ID V5FUK7_BYSSN Unreviewed; 1096 AA.
AC V5FUK7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=alpha,alpha-trehalase {ECO:0000256|ARBA:ARBA00012757};
DE EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757};
GN ORFNames=PVAR5_4414 {ECO:0000313|EMBL:GAD95768.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD95768.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:GAD95768.1}.
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DR EMBL; BAUL01000137; GAD95768.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FUK7; -.
DR eggNOG; KOG4125; Eukaryota.
DR HOGENOM; CLU_006285_4_0_1; -.
DR InParanoid; V5FUK7; -.
DR OrthoDB; 1769273at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
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; 2.60.120.260; Galactose-binding domain-like; 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 Hydrolase {ECO:0000313|EMBL:GAD95768.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1096
FT /note="alpha,alpha-trehalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004733154"
FT DOMAIN 78..343
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 434..623
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
SQ SEQUENCE 1096 AA; 119238 MW; E0A68EABEFDBEDAB CRC64;
MRLTFLEWGL LASLIQSTSV SALSHDARVG RVLQRYSGPA SIERRGNAAG NSSHLYSTRF
DGVSWDQENW RLESTTLDEG HFQSRGSVAN GYIGINVASA GPFFELDVPV DGDVISGWPL
FSRRQTFATI SGFFDLQPET NGSNFPWLNQ YGGESVISGV PHWSGLILDL GNDTYLDATV
DNETISDYTT TFDYKAGLLS WSYTWKPKHA QASFNVTYRL FTHKLHVNQA VVRMEVTSSD
DTEATIANVI DGYSAVRTDF VESGEDGPAI YSAVRPWGVN NVTAYIYAVM SGSEGVNTSN
LAVTKDKPYL HTNDSSIAQS ANVKFTAGKT LSITKFVGAA SSDAFPDPRK TAKGAALKGQ
AAGYERSFRT HVSEWASVMP DGSVDDFTFP ENGTLPQDEY IIDSAISAVT NPYYLLQNTV
GKNAIRKASS TSLNSESISV GGLTSDSYAG QIFWDADTWM QPGIAASHPE AAQCITNYRI
AKYGQARENI DTAFTSSKNK THFSDSAAIY PWTSGRFGNC TGTGPCFDYE YHLNGDIGLA
FINQWVATGD DSFFKEKLFP IYDSMATTFS NLLERNGTSW TLTNMTDPDE YANHVDAGGY
TMPLIAQTLI YANAFRKKFG IEQNSTWTDM AENVLLLREN GVTLEYTTMN GTAAVKQADV
VLDTYPLNYD LGYTSQDALN DLDYYAGSQS ADGPAMTWAI FSIVASEVSP SGCSAYTYGQ
TAYVPYARAP FYQLSEQMVD DASLNGGTHP AYPFLTGSGG ANQVVLFGYL GLRLLPDNVI
HIDPDLPPQV PHVKYRTFYW RGWPISANSN YTHTTIQRAT DVPPLETADP KFANVTIPVH
VGSERNATVY RLPINGTLTV VNRQIASRNT VAGNIAQCRP VTSTSEFEPG QFPIAAVDGA
TSTKWQPSYA ANVSALTVSL TQTESNAPIS GFTFDWAQAP PVNATVILHN NSVEDPVSAF
SSTSGSSSKS DYSIVLSLHN ITLSDPYNPK TTNLDAINIP RGNSTNATLS EPVPISRFAT
LLIVGNQALS EAEVQAKNGT GATVAEWSIL AGNSTVVASD PDAEKRKLKR SAVPLGRYMR
GRRRDSLELD ERLQMI
//
