ID   TPS1_APHAV              Reviewed;        1155 AA.
AC   Q5K2C4; Q5K2C3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1;
DE            EC=2.4.1.15;
DE   AltName: Full=Trehalose-6-phosphate synthase 1;
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase 1;
GN   Name=tps-1;
OS   Aphelenchus avenae (Mycophagous nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchidae; Aphelenchus.
OX   NCBI_TaxID=70226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX   PubMed=15935281; DOI=10.1016/j.biochi.2005.01.010;
RA   Goyal K., Browne J.A., Burnell A.M., Tunnacliffe A.;
RT   "Dehydration-induced tps gene transcripts from an anhydrobiotic nematode
RT   contain novel spliced leaders and encode atypical GT-20 family proteins.";
RL   Biochimie 87:565-574(2005).
CC   -!- FUNCTION: Catalyzes the production of trehalose from glucose-6-
CC       phosphate and UDP-alpha-D-glucose in a 2 step process. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC         trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q5K2C4-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q5K2C4-2; Sequence=VSP_038109;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 20 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the gob-1 trehalose
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; AJ811568; CAH18873.1; -; mRNA.
DR   EMBL; AJ811569; CAH18874.1; -; mRNA.
DR   AlphaFoldDB; Q5K2C4; -.
DR   SMR; Q5K2C4; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 1.20.58.1800; -; 1.
DR   Gene3D; 3.30.70.3080; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR049063; T6PP_C.
DR   InterPro; IPR041064; T6PP_helical.
DR   PANTHER; PTHR10788:SF110; ALPHA,ALPHA-TREHALOSE-PHOSPHATE SYNTHASE [UDP-FORMING] 2; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF21141; T6PP_C; 1.
DR   Pfam; PF18572; T6PP_N; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycosyltransferase; Transferase.
FT   CHAIN           1..1155
FT                   /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT                   forming] 1"
FT                   /id="PRO_0000385173"
FT   REGION          56..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..175
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000303|PubMed:15935281"
FT                   /id="VSP_038109"
SQ   SEQUENCE   1155 AA;  130891 MW;  5D15061B15C32E47 CRC64;
     MSHGTKYRDA LLFSLTLYDV NTGKSRLKEL YAAVPGIRKS LLGVHAKRFG EQYHHLQRRR
     SVSSRGGSLR GSMDSLNDSG QNGAEDVIGV EDEEEAQKFR GKRTSISLDP AAAGEVMFTI
     EDGACFPSGG LANTHFQQRV INVSNAPPVS LKREKSGEWE IKQGSGGLVS CVDPIMSVNQ
     ENMWLANLGM NIDKKKMLRS TELLNVTDDS APLAPATNTL GLPLMRQALA DVLFHVIADD
     DIKEQNEDEQ SRNVRWGHSS VEAGGVAPSQ PWEEMSLLGV LNQYNRSNYK LNPVVVQEQD
     YNVYYGGISN GLLWPALHNL PEYIVADYDD PKVLYEHWCA YVRVNYQFAI DAVRNSRPQD
     FIWIHDYHLM LTGMIMQSLD SSLEIGFFLH IPFLPPDNFF TKYRLCAFPI MRGLLRFTKV
     GFQTHRDRAK FVELVGIHLP TARVTYDEKM DIHTVTYQGW SCSLGVFPVS IKNEDFLKVA
     QSAETIKKAD DIRKEILGET PVDSARLLFS VERFDYTKGI KEKLLAYRRY FERHPDRIGK
     DVLYQVAVTN RRSVDTYRMY QDECIQMAED INREFATDEY PNWKPLIFRT DGLQRADLVA
     HYLAMDVGVV TPKKDGMNLV AKEMLVCNPS AGLVLSTGAG SEIQFTMAGL HPDDGDKCYH
     RVVDVYDADH YADAFYEAAV EPEGERAAHG QRLNEFIMNN DIERWSTAFL DPGWSHLVIR
     QSEIKDLDDF YSLMMRTRDV RRQIVERVLK GIPIRSHFSI SLSNTKESLL LACQPGTRTL
     HLKPSLEEDE QTEPAHFDIA NELDEFEKDL NFMKFIQSDD VYNVEQFINS LQEYHPVSAD
     KFRDEVIELG DVLTEADHFN FFFTDRDGTL KSYSCSYPAS IQPAYSGVIQ AQFARRCAQT
     CAIVTTAPLM RIGVLDVSTI PEGYYYFGAS AGREWFIDPA NKFKDQSIPE EDLELLERVF
     AAISDLLEEP KFKHFTWVGS GLQKHYGHIT IAHQDAFNSV PRHQVRAIDQ KIKDIIHRID
     PDQHTLKVKE TETDIKIFLK SESGEIFDKG QGIRLLVEHM KCDISNGTIL VCGDSSTDLP
     MLQACLEANP SGVYTVWVTR SDELKTTVRE LCERFGNKNF VFVSCPEVLL GGMAQATIRE
     ISIGRPGPRA SHDSE
//