ID G3BFV6_CANTC Unreviewed; 828 AA.
AC G3BFV6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 22-FEB-2023, entry version 43.
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=CANTEDRAFT_132431 {ECO:0000313|EMBL:EGV60740.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV60740.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL996528; EGV60740.1; -; Genomic_DNA.
DR RefSeq; XP_006689954.1; XM_006689891.1.
DR AlphaFoldDB; G3BFV6; -.
DR STRING; 590646.G3BFV6; -.
DR GeneID; 18249621; -.
DR KEGG; cten:CANTEDRAFT_132431; -.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_1_1_1; -.
DR OrthoDB; 1329212at2759; -.
DR Proteomes; UP000000707; 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; 1.
DR Pfam; PF07492; Trehalase_Ca-bi; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00927; TREHALASE_1; 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:UP000000707}.
FT DOMAIN 170..199
FT /note="Neutral trehalase Ca2+ binding"
FT /evidence="ECO:0000259|Pfam:PF07492"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 95095 MW; 07C350506484D6E6 CRC64;
MSDSQHKRTH SSSSEFDPFE DPEDYYSNKN VSMNRARTFS VFESSSTKFS PYSDDPISER
SHENTPTPSD SLSSTPAPEV SDKNVPVPML QSDSSGSSRS EESSNFAKRP SIVPVYDESF
SSTSELTKTE EEVKEVNERI KQLHLRRSSW DDNMYRRPKK FYIPDVDTTL TQLLNNEDTD
HNCQITIEDT GPKVLKLGTA NSNGYKQFDI RGTYMLSNLL QELTIAKRLG KKHLVLDEQR
LSENPVFRMK RLISTQFWKN LTRQMTKNTI MEMAKDTKIP EEYINEKGEK VAARETHRIY
VPHNRADQFE YFMSIKKTNT DANLDVQYLP EVIDAKFIRS INKKPGLLAL QSRPDPNDPN
NLINEPYVVP GGRFNELYGW DSYMESLGLL VDVTPTNTTN LDLAKGMTEN FIYEINHYGK
VLNANRSYYL GRSQPPFLTD MALRVFNKLM EVRPEATEES LKFLERAVKA AIIEYKTIWT
AKPRYDDATG LSCYHPEGLG VPPETESSHF VEVLKPYTEK YNVSHEEFIE LYNSEKIKEP
ALDEYFLHDR AVRESGHDTS YRLEGKCAYL ATVDLNSLLY KYEVDIAFMV ETYFHNSLQV
NGVVETKSSW LERATIRKQN ITKYLWNEKD GIFYDYHIKN HTQTGYESAT TFWPLWSKAA
SPEQASRLVK QSLHKFEEFG GLVAGTEASR GAVNLSRPSR QWDYPYGWAP QQILAWIGLA
NYGFDGDARR LIYRWLYLMT KAFADYNGVV VEKYNVVKGA TPHKVDAEYG NQGADFKGVA
TEGFGWVNAS YMFGLTFLNV HAIRNIGALM PPDVFLANMH PDQRQLYE
//
