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Protein

Acid trehalase

Gene

treA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose.

GO - Molecular functioni

  • alpha,alpha-trehalase activity Source: ASPGD
  • carbohydrate binding Source: InterPro

GO - Biological processi

  • cellular response to desiccation Source: EnsemblFungi
  • cellular response to ethanol Source: EnsemblFungi
  • cellular response to freezing Source: EnsemblFungi
  • trehalose catabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH65. Glycoside Hydrolase Family 65.
mycoCLAPiTRE65A_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid trehalase (EC:3.2.1.28)
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
Gene namesi
Name:treA
ORF Names:AN9340
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome VIII
  • UP000005890 Componenti: Partially assembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AN9340.

Subcellular locationi

GO - Cellular componenti

  • cell wall-bounded periplasmic space Source: EnsemblFungi
  • extracellular region Source: ASPGD
  • fungal-type cell wall Source: EnsemblFungi
  • fungal-type vacuole Source: EnsemblFungi
  • spore wall Source: ASPGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 10541033Acid trehalasePRO_0000012109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence analysis
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence analysis
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence analysis
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence analysis
Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence analysis
Glycosylationi513 – 5131N-linked (GlcNAc...)Sequence analysis
Glycosylationi570 – 5701N-linked (GlcNAc...)Sequence analysis
Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence analysis
Glycosylationi618 – 6181N-linked (GlcNAc...)Sequence analysis
Glycosylationi644 – 6441N-linked (GlcNAc...)Sequence analysis
Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence analysis
Glycosylationi734 – 7341N-linked (GlcNAc...)Sequence analysis
Glycosylationi803 – 8031N-linked (GlcNAc...)Sequence analysis
Glycosylationi826 – 8261N-linked (GlcNAc...)Sequence analysis
Glycosylationi838 – 8381N-linked (GlcNAc...)Sequence analysis
Glycosylationi903 – 9031N-linked (GlcNAc...)Sequence analysis
Glycosylationi937 – 9371N-linked (GlcNAc...)Sequence analysis
Glycosylationi966 – 9661N-linked (GlcNAc...)Sequence analysis
Glycosylationi992 – 9921N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP78617.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 65 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000178675.
InParanoidiP78617.
OrthoDBiEOG76MKHN.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.70.98.40. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR011013. Gal_mutarotase_SF_dom.
IPR005195. Glyco_hydro_65_M.
IPR005196. Glyco_hydro_65_N.
[Graphical view]
PfamiPF03632. Glyco_hydro_65m. 1 hit.
PF03636. Glyco_hydro_65N. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF74650. SSF74650. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P78617-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFKSVFTLL PLLAQLPSGG ASLPNNHGRV ENCVRNHDGI HKFRHSNNTY
60 70 80 90 100
QSMFPGVTWD EDQWVLTTSS LDQGHYQSRG SVANGYIGIS VSSVGPFFEL
110 120 130 140 150
DLPVAGDVIN GWPLYSRRQS FATISGFFDI QAETNGSNFP WMNQYGGESV
160 170 180 190 200
ISGVPHWSGL ILDLGDDDYL DSTVDNVTLS DFKSSYDFKA GVLSWSYTWT
210 220 230 240 250
PAGDKGSYAI TYRLFANKLN VNQAVVDMEI TPSQDGHATI VNVLDGYSAV
260 270 280 290 300
RTDFVESQED DGAIYSAVRP WGIPDVSAYF YANITGSKHV DLSSRRLIHG
310 320 330 340 350
KPYVSANESS IAQAADVNFV ANEKVRITKF VGAASTDAFP DPQATAKRAV
360 370 380 390 400
SEALDAGYQR SLRSHVQEWA SIMHEDSVDR YVNPTTGKLP DDDNIINSAI
410 420 430 440 450
IAVANTYYLL QNTVGKNAIR AAQDAPLNVN SFSVGGLVSD SYAGLVFWDA
460 470 480 490 500
DVWMQPGLVA SHPEAAQAVT NYRTKLYPQA KKNIETTYTG SKNATYIDPS
510 520 530 540 550
AAIYPWTSGR FGNCTGTGAC WDYQYHLNGD IGLSLIYQWV VSGDTNTFRE
560 570 580 590 600
KHFPIYDSVA ALYGSIVERN GSYWTLTNMT DPDEYANHID AGGFTMPMIS
610 620 630 640 650
ETLEYANQFR QQFGLEPNET WTEISENVLV LRENGVTLEY TTMNGTAAVK
660 670 680 690 700
QADIVLVTYP LVYDNYTAET ALTDLDYYAN RQSADGPAMT WAIFSIAAGA
710 720 730 740 750
VSPSGCSAYT YHQYSYAPYA RAPFFQLSEQ MLDNASINGG THPAYPFLTG
760 770 780 790 800
HGGANQVVLF GYLGLRLLPD DAIHIEPNLP PQIPYVKYRT FYWRGWPISA
810 820 830 840 850
QSNYTHTVLQ RSQSAPLDTA DRRFANTSIP VFVGLADNAT LHHLPPHGPL
860 870 880 890 900
TVRNREIGTI NTIEDNLIQC SPVSSTDAFE QGQFPISVVD GATSTRWQPS
910 920 930 940 950
SSNASAVTVN LGSTTGRSVQ TVASGFHFDW AAAPPVNASV IFHDTPLSDP
960 970 980 990 1000
VAALSSPGPH VRIVANLTNI EQSGPYDPEA TDLNEIKIPV GNTTRIELAQ
1010 1020 1030 1040 1050
EVPVGRYATL VISGNQALAQ ADGEDHVGAT VAEWAILGPK SGSPRRRIQP

