TPS2_CAEEL
ID TPS2_CAEEL Reviewed; 1229 AA.
AC O45380; Q7YZT5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 126.
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; Synonyms=tps2; ORFNames=F19H8.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=13678635; DOI=10.1016/s0020-7519(03)00173-5;
RA Pellerone F.I., Archer S.K., Behm C.A., Grant W.N., Lacey M.J.,
RA Somerville A.C.;
RT "Trehalose metabolism genes in Caenorhabditis elegans and filarial
RT nematodes.";
RL Int. J. Parasitol. 33:1195-1206(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Catalyzes the production of trehalose from glucose-6-
CC phosphate and UDP-alpha-D-glucose in a 2 step process.
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 -!- DEVELOPMENTAL STAGE: Expressed in all development stages.
CC {ECO:0000269|PubMed:13678635}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:13678635}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD54507.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ512333; CAD54507.2; ALT_FRAME; mRNA.
DR EMBL; AJ811574; CAH18872.1; -; mRNA.
DR EMBL; Z93378; CAB07584.3; -; Genomic_DNA.
DR PIR; T21127; T21127.
DR RefSeq; NP_497035.3; NM_064634.5.
DR AlphaFoldDB; O45380; -.
DR SMR; O45380; -.
DR BioGRID; 532368; 1.
DR STRING; 6239.F19H8.1a; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EPD; O45380; -.
DR PaxDb; O45380; -.
DR PeptideAtlas; O45380; -.
DR EnsemblMetazoa; F19H8.1a.1; F19H8.1a.1; WBGene00006603.
DR GeneID; 3565050; -.
DR KEGG; cel:CELE_F19H8.1; -.
DR UCSC; F19H8.1; c. elegans.
DR CTD; 3565050; -.
DR WormBase; F19H8.1a; CE37507; WBGene00006603; tps-2.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_007752_0_0_1; -.
DR InParanoid; O45380; -.
DR OMA; ANDIERW; -.
DR OrthoDB; 772297at2759; -.
DR PRO; PR:O45380; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006603; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; O45380; baseline and differential.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IBA:GO_Central.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProt.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
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 Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..1229
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 2"
FT /id="PRO_0000385177"
FT REGION 196..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 139911 MW; 707A48DA05E6383D CRC64;
MGSEPPPSEK KVREPFSRAM KDVQISDEQR LKELWHLLDL LEIEYKKTAD LHTLISSVSE
SLTMVWKRRD PKSELALKGL LLILEYCLSH VFDGHAVFEI FVSSLGFNTV IFWKHCAGYI
FDSDLGRGTK FRDALLFSLT LYDVNTGKNR LRELYAAVPG IRKSLLGVNA KQFGERYHHL
QKRLARYGSH TSLCSVSSDS EGEEAIHNVR SGTHTESESE EDPKAPRSGL ATSHFQQRVI
NVSNAPPVSL KREKTGDWEI KQGSGGLVAC VDPVMSKDHE NLWLANLGMN INDKKQKRPG
SVASIPESFP STNTLGLPLI KQTIAEVFFH VLADDDMDAP KNEKQKKARE EMSLLGVLNN
YNRGNYKLNP VVVQEDDYNV YYGGISNGLL WPALHNLPEY IVSEYDDEKI LRAHWCAYVR
VNYQFAIDAV RNSRPQDFIW IHDYHLMLVG MIMQSLDQHL EVGFFLHIPF QPPGEFFSKY
STVGFAVLRG LLRFTKVGFQ THRDRTKYIE LVQHYFGTAK IVYDNKMDIY SITNEGWTCS
LGVFPVSIKN DDFLKFVDLP ETIKLKNDLR KRVMGDTPAP DGRFFFSVER FDYTKGIMEK
LQAYKRYFER HPDRIGKDVL FQIAVTNRRS VDTYRVYQDE CIDLADKINE IFKDPNNPTW
KPLVFQTDGL PRSELVAAYL AMDIGVVTPK KDGMNLVAKE MLVCNPKAGL VLSTGAGSEI
QFTTAGLYSD KEKNYHRISN VFDPDSYCDA FYSAALEPED VRAEHGKRLH EFIMANDIER
WSCAFLDPSW THEVIRPTQV ETLDDFFSLM MKTRNVRRQI VGRVLKGIPI RSHFAISLRN
AKESLEQICK PGTHTAEFKS GPDSKEVAHF EIDNELQEFE RDLSFIDYVQ SDDADNVEQF
VDTLISSHPI SVETYKKEVE NAVELLYSAD HFHYFFTDRD GTLKSYSCSY PSSIQPAYSG
VIQAQFARRC AQTCVILTTA PLMHIGVLDV STIPNGYYYF GASGGREWFI DNGHNFKDES
ILKGEKADVL ASAYTRISHL LEEPEFRPFT WVGSGLQKHY GHLTIAFQDV YKTITEAQGK
QLHEEIEKIV KDVDPHGTRL QLASTEFDIK VYMKTETDGH VFDKGDGLRL LCEKMHCDLT
EGNVLVCGDS STDIPMLKEC LIRNPKGVYT IWVTVNDKLK EEVRALCASY SNSNVAFVSC
PEVLLGAMAQ ATIREITITR TRKMSRNIV
