ID K0KH76_WICCF Unreviewed; 1021 AA.
AC K0KH76;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=alpha,alpha-trehalase {ECO:0000256|ARBA:ARBA00012757};
DE EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757};
GN Name=ATH1 {ECO:0000313|EMBL:CCH44570.1};
GN ORFNames=BN7_4136 {ECO:0000313|EMBL:CCH44570.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH44570.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH44570.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
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:CCH44570.1}.
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DR EMBL; CAIF01000143; CCH44570.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KH76; -.
DR STRING; 1206466.K0KH76; -.
DR eggNOG; KOG4125; Eukaryota.
DR HOGENOM; CLU_006285_4_0_1; -.
DR InParanoid; K0KH76; -.
DR Proteomes; UP000009328; 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:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:CCH44570.1};
KW Hydrolase {ECO:0000313|EMBL:CCH44570.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..357
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 418..635
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
SQ SEQUENCE 1021 AA; 114852 MW; D451E72283F51C55 CRC64;
MPIIEKDKSR NNESRQPKTK RRKTILFSMT LLFPTLLVLL AFVPTVVLNT VSPFDQDDEK
ARWLKMFEKS EKLFRQVPDS GNAFYDERNN ILGHTHFSKN VYSRQAYVSN GYIGARLSTL
GQGFTYDQFN IHANSMDEEF LKNGWPLFNK RYTGAFVSGF FDLEPELPDT NFPELYANGS
DSVISAIPYW PVLQLHATIG GQHYIFDPQQ TFDNDVTNYV QNLSLQNGIV STRLTWLNKV
NVKINVMAHK QIAPLGLISM ELSAVDEDVE MIVQDQLNLT TAQRSVLQDI GVDDLGIYMQ
VTPNNIDYSR VAVYSRLDLN DTHSYVDEEG QTVINEHHFT LTKEKFKITK YAGIISTEYQ
ERGTGSELEN AKKIVDFAQS VGLQQLYDSH NHEWDEQFKE TNIYIPGSGF LTLAARSSLY
HLYANTRIGT RDLTSALGTT GLSSDSYGGM TFWDTDLWIV PAILPFAPQV AKCISQYRNF
THNQAIENAQ EYGFEGAAYP WTSGRFGNCT STGPCVNYEY HLNVDIAYSS WLIYLASGDE
EYLRYTAWPI LRDASNFLTD YVTFNTTLNQ FTTHNLTDPD EYANHVDNGA FTNAGIDSLM
KWTLMAASHL GEPINPKWAK VNDNVYIPRS EDGITLEYIG MNASVSIKQA DVVLLTFPLD
FNDHHSYEDA ERDLYYYSIK QADVGPAMTF PVFSIASAKL LNKGCSVHSY LQKSVLPYLR
APFAQFSEQA DDNTATNGGT NPAFPFMTGH GGYLQALVYG VHGLRFSVKL TPDGKLDRFL
TFDPIAISGL PGGVKISGFK YSNQLLDVIV TDIEGIIIHK GDDPIEIEVR ERNPKTGRYT
LQPGEKLKVP LFVPGMNIDG STVECKPITN LTVGVPGDVP LSAIDGNNYT YWQPLDREPA
RLLIDLGFPQ KLSKGLIIWG ERPAKTLSIY GTEEISLDME EAFMNIENIK FTSLVDKLDI
ETSEPYKEEY SKDIKLLPNN ITEFEIGNNT LFTKFIIVEI TDALDPQEPS GATVNEVALF
Q
//
