ID A6RB45_AJECN Unreviewed; 658 AA.
AC A6RB45;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
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_06183 {ECO:0000313|EMBL:EDN10380.1};
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:EDN10380.1, 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|ARBA:ARBA00001576,
CC 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; CH476661; EDN10380.1; -; Genomic_DNA.
DR AlphaFoldDB; A6RB45; -.
DR STRING; 339724.A6RB45; -.
DR VEuPathDB; FungiDB:HCAG_06183; -.
DR HOGENOM; CLU_006451_1_1_1; -.
DR OMA; ESATAYW; -.
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; IPR018232; Glyco_hydro_37_CS.
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.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 93..122
FT /note="Neutral trehalase Ca2+ binding"
FT /evidence="ECO:0000259|Pfam:PF07492"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 75713 MW; 756ED4832017013F CRC64;
MSVPVDEHSL CAHRRRSSRS SDADPFSEPD VYYGQEEHLK QHAQAHRRTL SSSLKRFDLT
DLRDFIGNVP SRRTSHDERV QSRKFIIDVD ATLETLLERE DTDHNVQITI DDQGPKVFAV
GTAASNGYNR FDLRGTYMIS NLLQELTLAK DYGRKHIILD EQRLNENPVT RLSRLIKKCY
WNALTRRIDG SNIVAVAADP KDWTADPVPR IYVPPGAPEQ YEYYKRIADA QPELRLDVQY
LPEGGPTAEY ILNANRSYYL CRSQPPFLTD MALRVYDRIK ADPSAKDFLR TAILSAIKEY
YSVWMVEPRY DPITGLSRYR PTGLGVPPET ESSHFYHLLM PHAKKLGISF EEFVQGYNNG
QIKDPELDDY FLHDRAVRES GHDTSYRLEK VCANLATVDL NSLLYKYEVD IARTIRDFFG
DKLSIPTEFR TPQNAEHGFE SSAVWDRRAR RRKAAMDKYL WDEGKGTYFD YNTVEQERTD
YESATTFWTM WAGVASPYQA SRLVNEALPK FEAYGGLVSG TEKSRGPIGL DRPNRQWDYP
YGWAPQQMLA WSGLIRYGYQ DEAERLAYKW LYMIIKAFVD FNGAVVEKYD VTRPIDPHKV
EAEYGNQGGD FKGVSREGFG WVNASFVYGL EFLNAHMRRA LGACTPYETF SKATAVQY
//