TREH1_SULAC
ID TREH1_SULAC Reviewed; 558 AA.
AC Q4J7W0;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Trehalase 1 {ECO:0000303|PubMed:29574614};
DE EC=3.2.1.28 {ECO:0000269|PubMed:29574614, ECO:0000269|PubMed:29642287};
DE AltName: Full=Alpha,alpha-trehalase {ECO:0000305};
DE AltName: Full=SaTreH1 {ECO:0000303|PubMed:29574614};
GN Name=treH1; OrderedLocusNames=Saci_1816 {ECO:0000312|EMBL:AAY81122.1};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF GLU-374; GLY-523; GLU-524 AND HIS-525.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=29574614; DOI=10.1007/s00253-018-8915-7;
RA Yuasa M., Okamura T., Kimura M., Honda S., Shin Y., Kawakita M., Oyama F.,
RA Sakaguchi M.;
RT "Two trehalose-hydrolyzing enzymes from Crenarchaeon Sulfolobus
RT acidocaldarius exhibit distinct activities and affinities toward
RT trehalose.";
RL Appl. Microbiol. Biotechnol. 102:4445-4455(2018).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=29642287; DOI=10.4014/jmb.1802.02038;
RA Lee J., Lee A., Moon K., Choi K.H., Cha J.;
RT "Saci_1816: A trehalase that catalyzes trehalose degradation in the
RT thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius.";
RL J. Microbiol. Biotechnol. 28:909-916(2018).
CC -!- FUNCTION: Catalyzes the hydrolysis of alpha,alpha-trehalose into two
CC molecules of D-glucose. {ECO:0000269|PubMed:29574614,
CC ECO:0000269|PubMed:29642287}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC Evidence={ECO:0000269|PubMed:29574614, ECO:0000269|PubMed:29642287};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41.8 mM for trehalose (at 50 degrees Celsius and pH 4.0)
CC {ECO:0000269|PubMed:29574614};
CC KM=54.5 mM for trehalose (at 60 degrees Celsius and pH 4.0)
CC {ECO:0000269|PubMed:29574614};
CC Note=kcat is 77.0 sec(-1) at 50 degrees Celsius and pH 4.0. kcat is
CC 102.5 sec(-1) at 60 degrees Celsius and pH 4.0.
CC {ECO:0000269|PubMed:29574614};
CC pH dependence:
CC Optimum pH is 4.0 (PubMed:29574614, PubMed:29642287). More than half
CC of the maximal activity is observed over a range between pH 3.3 and
CC 4.0 (PubMed:29574614). {ECO:0000269|PubMed:29574614,
CC ECO:0000269|PubMed:29642287};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:29574614, ECO:0000269|PubMed:29642287};
CC -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from
CC alpha,alpha-trehalose: step 1/1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR EMBL; CP000077; AAY81122.1; -; Genomic_DNA.
DR RefSeq; WP_011278624.1; NC_007181.1.
DR AlphaFoldDB; Q4J7W0; -.
DR SMR; Q4J7W0; -.
DR STRING; 330779.Saci_1816; -.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR EnsemblBacteria; AAY81122; AAY81122; Saci_1816.
DR GeneID; 3474304; -.
DR KEGG; sai:Saci_1816; -.
DR PATRIC; fig|330779.12.peg.1761; -.
DR eggNOG; arCOG03286; Archaea.
DR HOGENOM; CLU_010399_3_1_2; -.
DR OMA; AFVLTWH; -.
DR UniPathway; UPA00300; UER00535.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR045582; Trehalase-like_N.
DR Pfam; PF19291; DUF5911; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..558
FT /note="Trehalase 1"
FT /id="PRO_0000448957"
FT MUTAGEN 374
FT /note="E->Q: Less than 1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:29574614"
FT MUTAGEN 523
FT /note="G->S: No change of activity."
FT /evidence="ECO:0000269|PubMed:29574614"
FT MUTAGEN 524
FT /note="E->Q: Less than 1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:29574614"
FT MUTAGEN 525
FT /note="H->E: 15% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:29574614"
SQ SEQUENCE 558 AA; 63575 MW; FC150F0AEB5102BD CRC64;
MLGMKPLGFI GNGLTSALVD NGSIVWLTFP RFDSPSVFGK LLDDNAGEFS IRPVEDKFKV
SQSYLVPNVL STTFKSSNGK AEIVDLMPIG EKAIIRKVRT EIPLSFKIIP MFNYGLYRPI
IRRKDDGIQF LNPVSRECLS LLSDVPTDEI KPPGTTLYLV YSSDCAYGPL DKGKQLENDL
ENSFNLTIDY WKDKIRSNDE VWRTSVGVLL GLIYSPSGSS IAAATTSLPE AVGDSRNWDY
RFVWVRDSSM ISEALLYSGY VVEARRILNF MLALVNFTAK PLLHPLYAVD GSDPPPEIEI
PWLSGYMNSR PVRVGNAAAS QIQLDIEGFL VDAIYKYYKY TSDRVFVEEN WDKIKYIGDW
VSKNWMLKDA GMWEDRGDPK HYTHSKVMMW VALDRIEKIM NVKIHEKDEI KEWVMRNCVK
DGSFVRSSDS NDVDANLLTL PLYDFIDVKD PIFLKTLKRI EDELYVDGFV KRYSQDFMGE
AKHPFALATI WLARVYIRLG RKERAMELLD KVLKPSGTLY LIGEHIDVEN MEYTGNYPQA
FVHAQLLLAL KEVKGLST
