Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_103595g0010 |
Family | GT4 |
Protein Properties | Length: 1026 Molecular Weight: 115398 Isoelectric Point: 6.3559 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT4 | 466 | 635 | 0 |
LNNPSKPIILALARPDPKKNMATLVKAFGECIKLRKLANLMLIMGNRDDIDQMPAASANVLTTVLKLIDKYNLYGEVAYPKHHKQSEVADIYRIAAKTKG VFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIKQTLNNGLLVDPHNDKEIAAALYKLVADKNLWAE |
Full Sequence |
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Protein Sequence Length: 1026 Download |
MAGNEWMNGY LEAILDGGAN DEDDYTLQKK DSSVKSGVSV LPQLGAFNPA RYFIDEVVNG 60 TDEMDLHHFW VKVTATKNPE ERNTRLENLC WRIWHVSRRK NKGKLEQSKR LHMLRLERER 120 GRRDVTEDLS EDLSEGERLG GDGQGLKLSE SHFNLELLVE QPHKDKRLYV ILISLHGLVR 180 GENMELGRDS DTGGQVKYVV EFAKALAKMP EVYRVDLLTR QICSPEVDSS YGEPTEMLTS 240 DQDEDILESG GAYIVRIPCG CKEKYIEKEL LWPHIPEFVD GALGHILNIS KALGDLIGEG 300 RPVWPHVIHG HYADAGDAAC LLSGALDVPM VLTGHSLGRN KLEQLLKQGM HSKEDINATY 360 KIMRRIEAEE LCIDSAELVV TSTRQEIEEQ WGLYDGFDLE LNKKIRHRIK RGVHCYGRYM 420 PRMTVIPPGM DFSNVITHDE NTDNALDNDS TQLPESPLWG EIPRFLNNPS KPIILALARP 480 DPKKNMATLV KAFGECIKLR KLANLMLIMG NRDDIDQMPA ASANVLTTVL KLIDKYNLYG 540 EVAYPKHHKQ SEVADIYRIA AKTKGVFINP ALVEPFGLTL IEAAAHGLPM VATKNGGPVD 600 IKQTLNNGLL VDPHNDKEIA AALYKLVADK NLWAECRQNG LKNIHLYSWP QHCKIYLSRI 660 SQCRMRHPQW QSENDLNENV DSESDSGSFK DAPDTSLRLS LDADKPSRSN SLYDTIELDK 720 LLQNEDSGKG FSEHIRMILE KTKESPSKLR ETNDANSPEI EGIDRSNSLN SSGKLLLRRR 780 KRLFVIAVDC YDAIGEPLVS KQVIIIQEIM NAVRFAGNFS SPGFILSTAL TVSETLSMLQ 840 SIGIKVSAFD ALICSSGSQL LYTAGDNLDS SIYPDPDYDS HIDYRWGAEG LRKSMKKLRG 900 PENSRFLVED AEASNSHCLA YQVKNISTAP KADELRRQLR MRGLRCHVVY TQNCSRLRVL 960 PLHASRSQAL RYLYVRWGLD IANMYVFLGE KGDTDYEEMI GGMHKSLILK GIVNDGSEKM 1020 MRSPTS |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN00142 | PLN00142 | 6.0e-35 | 170 | 660 | 549 | + sucrose synthase | ||
TIGR02470 | sucr_synth | 1.0e-49 | 170 | 660 | 527 | + sucrose synthase. This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
cd03800 | GT1_Sucrose_synthase | 2.0e-146 | 169 | 658 | 491 | + This family is most closely related to the GT1 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light. | ||
TIGR02472 | sucr_P_syn_N | 3.0e-171 | 168 | 660 | 494 | + sucrose-phosphate synthase, putative, glycosyltransferase domain. This family consists of the N-terminal regions, or in some cases the entirety, of bacterial proteins closely related to plant sucrose-phosphate synthases (SPS). The C-terminal domain (TIGR02471), found with most members of this family, resembles both bona fide plant sucrose-phosphate phosphatases (SPP) and the SPP-like domain of plant SPS. At least two members of this family lack the SPP-like domain, which may have binding or regulatory rather than enzymatic activity by analogy to plant SPS. This enzyme produces sucrose 6-phosphate and UDP from UDP-glucose and D-fructose 6-phosphate, and may be encoded near the gene for fructokinase. | ||
TIGR02468 | sucrsPsyn_pln | 0 | 1 | 1020 | 1049 | + sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant. Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAF40445.1 | 0 | 1 | 1023 | 1 | 1025 | AC004809_3 Strong similarity to the sucrose-phosphate synthase from Craterostigma plantagineum gb |
GenBank | ABA64521.1 | 0 | 1 | 1026 | 1 | 1029 | sucrose-phosphate synthase isoform B [Nicotiana tabacum] |
RefSeq | NP_171984.2 | 0 | 1 | 1023 | 1 | 1023 | ATSPS3F (sucrose phosphate synthase 3F); sucrose-phosphate synthase/ transferase, transferring glycosyl groups [Arabidopsis thaliana] |
Swiss-Prot | O04933 | 0 | 1 | 1026 | 1 | 1043 | SPS2_CRAPL RecName: Full=Sucrose-phosphate synthase 2; AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase 2 |
RefSeq | XP_002518055.1 | 0 | 1 | 1023 | 1 | 1025 | sucrose phosphate syntase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2r68_A | 0 | 191 | 677 | 31 | 473 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 2r66_A | 0 | 191 | 677 | 31 | 473 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 2r60_A | 0 | 191 | 677 | 31 | 473 | A Chain A, Structure Of Apo Sucrose Phosphate Synthase (Sps) Of Halothermothrix Orenii |
PDB | 3s29_H | 3e-38 | 170 | 677 | 281 | 779 | A Chain A, Structure Of Apo Sucrose Phosphate Synthase (Sps) Of Halothermothrix Orenii |
PDB | 3s29_G | 3e-38 | 170 | 677 | 281 | 779 | A Chain A, Structure Of Apo Sucrose Phosphate Synthase (Sps) Of Halothermothrix Orenii |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO796578 | 431 | 147 | 567 | 0 |
HO796578 | 77 | 562 | 638 | 0 |
HO796578 | 40 | 62 | 101 | 0 |
HO796578 | 26 | 647 | 672 | 0 |
HO796578 | 40 | 106 | 145 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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