ID Q9BLC8_ARTSF Unreviewed; 703 AA.
AC Q9BLC8;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 22-FEB-2023, entry version 50.
DE RecName: Full=Trehalase {ECO:0000256|ARBA:ARBA00019905, ECO:0000256|RuleBase:RU361180};
DE EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757, ECO:0000256|RuleBase:RU361180};
DE AltName: Full=Alpha-trehalose glucohydrolase {ECO:0000256|RuleBase:RU361180};
OS Artemia franciscana (Brine shrimp) (Artemia sanfranciscana).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Anostraca; Artemiidae; Artemia.
OX NCBI_TaxID=6661 {ECO:0000313|EMBL:BAB40813.1};
RN [1] {ECO:0000313|EMBL:BAB40813.1}
RP NUCLEOTIDE SEQUENCE.
RA Tanaka S., Namubu F., Namubu Z.;
RT "Cloning and characterization of cDNAs encoding trehalase from post-dormant
RT embryos of the brine shrimp, Artemia franciscana.";
RL Zool. Sci. 16:269-277(1999).
RN [2] {ECO:0000313|EMBL:BAB40813.1}
RP NUCLEOTIDE SEQUENCE.
RA Tanaka S., Nambu Z., Nambu F.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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; AB059269; BAB40813.1; -; mRNA.
DR AlphaFoldDB; Q9BLC8; -.
DR SMR; Q9BLC8; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0005991; P:trehalose metabolic 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 PANTHER; PTHR23403; TREHALASE; 1.
DR PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR Pfam; PF01204; Trehalase; 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 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..703
FT /note="Trehalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004324216"
FT REGION 647..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 242..269
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 647..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 79997 MW; E3A8922D8BCF4174 CRC64;
MCAFLSFFVV FGFATTVSCR GDLVLSERAK QLPPVCASEI YCHGTFLHTI QMAGLFRDSK
TFVDKKLKIN PEEVLASFEV LMNSTDQNPS RDQLAAFINL HFEPEGSEFE EWDPIDWHSN
PSFLDGIRDT NLKIWGNSLH EAWTWLGRKI RDDVRINPQL YSMMYLPNPF IIPGGRFRET
YYWDSYWIIK GLLISGMHET VKGMLLNFLL MVDTIGLVPN GGRIYYEKRS QPPLLTPMVE
LYVNASGDIE FLKQNIHLLE KEMDFWLQER TVNVDGHRLI RYDVKVGGPR PESYKEDIEA
IHHNPDLEAQ LDFYMNIAAG AETGWDFSSR WYWNGDIQTN LSHVRTRDIL PVDLNSFIAW
DFDIMSRFEK QLGRDNASVV YSDLYSEWKT SINAILWDDE AGSWFDYDSA HRRWNTNFYV
SNLTPLFVGC YDPKTVHHED VATRVLDYLE KSNALKFPGG VPTSLMQTSQ QWDFPNGWPP
LQHMLVMGLD KTGDPRAKEL AFDLAQRWVF NNYEAFTQSL PNAMFEKYDV TVVGLPGGGG
EYDVQLGFGW TNGVVMDFLV KYGERLTSVR DAKQLIWSPS SVSVGVGAGA TFLGAWIGLA
STRFYRQLFK SDHKMGGIHG VAEAIQGLIA CVGSLLVATA ALFSEKDTTK RPTSGQTPQS
SPIRRTKSLP GFLLFQRGSK GDEEHLLRNR AISEECSYSS IEE
//
