ID F3G6A6_PSESJ Unreviewed; 604 AA.
AC F3G6A6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 71.
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=PSYPI_09445 {ECO:0000313|EMBL:EGH42606.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH42606.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH42606.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH42606.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH42606.1}.
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DR EMBL; AEAI01000474; EGH42606.1; -; Genomic_DNA.
DR AlphaFoldDB; F3G6A6; -.
DR PATRIC; fig|629263.4.peg.1555; -.
DR HOGENOM; CLU_020726_0_0_6; -.
DR BioCyc; PSYR629263:G11X0-1884-MONOMER; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000004986; 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 93..444
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 604 AA; 68132 MW; A6379F98024BB507 CRC64;
MPLRTDDNWR HGAVLLDPEH TRFALWAPDA SFVNVELQDG QSLAMLPQSD GWFVLEARCK
AGTRYRFRID HELDVPDPAS AAQVDDVHSE SLVVDPDAYS WQNTAWNGRH WHEAVIYELH
VGAMGGYAGV EKHLPRLAKL GVTAIELMPL AQFPGDRNWG YDGVLHYAPQ SSYGTPEQLK
HLIDTAHGLG LMVILDVVYN HFGPDGNYLG SYAKEFFRTD LHTPWGDAID FRRPQVRDFF
VDNALMWLLE YRFDGLRIDA VHAIRDETFL PEFAERVRGR IEPGRHVWLN LENEFNQAGL
LEKGFDAQWD DDGHNTLHVL LTGETDAYYS DFAKEPPQKL ARLLSEGFVY QGEPTRHGHT
RGEPSAHLSP SFFVLFLQNH DQIGNRALGE RLPQLCAPAA LKAATVLLLL SPMIPLMFMG
DEWAASEPFL FFTSHHGELA DAVREGRRKE FADFAAFADP EKREHIPDPN DIKTFEASRP
AFSAVDLDTD IGLDHRSWLE FYTQLLALRH QEIMPRLQGA RFLKTDILGD KAVSARWTLV
DGSELRIDLN LSEHAVDAPP QAGAREIFSS AEKSSELSPR GILNAYTAIV SLKASDVLEE
QDEQ
//
