ATC1_ARTBC
ID ATC1_ARTBC Reviewed; 1054 AA.
AC D4B5H9;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Cell wall acid trehalase ARB_03719 {ECO:0000305};
DE EC=3.2.1.28 {ECO:0000250|UniProtKB:Q5AAU5};
DE AltName: Full=Alpha,alpha-trehalase {ECO:0000250|UniProtKB:Q5AAU5};
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000250|UniProtKB:Q5AAU5};
DE Flags: Precursor;
GN ORFNames=ARB_03719;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Cell wall acid trehalase that catalyzes hydrolysis of the
CC disaccharide trehalose and required for growth on trehalose as carbon
CC source (By similarity). Plays a role in virulence (By similarity).
CC {ECO:0000250|UniProtKB:Q5AAU5}.
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:0000250|UniProtKB:Q5AAU5};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}. Secreted,
CC cell wall {ECO:0000250|UniProtKB:Q5AAU5}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; ABSU01000041; EFE29423.1; -; Genomic_DNA.
DR RefSeq; XP_003010063.1; XM_003010017.1.
DR AlphaFoldDB; D4B5H9; -.
DR SMR; D4B5H9; -.
DR STRING; 663331.D4B5H9; -.
DR EnsemblFungi; EFE29423; EFE29423; ARB_03719.
DR GeneID; 9525659; -.
DR KEGG; abe:ARB_03719; -.
DR eggNOG; KOG4125; Eukaryota.
DR HOGENOM; CLU_006285_4_0_1; -.
DR OMA; WPLFSRR; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
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 1: Evidence at protein level;
KW Cell wall; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1054
FT /note="Cell wall acid trehalase ARB_03719"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434664"
FT REGION 950..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 586
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 450..451
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 654..655
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1004
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1054 AA; 114794 MW; AEA6EAA96DD7D914 CRC64;
MKQPNINLAA CILWLLSIIT AVAAETDAER NTGVFARNSA ARNRSPGNEP PGYATRFKGV
TWDVANWRLT TTELDQGHYQ SRGSVANGYL GINVAAVGPF FELDIPVSGD VINGWPVFSR
RQTFATISDF YSFQRSINAT NFPWLDKYGG DLISGVPHWS GLILDLGDGN FLDATVKNST
ISNFSSTLDM KGGILTWQYT WSPEKHNGTY DIFYQLVAHK LHVNQALVRL EITPSRDGNV
SVVNVIDGYS AVRTDFKGSG QDGSAIYTSV NPEGISNVTA FIYAELSGTE GVDLSSSSLV
DDKPYIHMNG STIAQSVNVK LRAGQTTKID KFVGAASTDG FKNPRQAAKE ASARALRTGY
EESLKSHIAE WATVFPSDST EDYTIPGKKW LPLDHHIIEA SIVSVVNPYY LLQSTVSNNA
LAAVKNAPLN RGSIAVGGLT SDSYGGLVFW DADIWMQPGL VVAFPEASQI FSNYRVDKYG
QALRNAQTQH LSSKNDTYFS PDAAVYPWTS GRFANCTATG PCFDYQYHLN GDIGMQIVNN
WVTTGDTEHF KSKLFPVYNS IATFFSQLVE KNGTKWTVTN MTDPDEYANL VDGGGYTMPL
IATTLKYANQ FREMFGIGAN QTWNEIAQNV QVSRDQASQI TLEYTTMNGS TQVKQADIVL
NTFPLHYTED YTHDNALRDL DYYAAKQSPN GPAMTYAIFS IVANEVSPSG CSAYTYGQYS
FSPYVRAPFF QFSEQLMDDW SINGGTHPAY PFLTGNGGAN QVAVFGYLGL RLIPDGILHL
NPNLPPQIPH LRYRTFYWHG WPLEASANYT QTTIQRATNR RPLTSADPKY ASAPITVHVG
PANNITVYSL PPSGQLVIPN RQIGSISTVP GNLVQCQPVF SPNEFAPGQF PISAVDGAAS
TKWQPRRASS TSSLTVTLPD HASSATISGF AFDWAQAPPV SAKVVLHDEP LHPVTDPENG
DASGSSPTTP ASSVTVWESA KVPLSDPYDP IKIDLNMIMS YKGNTTNVTL PSTVPATKFA
TLLIRGNQAL GPVEVRAGNG TGATVAEWSI VRSS
