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
//