ID A0A094D5Y7_9PEZI Unreviewed; 1193 AA.
AC A0A094D5Y7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 29.
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=V496_05587 {ECO:0000313|EMBL:KFY59633.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY59633.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY59633.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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:KFY59633.1}.
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DR EMBL; JPJY01001026; KFY59633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094D5Y7; -.
DR STRING; 1420909.A0A094D5Y7; -.
DR HOGENOM; CLU_271597_0_0_1; -.
DR OrthoDB; 1329212at2759; -.
DR Proteomes; UP000029302; 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:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 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; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011120; Trehalase_Ca-bd.
DR PANTHER; PTHR23403:SF6; CYTOSOLIC NEUTRAL TREHALASE-RELATED; 1.
DR PANTHER; PTHR23403; TREHALASE; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF01204; Trehalase; 1.
DR Pfam; PF07492; Trehalase_Ca-bi; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SMART; SM00702; P4Hc; 1.
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 Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302}.
FT DOMAIN 932..1173
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 135870 MW; 9A300AED65DA09B0 CRC64;
MSTTDGNKPK ESNGNGTPNE PRRISIEIDQ FAPAETYYGL KNTAHQNPRR QSTFSTNYAA
SRVREDTLSE LPARRGSHDE STLGQLKFLI NVDSTLENLQ KQEDTDNNFQ ITIEDNGPKV
ISLGTVTSNG FRRHDIRGTY MLSNLLQELS LAKEAGRHMI VLDESRLNEN PVSRLSRLIK
DTFWDRLTRR IDGHVIEIAG KDPKDWTDDP RPRVYIPRGA PEQFEYYTQV AKDRPEVRLD
VQWLPEKITP ESVRDMNAKP GLLALAMEEY RDPSTQKMTL RGVPFVVPGG RFNELYGWDS
YMESLGLIVN GRVDLAKAMV TNFCFCIKHY GKILNANRSY YLCRSQPPFL TDMASRVYDK
IQHEKGAREF LRLATLAAIK EYRSVWIAEP RLDSITGLSR YRPEGLGVPP ETEASHFIHI
LEPYAKKHNL SFDAFVEAFN NRVILEPELD DYFMHDRAVR ESGHDTSYRL ERTCADLATI
DLNSLLYKYE VDIARIIRVH FDDKLAVPAE FCTGNMVPGQ LETSALWDRA SRARKKAINK
YLWNEEKGMF FDYNTVSQQQ QTYESATTFW AMWAGLATPK QGEQMVAQAI PILEAAGGLL
SGTRHSRGEI GIERPNRQWD YPYGWAPQQM LAWTGLQRYG HQDVAERLAY KWLYMITKAF
VDYNGVVVEK YDVTRPVDPH RVDAEYGNQG SDFKGVAKEG FGWVNASYVY GMQICNVHMR
RALGTCTPYE TYRKMTEHGQ ISLRSRWTYG SRWLHYYSAN GSGGEWMGDG GEREESAQEQ
AHPQSQAIDP ASPIQTSTME DRAAAFAFRG FRMLISGGEN ATTMTRKVQE DRESSDNNPR
QREGGRRCSL LLVVLHSTLH TPFKSATMST ILQKTRNKAN QDGVVTQLIR TNYTSSPVSI
PDDFLAPLAD PSSITVSQID FANTELPEYK GHYAVVLDNV LSPQECEELI HLVEQSAGAH
GDDETVENNG WKPAMVNAGS NKEFLALDYR NSDRIIWDNE VIMQRLWTRI VEAQGMREHH
SVLEGNRYAN VMGMLAVRRG DRWVFSRKGP NERMRFLKYG AGQFFRPHCD GTYETPDGQQ
RSFYTLHLYL NDSAQALGIK EPKPDLQKKE GKTGLEDEML RGGATTFHSY NERRRLDVDP
KAGRVLIFQQ RNLFHSGDDV TAGIKYTMRS DLMYEFENKG GNEGDSDGDI TFA
//
