ID A6R7G6_AJECN Unreviewed; 463 AA.
AC A6R7G6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Trehalase {ECO:0000256|RuleBase:RU361180};
DE EC=3.2.1.28 {ECO:0000256|RuleBase:RU361180};
DE AltName: Full=Alpha-trehalose glucohydrolase {ECO:0000256|RuleBase:RU361180};
GN ORFNames=HCAG_05574 {ECO:0000313|EMBL:EDN09075.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN09075.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(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 Evidence={ECO:0000256|RuleBase:RU361180};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC {ECO:0000256|ARBA:ARBA00005615, ECO:0000256|RuleBase:RU361180}.
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DR EMBL; CH476659; EDN09075.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R7G6; -.
DR STRING; 339724.A6R7G6; -.
DR VEuPathDB; FungiDB:HCAG_05574; -.
DR HOGENOM; CLU_590463_0_0_1; -.
DR OrthoDB; 1329212at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
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; IPR011120; Trehalase_Ca-bd.
DR PANTHER; PTHR23403:SF6; CYTOSOLIC NEUTRAL TREHALASE-RELATED; 1.
DR PANTHER; PTHR23403; TREHALASE; 1.
DR Pfam; PF01204; Trehalase; 2.
DR Pfam; PF07492; Trehalase_Ca-bi; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|RuleBase:RU361180};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 52..81
FT /note="Neutral trehalase Ca2+ binding"
FT /evidence="ECO:0000259|Pfam:PF07492"
SQ SEQUENCE 463 AA; 52423 MW; DB0593B1CC37E0BA CRC64;
MKENTPLTAP LDDHGFSHAI RELRKSSSIH ITDSADEGSL PPVFKVWVDN AMESLLEQED
TDKNLQITIL DNGPKVVSLG TFLSDGGRTR EIRGTYLLAN LLEELHLTKG RLASKMIHFH
CVSKNRYFAC LGLLELGRLD LVRDILYNFI FQVKHYGKIP NANRSYYLCR SQPPFLSDLA
VRTFKSIDNK EEAAAVLRAG ILAAIKEYFT VWMSEPRYDP TTGLSRFKPP GKGIPLEVEE
GHFDAVLYSY AEKYACTIPE FIDQYNFGNV NEPELDEYFM HDRGVRESGH DTSYRFDQGC
ADLATVDLNC LLYKYESDIA WAIKNVFNDK LPIPAEWRTP ETHYLRIRNN PLPATGAASP
AANKPTPSVT RALPKFECVG GLSNQLVYRW LQLMVRVAVN YHGAIVEKYD VTQLDNPSQV
DAEYGNQGLD FKYANVEGHR KLMVKALGLC VPYDDLRMEN AHI
//
