
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 292
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT SITE 381
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 598 AA; 67292 MW; D4F14F0DA7E3FADE CRC64;
MPLRTLETWP HGAIMLDAEH TRFALWAPDA FYVSLELENG QSLPLLPQAD GWFVIKTRCP
AGTRYRYNID GELEVPDPAS RAQAGDIGSH SVVVDPLAYR WQHSAWQGRP WNEAVIYELH
VGALGGFNEV EQHLARLVEL GITAIELMPL AQFPGERNWG YDGVLPYAPQ ASYGSPEQLK
HLIDTAHGHG LAVILDVVYN HFGPDGNYLH RYAKGFFRED QHTPWGAAID FRRHEVRDFF
IDNALMWLLE YRFDGLRLDA VHAIDDPDFL QELAQRVRRQ IDPARHVWLM AENEHNQASL
LEQGFDAQWN DDGHNALHVL LTGETDAYYA DYAQNPTEQL ARCLSQGFVF QGHITRHGTP
RGEPSGHLPP TAFVLFLQNH DQIGNRAFGE RLHQLARSEA LNAATVLLLL SPMIPLMFMG
DEFAAEQPFL FFTSHHGELA ELVREGRRNE FAAFSAFADP HKREQIPDPN AMQTFEASRP
KLTATRQPPV YDLYRRLLQT RHQHIIPHLP GTQALGAQVL AEGAVTARWR LGDGRQLRID
LNLRDAPVVH TPQADATLLF EYPPHSAGLL DQGTLAPYCA LVSLTAAVPL LPPDGERP
//
