ID A0A143Q6C9_9NOCA Unreviewed; 602 AA.
AC A0A143Q6C9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Name=treZ {ECO:0000313|EMBL:AMY18640.1};
GN ORFNames=A3Q40_01247 {ECO:0000313|EMBL:AMY18640.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY18640.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY18640.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY18640.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL Submitted (APR-2016) 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; CP015219; AMY18640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143Q6C9; -.
DR STRING; 1653478.A3Q40_01247; -.
DR KEGG; rhu:A3Q40_01247; -.
DR PATRIC; fig|1653478.3.peg.1255; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000076180; Chromosome.
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:UP000076180}.
FT DOMAIN 120..465
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 302
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 263..268
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 327..331
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 397..402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 398
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 602 AA; 65519 MW; 031DF388080C79F8 CRC64;
MDEPPPGYRG RMSPSPSSDT AATRTFSVWA PTPDRVRLHL DGELHDMHET DGWWSVDVPA
ADGARYGFVL GDDDAVIPDP RSPRQPDGVH EPSAVFDVDR TAWTDDGWTG RRLAGGVLYE
LHIGTFTPEG TFDAAIGKLD HLVDLGVTFV EVMPVNGFNG THNWGYDGVL WYTVHEGYGG
PAGLQRFVDA CHARGLAVAL DVVYNHLGPS GNYLEKFGPY LAEGANSWGQ TVNVAESGSD
VVRRYIVDNA LRWFDEFHID ALRLDAVHAL ADTTAVHILE QLAVETESLS AHVGRPLSLI
AESDLNDPTL ITPRAGGGYG LTAQWDDDVH HAVHAAVSGE RQGYFGDFGS MSCLATTIGH
GFFHAGTYSS FRGRIHGRPV DPRVLPASSL VAYTTTHDQV GNRAVGDRPG HYLTTGQQAV
KAALILLSPF TPMLFMGEEF DASSPFQFFT SHPEPELGKA TAEGRKAEFA SHGWDSDDIP
DPQDPATFER SKLNWSEVTV GKHAALLEIY RSLLALRAER PEFTDPWLTN VRVDHDEDER
WIVVHRKRVG TPGRGTALAC NLSDTPVTVP VGGTPVLWSS ETTSDRTGSS TTLPGHSFVV
LT
//
