ID A8D372_LOCMI Unreviewed; 813 AA.
AC A8D372;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Trehalose-6-phosphate synthase {ECO:0000313|EMBL:ABV44614.1};
GN Name=tps {ECO:0000313|EMBL:ABV44614.1};
OS Locusta migratoria manilensis (Oriental migratory locust).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Oedipodinae; Locusta.
OX NCBI_TaxID=229990 {ECO:0000313|EMBL:ABV44614.1};
RN [1] {ECO:0000313|EMBL:ABV44614.1}
RP NUCLEOTIDE SEQUENCE.
RA Cui S.Y., Xia Y.X.;
RT "Isolation and characterization of the trehalose-6-phosphate synthase gene
RT from Locusta migratoria manilensis.";
RL Insect Sci. 16:287-295(2009).
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000256|ARBA:ARBA00006330}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
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DR EMBL; EU131894; ABV44614.1; -; mRNA.
DR AlphaFoldDB; A8D372; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR BRENDA; 2.4.1.15; 8204.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR CDD; cd03788; GT20_TPS; 1.
DR CDD; cd01627; HAD_TPP; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR NCBIfam; TIGR00685; T6PP; 1.
DR PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1.
DR PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 2: Evidence at transcript level;
FT REGION 782..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 91685 MW; 02BF244EFA785BBD CRC64;
MTASFNCFVF KVDDGFADTM GDPVTSKCMI VVSNRLPFVL KRNEKTGALE RKASAGGLVT
AVAPVVVQGH GLWVGWPGIH LENPDEPIPE SNPNDNTPTA GLLSKKVVAV CVEPGKFDSY
YNGCCNGTFW PLFHSMPDRA VFLAEHWKNY YSVNELFAEK TIKALRCLLD EQPTATPLVW
IHDYHLMLAA NWVRQIAEES NLRLKLGFFL HIPFPPWDIF RLCPWSDEIL QGILGNDMVG
FHIEDYCLNF IDCCQRRLGC RVDRKGLMVE HGGRTVIVRP LPIGIPYDRF VNMAEAAPKV
LPTNQKFVLG VDRLDYTKGL VHRLKAFELL LEKYPEHIEE VTLLQISVPS RTDVKEYQDL
KEEMDQMVGR INGRFTTYNW SPIRYIYGQV GQDELAAFYR DAAVTLVTPL RDGMNLVAKE
FVACQINEPP GVLIVSPFAG AGEMMHEALI CNPYEIHTAA EVIHRALTMP EDERTLRMNY
LRRREKLHDV NYWMKSFFKA MGSLREDGDD GLPTTMQPVT MDDFDEYLSK YLGNHHKLAL
LLDYDGTLAP IAPHPDLAIL PPETKSVLER LSNMPDVYVA IISGRNVVNV KQMVGIEGIT
YAGNHGLEIL HPDGSKFVHP MPSEFEDKVT DLLKALQEQV CREGAWVENK GALLTFHYRE
TPMYLRAEMV AQAQTLIEQA GFKAGSAHCA IEAKPPVQWN KGRASLYILR TAFGVDWSER
IRIIYAGDDV TDEDAMEALK GMAATFRVTS SHIVKTAAER RLPNTDSVLT MLKWLERHLS
GREPRQDANG GPYRRPSKRK GCECKPKSAG KQC
//