ID   TPS2_ZYGRO              Reviewed;         900 AA.
AC   Q9P4D3;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Trehalose-phosphatase {ECO:0000305};
DE            EC=3.1.3.12 {ECO:0000305|PubMed:12748054};
DE   AltName: Full=Trehalose-6-phosphate phosphatase {ECO:0000303|PubMed:12748054};
DE   AltName: Full=ZrTPS2 {ECO:0000303|PubMed:12748054};
GN   Name=TPS2 {ECO:0000303|PubMed:12748054};
OS   Zygosaccharomyces rouxii (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956 {ECO:0000312|EMBL:AAF80562.1};
RN   [1] {ECO:0000312|EMBL:AAF80562.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=KACC30010 {ECO:0000312|EMBL:AAF80562.1};
RX   PubMed=12748054; DOI=10.1016/s1567-1356(03)00035-7;
RA   Kwon H.B., Yeo E.T., Hahn S.E., Bae S.C., Kim D.Y., Byun M.O.;
RT   "Cloning and characterization of genes encoding trehalose-6-phosphate
RT   synthase (TPS1) and trehalose-6-phosphate phosphatase (TPS2) from
RT   Zygosaccharomyces rouxii.";
RL   FEMS Yeast Res. 3:433-440(2003).
CC   -!- FUNCTION: Phosphatase catalytic subunit of the trehalose synthase
CC       complex that catalyzes the production of trehalose from glucose-6-
CC       phosphate and UDP-alpha-D-glucose in a two step process.
CC       {ECO:0000269|PubMed:12748054}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC         trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC         Evidence={ECO:0000305|PubMed:12748054};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P31688};
CC   -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC   -!- INDUCTION: Repressed by salt and thermal stress.
CC       {ECO:0000269|PubMed:12748054}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC       phosphatase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 20 family. {ECO:0000305}.
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DR   EMBL; AF208030; AAF80562.1; -; mRNA.
DR   AlphaFoldDB; Q9P4D3; -.
DR   SMR; Q9P4D3; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   BRENDA; 3.1.3.12; 6763.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; IGI:UniProtKB.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IGI:UniProtKB.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   PANTHER; PTHR10788; PTHR10788; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   TIGRFAMs; TIGR00685; T6PP; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..900
FT                   /note="Trehalose-phosphatase"
FT                   /id="PRO_0000453075"
FT   REGION          76..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          874..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..900
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   900 AA;  103843 MW;  9A56724C033659D8 CRC64;
     MVNSGHRRQR IINCVAQLPY KIQLGETNDE WNIVPATGSS SLYSSIEYLN SEEKAKDYEQ
     HVLGWTGEIG RESLPSRLFN SKNRDKSENG EKGENDLHAK EEREKEEDPL YLTNDQIDGI
     TKDLRRHGKS DDHYNVDNVH PVWLLRRDQK RWRGFAENVL WPTFHYILKF SSDSGEKENL
     SWYDYVRFNE AYAMKIGEIY EKGDIIWIHD YYLLLLPQLL RMKFNDQDLT IAYFHHSPWP
     SNEYFRVLPR RKQILDGLMG ADRGWFQNEG FARHFVSSCK RLLDSTSRKS KNRLGMEQYQ
     ISAYGGDIVV DSLPIGINRV KLLEDTFTKD IAQKVLAIKD AFQGKKIIVG RDRLDSVRGV
     VQKLRAFETF LSMYPEWRDQ VVLIQVSVPS MKGGTNQLIR LEQQVNELVT SINMQYGSLN
     FSPVHHYYMR IPKDVYLSLL RVADLCVIAS VRDGTNTTAL EYVTVKSHMS NYNCYGNPLI
     LSEFSGTSTI LKDAMIINPW DSVAVAKSIN RALSLSRDEK RALEDKIWPQ VPTIQKWTDQ
     FLSTLSDIVD EAHNTTDRKM TPALNRPALL EHYRQSKRRL FLFDYDGTLT PIVQDPAAAI
     PSARLISILQ KLASDPCNQI WIISGRDQAF LNKWLGSRLP QLGLSAEHGC FYKDVDEENW
     INLTEKFDMS WQEKVGSIME EFTRRTPGSF IERKKVALTW HYRRADPELG EFYASELKKE
     LDKICADYDL DVMEGKANIE VRPKFVNKGE IVKRLVWHHH GRRQDMLNTK KEELPISEMP
     DFTLCLGDDF TDEDMFNQLN DIEAVWKKQY EDEVNQWGGF GLYPCTVGSA SKKTVAKAHL
     TDPQQVLDTL GLLVGDVSLF QSAGTVELDS RGHVKHSDSS IRSEQASARY AMKRQQSYKN