TREB_EMENI
ID TREB_EMENI Reviewed; 751 AA.
AC O42777; C8VFW3; Q5B1E5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cytosolic neutral trehalase;
DE EC=3.2.1.28 {ECO:0000305|PubMed:10320571};
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
GN Name=treB {ECO:0000303|PubMed:10320571}; ORFNames=AN5635;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10320571; DOI=10.1046/j.1365-2958.1999.01327.x;
RA d'Enfert C., Bonini B.M., Zapella P.D.A., Fontaine T., da Silva A.M.,
RA Terenzi H.F.;
RT "Neutral trehalases catalyse intracellular trehalose breakdown in the
RT filamentous fungi Aspergillus nidulans and Neurospora crassa.";
RL Mol. Microbiol. 32:471-483(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Hydrolyzes intracellular trehalose to glucose (Probable). The
CC disaccharide trehalose serves as a storage carbohydrate that is
CC mobilized during conidial germination (PubMed:10320571). Regulates the
CC level of trehalose as a protectant for cell integrity during heat
CC stress (PubMed:10320571). {ECO:0000269|PubMed:10320571,
CC ECO:0000305|PubMed:10320571}.
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:0000305|PubMed:10320571};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P32356};
CC -!- ACTIVITY REGULATION: Activated by calcium.
CC {ECO:0000250|UniProtKB:P32356}.
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32356}.
CC -!- DEVELOPMENTAL STAGE: Expressed during spore germination and growth.
CC {ECO:0000269|PubMed:10320571}.
CC -!- INDUCTION: Induced during recovery from thermal stress.
CC {ECO:0000269|PubMed:10320571}.
CC -!- DISRUPTION PHENOTYPE: Abolishes trehalose degradation during conidial
CC germination and delays germ tube formation (PubMed:10320571).
CC Resistance to thermal stress (PubMed:10320571).
CC {ECO:0000269|PubMed:10320571}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99831.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA62728.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF043229; AAB99831.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000098; EAA62728.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001305; CBF81508.1; -; Genomic_DNA.
DR RefSeq; XP_663239.1; XM_658147.1.
DR AlphaFoldDB; O42777; -.
DR SMR; O42777; -.
DR STRING; 162425.CADANIAP00003435; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR EnsemblFungi; CBF81508; CBF81508; ANIA_05635.
DR EnsemblFungi; EAA62728; EAA62728; AN5635.2.
DR GeneID; 2871930; -.
DR KEGG; ani:AN5635.2; -.
DR VEuPathDB; FungiDB:AN5635; -.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_1_1_1; -.
DR InParanoid; O42777; -.
DR OMA; GLERPNR; -.
DR OrthoDB; 417479at2759; -.
DR BRENDA; 3.2.1.28; 517.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015927; F:trehalase activity; IMP:AspGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:AspGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:AspGD.
DR GO; GO:0005993; P:trehalose catabolic process; IMP:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001661; Glyco_hydro_37.
DR InterPro; IPR018232; Glyco_hydro_37_CS.
DR InterPro; IPR011120; Trehalase_Ca-bd.
DR PANTHER; PTHR23403; PTHR23403; 1.
DR Pfam; PF01204; Trehalase; 1.
DR Pfam; PF07492; Trehalase_Ca-bi; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS00927; TREHALASE_1; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..751
FT /note="Cytosolic neutral trehalase"
FT /id="PRO_0000173793"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT ACT_SITE 670
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 299..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 345..347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
SQ SEQUENCE 751 AA; 86425 MW; 7F380745123EBC57 CRC64;
MDDSALPSNT SNGINGRTAH RRSSSGGDPF QHPDIYYGNP ESVERIKNRR RAFSSSLKSF
NRQDFHEMLG DRNTRRGSMD PTSGNPRKFL IDVDATLHSL LEREDSDRNM QITIEDVGPK
VFSLGTAASH GYNRFDVRGT YMLSNLLQEL TIAKDYGRKQ IVLDEERLSE NPVSRLSRLI
KNSFWNSLTR RIDGRNIEVA GRDPKDWTDD PRPRIYVPPG APEQLEYYRR IAEEKPELRL
DVQELAAEIT PEYVRDLNEK PGLLALAMEE KYDEKTGKTD FAGVPFVVPG GRFNELYGWD
SYMESLGLLA SNRVDLAKAM VINFCFCIKH YGKILNANRS YYLTRSQPPF LTDMALRVYD
RIQNEPGAMD FLRHAILAAI KEYYSVWMAE PRLDPVSGLS RYRSPGIGVP PETEASHFLH
LLTPYAEKHG MEFKEFVQAY NYGKVKEPEL DEYFMHDRAV RESGHDTSYR LERVCGNLAT
VDLNSLLYKY EVDIARVIRV YFKDKLEIPV EFRTPATKDI QSESSSVWDR RARRRKMRMD
TYLWDEEKGM YFDYDTVKQE RTNYESATTL WAMWAGLVTP RQASAMITKA LPRFEEFGGI
VSGTEESRGA VGLNRPTRQW DYPYGWAPQQ MLAWTGFARY GYQEEAERLA YKWLYMITKA
FVDFNGVVVE KYDVTRPIDP HRVDAEYGNQ GVDFKGAPRE GFGWVNASYV YGLEMLNAHQ
RRALGAVTPW ETYSKAVSAQ GSDTVLENRS E