VPLL
Length:1,054
Mass (Da):115,111
Last modified:May 1, 1997 - v1
Checksum:iB2B26466CA0992F1
GO

Sequence cautioni

The sequence CBF87435.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA66407.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75428 Genomic DNA. Translation: AAB57642.1.
AACD01000172 Genomic DNA. Translation: EAA66407.1. Sequence problems.
BN001308 Genomic DNA. Translation: CBF87435.1. Sequence problems.
PIRiT18304.
RefSeqiXP_682609.1. XM_677517.1.

Genome annotation databases

EnsemblFungiiCADANIAT00001124; CADANIAP00001124; CADANIAG00001124.
EAA66407; EAA66407; AN9340.2.
GeneIDi2867940.
KEGGiani:AN9340.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75428 Genomic DNA. Translation: AAB57642.1.
AACD01000172 Genomic DNA. Translation: EAA66407.1. Sequence problems.
BN001308 Genomic DNA. Translation: CBF87435.1. Sequence problems.
PIRiT18304.
RefSeqiXP_682609.1. XM_677517.1.

3D structure databases

ProteinModelPortaliP78617.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH65. Glycoside Hydrolase Family 65.
mycoCLAPiTRE65A_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00001124; CADANIAP00001124; CADANIAG00001124.
EAA66407; EAA66407; AN9340.2.
GeneIDi2867940.
KEGGiani:AN9340.2.

Organism-specific databases

EuPathDBiFungiDB:AN9340.

Phylogenomic databases

HOGENOMiHOG000178675.
InParanoidiP78617.
OrthoDBiEOG76MKHN.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.70.98.40. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR011013. Gal_mutarotase_SF_dom.
IPR005195. Glyco_hydro_65_M.
IPR005196. Glyco_hydro_65_N.
[Graphical view]
PfamiPF03632. Glyco_hydro_65m. 1 hit.
PF03636. Glyco_hydro_65N. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF74650. SSF74650. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the Aspergillus nidulans treA gene encoding an acid trehalase required for growth on trehalose."
    d'Enfert C., Fontaine T.
    Mol. Microbiol. 24:203-216(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiTREA_EMENI
AccessioniPrimary (citable) accession number: P78617
Secondary accession number(s): C8VR42, Q5AQU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: April 13, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.