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Database: UniProt
Entry: A0A180GY49_PUCT1
LinkDB: A0A180GY49_PUCT1
Original site: A0A180GY49_PUCT1 
ID   A0A180GY49_PUCT1        Unreviewed;      1064 AA.
AC   A0A180GY49;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=alpha,alpha-trehalase {ECO:0000256|ARBA:ARBA00012757};
DE            EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757};
GN   ORFNames=PTTG_12539 {ECO:0000313|EMBL:OAV96933.1};
OS   Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV96933.1};
RN   [1] {ECO:0000313|EMBL:OAV96933.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV96933.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAV96933.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV96933.1};
RA   Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA   Young S., Zeng Q., Fellers J.;
RT   "Comparative analysis highlights variable genome content of wheat rusts and
RT   divergence of the mating loci.";
RL   Submitted (MAY-2016) 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   -!- 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:OAV96933.1}.
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DR   EMBL; ADAS02000016; OAV96933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A180GY49; -.
DR   STRING; 630390.A0A180GY49; -.
DR   VEuPathDB; FungiDB:PTTG_12539; -.
DR   OrthoDB; 1769273at2759; -.
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   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           43..1064
FT                   /note="alpha,alpha-trehalase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008110415"
FT   DOMAIN          79..335
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          430..647
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   REGION          1006..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1064 AA;  118619 MW;  AF0E183923C583BF CRC64;
     MEVSENEFIP FPGPSGPAAP LMTTRPPLLL VWLLIAHSLC SGSPESYTNS TDIVYPTRFR
     GVEWDNEQWK LSTTLLEPGR YQSRISLANG YLGINLAALG PFFEKDNQSL NGWPVLDRRQ
     SFATIAGFYD SQPKLNSSNF PWLDQYGGES IISGVPHWAG LLVKTEAATL DASTDPRSIK
     NFHSALDLRT GLMKWKFEWV IDGQPEISIE YTMFVHKLHV NRAAVQLELK AVSDFELSVI
     DLLDGDCAAR TDFVEKRYHS SSSTICSAVR PNGMANVTGH VCSSLRSEAF SQSYLLKGSP
     TPSSSASPST IAQSARIKLK REQTVAVQKF IGAASGDAFS DPHTVALQSA IAGAKDGFSS
     QLDSHRREWS SIMTKESVDD YALAQYDPST IDPNIVELQI LAITNPFHLL QNTISSNAIA
     LANTSSALDN WSISVCGLGS SCYGGMIFWD AEVWMAPGLV LSHPHAAQRI INYRVAQFPQ
     AQDNIKMAFS SSQNRTNQFS PDDAIYPWTS GRFGNCTASG PCFDYEYHIN GDIGLSFFHH
     LVVTGNFEYF KRHLWPIYQA IAGLFSNLLS ETSTHKYALR NATDPDEYAN HVDNPAYTMF
     LIKHHLTTAN ELRGRVGQKP KPTWLKQANN LALPIDDQSG IILEYEGMNS SIVVKQADVV
     LIDDFLDFPN PHRLENLEYY GTKQSLNGPG MTYGVYSVVE NRFQISGCSS YTYHLFSSQP
     YIRAPWFQFS EQLVDDYSQN GGIHPAFPFL TGMGGDYRVT VYGYLGLRLE LDHLSVDPSL
     PPQIASLSYR KIYWHGYPIR AKSNQTHTSL FRPPSGALAD ADPDYAEAPI PVKHRSSGRI
     LKLGRARTVT VPNRPVYLAN PIQCAPIKSD QAFLPGQFPL SILDGSSATR WIPSDLPATV
     TVPLNEHFRA KQIIGFGFQS SNFTDFRIRF FDDPGQRTAL STYSSFNGTH VGFHPFVGLD
     DHDDHDHQQK ISQKDHGWSF YRFDQPIGFS KYANLTVFDT DQIQSAHPES FHTQDSRPKN
     QHTSQRNSKS LGMAQWTLLT SHHHSSRTPE SHNRNSGQTL IELL
//
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