TREC_BACSU
ID TREC_BACSU Reviewed; 561 AA.
AC P39795; O34517;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Trehalose-6-phosphate hydrolase {ECO:0000305};
DE EC=3.2.1.93 {ECO:0000269|PubMed:7651129, ECO:0000269|PubMed:7751281};
DE AltName: Full=Alpha,alpha-phosphotrehalase;
DE AltName: Full=Phospho-alpha-(1-1)-glucosidase {ECO:0000303|PubMed:7651129};
GN Name=treA {ECO:0000303|PubMed:7651129}; Synonyms=treC;
GN OrderedLocusNames=BSU07810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7651129; DOI=10.1111/j.1365-2958.1995.tb02396.x;
RA Helfert C., Gotsche S., Dahl M.K.;
RT "Cleavage of trehalose-phosphate in Bacillus subtilis is catalysed by a
RT phospho-alpha-(1-1)-glucosidase encoded by the treA gene.";
RL Mol. Microbiol. 16:111-120(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT region of the Bacillus subtilis chromosome containing genes for trehalose
RT metabolism and acetoin utilization.";
RL Microbiology 142:3057-3065(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=7751281; DOI=10.1128/jb.177.10.2721-2726.1995;
RA Gotsche S., Dahl M.K.;
RT "Purification and characterization of the phospho-alpha(1,1)glucosidase
RT (TreA) of Bacillus subtilis 168.";
RL J. Bacteriol. 177:2721-2726(1995).
CC -!- FUNCTION: Hydrolyzes trehalose-6-phosphate to glucose and glucose 6-
CC phosphate. Can also very effectively hydrolyze p-nitrophenyl-alpha-D-
CC glucopyranoside, but not lactose, maltose, sucrose or sucrose-6-
CC phosphate. Trehalose is also hydrolyzed, but to a much smaller extent
CC than trehalose-6-phosphate. {ECO:0000269|PubMed:7651129,
CC ECO:0000269|PubMed:7751281}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose 6-phosphate + H2O = D-glucose + D-
CC glucose 6-phosphate; Xref=Rhea:RHEA:23008, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58429, ChEBI:CHEBI:61548; EC=3.2.1.93;
CC Evidence={ECO:0000269|PubMed:7651129, ECO:0000269|PubMed:7751281};
CC -!- ACTIVITY REGULATION: Activity is stimulated by high salt concentrations
CC with different efficiencies depending on the kind of salt. In vitro,
CC inhibited by glucose. {ECO:0000269|PubMed:7751281}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:7751281};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:7751281};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7651129}.
CC -!- INDUCTION: Induced by trehalose and repressed by glucose, fructose or
CC mannitol. {ECO:0000269|PubMed:7651129}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; Z54245; CAA91015.1; -; Genomic_DNA.
DR EMBL; X80203; CAA56495.1; -; Genomic_DNA.
DR EMBL; D83967; BAA23408.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12610.1; -; Genomic_DNA.
DR PIR; B69725; B69725.
DR RefSeq; NP_388662.1; NC_000964.3.
DR RefSeq; WP_003244272.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P39795; -.
DR SMR; P39795; -.
DR STRING; 224308.BSU07810; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR jPOST; P39795; -.
DR PaxDb; P39795; -.
DR PRIDE; P39795; -.
DR EnsemblBacteria; CAB12610; CAB12610; BSU_07810.
DR GeneID; 939690; -.
DR KEGG; bsu:BSU07810; -.
DR PATRIC; fig|224308.179.peg.845; -.
DR eggNOG; COG0366; Bacteria.
DR InParanoid; P39795; -.
DR OMA; PNGEKWA; -.
DR PhylomeDB; P39795; -.
DR BioCyc; BSUB:BSU07810-MON; -.
DR BioCyc; MetaCyc:MON-5946; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008788; F:alpha,alpha-phosphotrehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012769; Trehalose_TreC.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR02403; trehalose_treC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..561
FT /note="Trehalose-6-phosphate hydrolase"
FT /id="PRO_0000054320"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00691"
FT ACT_SITE 254
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00691"
FT SITE 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00691"
FT CONFLICT 114..123
FT /note="FREAISSIDS -> LRGDLFNRQ (in Ref. 1; CAA91015)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="G -> E (in Ref. 1; CAA91015/CAA56495)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..290
FT /note="PNG -> LTA (in Ref. 1; CAA91015/CAA56495)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="V -> A (in Ref. 1; CAA91015/CAA56495)"
FT /evidence="ECO:0000305"
FT CONFLICT 547..561
FT /note="LRPYESIVYRLTKPC -> VAHMSPLFIV (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 65184 MW; 12C0AC7F069139A5 CRC64;
MKTEQTPWWK KAVVYQIYPK SFNDTTGNGV GDLNGIIEKL DYLKTLQVDV LWLTPIYDSP
QHDNGYDIRD YYSIYPEYGT MEDFERLVSE AHKRDLKVVM DLVVNHTSTE HKWFREAISS
IDSPYRDFYI WKKPQENGSV PTNWESKFGG SAWELDEASG QYYLHLFDVT QADLNWENEE
VRKHVYDMMH FWFEKGIDGF RLDVINLISK DQRFPNAEEG DGRSFYTDGP RVHEFLHEMN
EKVFSHYDSM TVGEMSSTTV DHCIRYTNPD NKELDMTFSF HHLKVDYPNG EKWALAPFDF
LKLKEILSDW QTGMHAGGGW NALFWCNHDQ PRVVSRYGDD GAYRVKSAKM LATAIHMMQG
TPYIYQGEEL GMTNPKFTDI SSYRDVESLN MYHAFKEKGM ADQDITAILQ AKSRDNSRTP
VQWDATENGG FTTGTPWIPV AGNYREINAE AALRDQNSVF YHYQKLIQIR KMYDIVTEGT
YEIIAKDDPN IFAYLRHGSN EKLLVINNFY GTEAAFTLPD SLAPDEWKAE VLLTNDEARE
GLQNMTLRPY ESIVYRLTKP C
