ID A0A1Q2CEI7_9ACTN Unreviewed; 564 AA.
AC A0A1Q2CEI7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=RPIT_06585 {ECO:0000313|EMBL:AQP44518.1}, SAMN05428934_103262
GN {ECO:0000313|EMBL:SDY71937.1};
OS Tessaracoccus flavus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1610493 {ECO:0000313|EMBL:AQP44518.1, ECO:0000313|Proteomes:UP000188324};
RN [1] {ECO:0000313|EMBL:AQP44518.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP1T {ECO:0000313|EMBL:AQP44518.1};
RX PubMed=26869509; DOI=10.1099/ijsem.0.000958;
RA Kumari R., Singh P., Schumann P., Lal R.;
RT "Tessaracoccus flavus sp. nov., isolated from the drainage system of a
RT lindane-producing factory.";
RL Int. J. Syst. Evol. Microbiol. 66:1862-1868(2016).
RN [2] {ECO:0000313|EMBL:SDY71937.1, ECO:0000313|Proteomes:UP000199635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP1 {ECO:0000313|EMBL:SDY71937.1,
RC ECO:0000313|Proteomes:UP000199635};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AQP44518.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RP1T {ECO:0000313|EMBL:AQP44518.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP019605; AQP44518.1; -; Genomic_DNA.
DR EMBL; FNPU01000003; SDY71937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2CEI7; -.
DR STRING; 1610493.RPIT_06585; -.
DR KEGG; tfl:RPIT_06585; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000188324; Chromosome.
DR Proteomes; UP000199635; 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:UP000188324}.
FT DOMAIN 96..456
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 242
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 240..245
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 306..310
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 378..383
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 379
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 564 AA; 61442 MW; FE12658DB41EC58F CRC64;
MRPAVWAPRA GTVTLDLGSA EHPMSATADG WFESPVDLAP GDRYAFRLDG GAPLPDPRSF
SLPDGVHGPS EVLDPALFTR ATQWPGRDLR GAVLYELHIG TFTGPGTFDA AVERLDHLVD
LGVDAVELMP VAAFPGERGW GYDGVALFAV HEPYGGVAGL VRFVDACHER GLAVVLDVVH
NHLGPEGNYL GQFGAYFTDR HETPWGEAVN LDGTDSREVR RFLLDSARHW LVDVGVDGLR
LDAVHALHDD SQRHFLAELS GCVSAWEGEV GRPLTLIAES DLNQPSMVSA VGSVPDARGM
DAQWADDVHH ALHSFFGRET QGYYGDFGTI DDVVKALTRP FVRDGSFSAF RGRLWGAPVD
PASPLYDGHS FVVFLQDHDQ VGNRAVGDRF HQHAGLGEQA AGAALYLLSP YTPMLFMGEE
WAASSPFPYF SDLGPELGPL VTEGRLREFA AMGWAEPTPD PQDPATARSA VLDWEERTTS
PHREMAEFYR RLLELRRLHP ELRDPDLADV RAEVVDGDTV ALHRGPFTIT ATRGRLALNP
PGEVLASYLD REGAGPGAVV TRRS
//
