TREA_EMENI
ID TREA_EMENI Reviewed; 1054 AA.
AC P78617; C8VR42; Q5AQU0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Acid trehalase;
DE EC=3.2.1.28;
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE Flags: Precursor;
GN Name=treA; ORFNames=AN9340;
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].
RX PubMed=9140977; DOI=10.1046/j.1365-2958.1997.3131693.x;
RA d'Enfert C., Fontaine T.;
RT "Molecular characterization of the Aspergillus nidulans treA gene encoding
RT an acid trehalase required for growth on trehalose.";
RL Mol. Microbiol. 24:203-216(1997).
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 -!- 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF87435.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA66407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U75428; AAB57642.1; -; Genomic_DNA.
DR EMBL; AACD01000172; EAA66407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001308; CBF87435.1; ALT_SEQ; Genomic_DNA.
DR PIR; T18304; T18304.
DR RefSeq; XP_682609.1; XM_677517.1.
DR AlphaFoldDB; P78617; -.
DR SMR; P78617; -.
DR STRING; 162425.CADANIAP00001124; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR CLAE; TRE65A_EMENI; -.
DR PRIDE; P78617; -.
DR EnsemblFungi; EAA66407; EAA66407; AN9340.2.
DR GeneID; 2867940; -.
DR KEGG; ani:AN9340.2; -.
DR VEuPathDB; FungiDB:AN9340; -.
DR eggNOG; KOG4125; Eukaryota.
DR HOGENOM; CLU_006285_4_0_1; -.
DR InParanoid; P78617; -.
DR OrthoDB; 125022at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0031160; C:spore wall; IDA:AspGD.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IMP:AspGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0005993; P:trehalose catabolic process; IMP:AspGD.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1054
FT /note="Acid trehalase"
FT /id="PRO_0000012109"
FT ACT_SITE 584
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 448..449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 650..651
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 992
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1054 AA; 115111 MW; B2B26466CA0992F1 CRC64;
MRFKSVFTLL PLLAQLPSGG ASLPNNHGRV ENCVRNHDGI HKFRHSNNTY QSMFPGVTWD
EDQWVLTTSS LDQGHYQSRG SVANGYIGIS VSSVGPFFEL DLPVAGDVIN GWPLYSRRQS
FATISGFFDI QAETNGSNFP WMNQYGGESV ISGVPHWSGL ILDLGDDDYL DSTVDNVTLS
DFKSSYDFKA GVLSWSYTWT PAGDKGSYAI TYRLFANKLN VNQAVVDMEI TPSQDGHATI
VNVLDGYSAV RTDFVESQED DGAIYSAVRP WGIPDVSAYF YANITGSKHV DLSSRRLIHG
KPYVSANESS IAQAADVNFV ANEKVRITKF VGAASTDAFP DPQATAKRAV SEALDAGYQR
SLRSHVQEWA SIMHEDSVDR YVNPTTGKLP DDDNIINSAI IAVANTYYLL QNTVGKNAIR
AAQDAPLNVN SFSVGGLVSD SYAGLVFWDA DVWMQPGLVA SHPEAAQAVT NYRTKLYPQA
KKNIETTYTG SKNATYIDPS AAIYPWTSGR FGNCTGTGAC WDYQYHLNGD IGLSLIYQWV
VSGDTNTFRE KHFPIYDSVA ALYGSIVERN GSYWTLTNMT DPDEYANHID AGGFTMPMIS
ETLEYANQFR QQFGLEPNET WTEISENVLV LRENGVTLEY TTMNGTAAVK QADIVLVTYP
LVYDNYTAET ALTDLDYYAN RQSADGPAMT WAIFSIAAGA VSPSGCSAYT YHQYSYAPYA
RAPFFQLSEQ MLDNASINGG THPAYPFLTG HGGANQVVLF GYLGLRLLPD DAIHIEPNLP
PQIPYVKYRT FYWRGWPISA QSNYTHTVLQ RSQSAPLDTA DRRFANTSIP VFVGLADNAT
LHHLPPHGPL TVRNREIGTI NTIEDNLIQC SPVSSTDAFE QGQFPISVVD GATSTRWQPS
SSNASAVTVN LGSTTGRSVQ TVASGFHFDW AAAPPVNASV IFHDTPLSDP VAALSSPGPH
VRIVANLTNI EQSGPYDPEA TDLNEIKIPV GNTTRIELAQ EVPVGRYATL VISGNQALAQ
ADGEDHVGAT VAEWAILGPK SGSPRRRIQP VPLL
