ID A0A024GSN4_9STRA Unreviewed; 747 AA.
AC A0A024GSN4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 28-JUN-2023, entry version 26.
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=BN9_112460 {ECO:0000313|EMBL:CCI49800.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI49800.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI49800.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI49800.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCI49800.1}.
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DR EMBL; CAIX01000346; CCI49800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GSN4; -.
DR STRING; 65357.A0A024GSN4; -.
DR InParanoid; A0A024GSN4; -.
DR OrthoDB; 1329212at2759; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 82..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 86406 MW; BE2A68947AA73DE0 CRC64;
MMKMLTRLGR NPSTDIQRSD EQQRNKRTCS CPKCFLTRSY GTLSQTEQDR TCKEERMSHN
CIGSREHHMT LRSVMNSVKR HAFVIGLTMF LTISVSVLFV HTQSQIDSKP SVIKNEKFMG
SLTDLYQKII DDTKRDFLEA QQSGDTNWSQ NWLQRLDPAI TELMSLYCHG EVLHTIQMAN
VFQDSKYFVD MPIRSNSSAK LIFHDFEHRQ LSLKKFVAAH NGSKDLEKDK AEYVGLLREF
LNRHFDQPGS DMIPATPNDY QEHTLPPLIS TIKNSEYQNW AFELHQLWKH LGRIPQSSVR
GSYLHTKPED MQQEGIKSSQ YIVVVPGGRF RESYYWDSLW IITGLLISDL KETARNVVNN
LLNYVAEYGF VPNGGRIYYL TRSQPPMLSE MVKLIAQYTR NTTLTEFDLE YLSYAVPILE
KEYSFWMKEG PGGHAVTFLR RKIDENGQYS VVTHTLNRYI SQANHPRPES YREDFVIASS
MYPTANNSVN QARQDRLKKN WYNDLIAAAE SGWDFSSRWL RDGVDLRTVY TSLVLPVDLN
AFMFRMEENL RDFHIALGNR HRARFFDAAA TRRAHAIEDV LWNEKEKCWK DYDLERHSHR
MIRAASDYSP LWAKAFNMSD TQRVKDVIVS LNVSGLIQSA GVQATTTFTG QQWDAPNAWP
PEQDLIIEGL LNLNTPESNA MARDLARRWV HSGFIAWKHT GLMYEKYNAT QAGNVGYGGE
YFPQFGFGWA NGVILKYLTI HQNLLLD
//
