TPS2_APHAV
ID TPS2_APHAV Reviewed; 1303 AA.
AC Q5K2C1; Q5K2C0; Q5K2C2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 2;
DE EC=2.4.1.15;
DE AltName: Full=Trehalose-6-phosphate synthase 2;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase 2;
GN Name=tps-2;
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=Q5K2C1-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q5K2C1-2; Sequence=VSP_038110, VSP_038111;
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; AJ811571; CAH18870.1; -; mRNA.
DR EMBL; AJ811570; CAH18869.1; -; mRNA.
DR EMBL; AJ811572; CAH18871.1; -; mRNA.
DR AlphaFoldDB; Q5K2C1; -.
DR SMR; Q5K2C1; -.
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:0004805; F:trehalose-phosphatase activity; IEA:UniProt.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
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; IPR023214; HAD_sf.
DR InterPro; IPR041064; T6PP_helical.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF18572; T6PP_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycosyltransferase; Transferase.
FT CHAIN 1..1303
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 2"
FT /id="PRO_0000385174"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 349..364
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:15935281"
FT /id="VSP_038110"
FT VAR_SEQ 420
FT /note="R -> RWGHSSAGEAGVEPSQPW (in isoform b)"
FT /evidence="ECO:0000303|PubMed:15935281"
FT /id="VSP_038111"
FT CONFLICT 180
FT /note="Y -> C (in Ref. 1; CAH18871)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="G -> A (in Ref. 1; CAH18871)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..229
FT /note="SG -> A (in Ref. 1; CAH18871)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="G -> S (in Ref. 1; CAH18871)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="I -> T (in Ref. 1; CAH18869)"
FT /evidence="ECO:0000305"
FT CONFLICT 381..383
FT /note="ATN -> TTY (in Ref. 1; CAH18871)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="P -> A (in Ref. 1; CAH18871)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="I -> T (in Ref. 1; CAH18869)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="L -> P (in Ref. 1; CAH18871)"
FT /evidence="ECO:0000305"
FT CONFLICT 1084
FT /note="F -> L (in Ref. 1; CAH18869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1303 AA; 147741 MW; ACF8CF07481DE669 CRC64;
MTVVPGETQC EEAQPAANGS SSPVLLQPFR RPRTDSRSRL DSGSNNTTLS EDCARKSILR
TLKSLGVEID ESASFEAIID SGGIEKLADF WRKRDSSSEI AFQGLLSVLE YCLQHSFDTN
EFFEKFVNAL GYHTVQFWRA GVPYVFDSDM SHGTKYRDAL LFSLTLYDVN TGKSRLKELY
AAVPGIRKSL LGVHAKRFGE QYHHLQRRRS VSSRGGSLRG SMDSLNDSGQ NGAEDVIGVE
DEEEAQKFRG KRTSISLDPA AAGEVMFTIE DGACFPSGGL ANTHFQQRVI NVSNAPPVSL
KREKSGEWEI KQGSGGLVSC VDPIMSVNQE NMWLANLGMN IDKKKMLRYD DCLRSQEHTL
ENMRSTELLN VTDDSAPLAP ATNTLGLPLM RQALADVLFH VIADDDIKEQ NEDEQSRNVR
EEMSLLGVLN QYNRSNYKLN PVVVQEQDYN VYYGGISNGL LWPALHNLPE YIVADYDDPK
VLYEHWCAYV RVNYQFAIDA VRNSRPQDFI WIHDYHLMLT GMIMQSLDSS LEIGFFLHIP
FLPPDNFFTK YRLCAFPIMR GLLRFTKVGF QTHRDRAKFV ELVGIHLPTA RVTYDEKMDI
HTVTYQGWSC SLGVFPVSIK NEDFLKVAQS AETIKKADDI RKEILGETPV DSARLLFSVE
RFDYTKGIKE KLLAYRRYFE RHPDRIGKDV LYQVAVTNRR SVDTYRMYQD ECIQMAEDIN
KEFATDEYPN WKPLIFRTDG LQRADLVAHY LAMDVGVVTP KKDGMNLVAK EMLVCNPSAG
LVLSTGAGSE IQFTMAGLHP DDGDKCYHRV VDVYDADHYA DAFYEAAVEP EAERAAHGQR
LNEFIMNNDI ERWSTAFLDP GWSHLVIRQS EIKDLDDFYS LMMRTRDVRR QIVERVLKGI
PIRSHFSISL SNAKESLLLA CQPGTRTLHL KPSLEEDEQT EPAHFDIANE LDEFEKDLNF
MKFIQSDDVY NVEQFINSLQ EYHPVSADKF RDEVIELGDM LTEADHFNFF FTDRDGTLKS
YSCSYPASIQ PAYSGVIQAQ FARRCAQTCA IVTTAPLMRI GVLDVSTIPE GYYYFGASAG
REWFIDPANK FKDQSIPEED LELLERVFAA ISDLLEEPKF KHFTWVGSGL QKHYGHITIA
HQDAFNSVPR HQVRAIDQKI KDIIHRIDPD QHTLKVKETE TDIKIFLKSE SGEIFDKGQG
IRLLVEHMKC DISNGTILVC GDSSTDLPML QACLEANPSG VYTVWVTRSD ELKTTVRELC
ERFGNKNFVF VSCPEVLLGG MAQATIREIS IGRPGPRASH DSE
