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Conserved domains on  [gi|414151920|gb|AFW99132|]
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sucrose synthase, partial [Vouacapoua macropetala]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00142 super family cl30293
sucrose synthase
1-183 5.14e-151

sucrose synthase


The actual alignment was detected with superfamily member PLN00142:

Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 437.49  E-value: 5.14e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920   1 ALEKTKYPDSDIYWKKFEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 80
Cdd:PLN00142 440 ALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 519
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920  81 PKFNIVSPGADMSIYFPFTETNHRLTSFHPEIEELLYSSVENEEHICVLKDRNKPIIFTMARLDRVKNITGLVEWYGKNA 160
Cdd:PLN00142 520 PKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNK 599
                        170       180
                 ....*....|....*....|....
gi 414151920 161 RLRELVNLVVVAGD-RRKESKDLE 183
Cdd:PLN00142 600 RLRELVNLVVVGGFiDPSKSKDRE 623
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
1-183 5.14e-151

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 437.49  E-value: 5.14e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920   1 ALEKTKYPDSDIYWKKFEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 80
Cdd:PLN00142 440 ALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 519
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920  81 PKFNIVSPGADMSIYFPFTETNHRLTSFHPEIEELLYSSVENEEHICVLKDRNKPIIFTMARLDRVKNITGLVEWYGKNA 160
Cdd:PLN00142 520 PKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNK 599
                        170       180
                 ....*....|....*....|....
gi 414151920 161 RLRELVNLVVVAGD-RRKESKDLE 183
Cdd:PLN00142 600 RLRELVNLVVVGGFiDPSKSKDRE 623
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
1-183 9.35e-134

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]


Pssm-ID: 274149 [Multi-domain]  Cd Length: 784  Bit Score: 392.52  E-value: 9.35e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920    1 ALEKTKYPDSDIYWKKFEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 80
Cdd:TIGR02470 417 ALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAFTMPGLYRVVHGIDVFD 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920   81 PKFNIVSPGADMSIYFPFTETNHRLTSFHPEIEELLYSSVENEEHICVLKDRNKPIIFTMARLDRVKNITGLVEWYGKNA 160
Cdd:TIGR02470 497 PKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLDRVKNLTGLVECYGRSP 576
                         170       180
                  ....*....|....*....|....
gi 414151920  161 RLRELVNLVVVAGDRR-KESKDLE 183
Cdd:TIGR02470 577 KLRELVNLVVVAGKLDaKESKDRE 600
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
1-117 4.96e-96

Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.


Pssm-ID: 395692  Cd Length: 540  Bit Score: 288.39  E-value: 4.96e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920    1 ALEKTKYPDSDIYWKKFEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 80
Cdd:pfam00862 424 ALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVGQYESHTAFTLPGLYRVVSGIDVFD 503
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 414151920   81 PKFNIVSPGADMSIYFPFTETNHRLTSFHPEIEELLY 117
Cdd:pfam00862 504 PKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
1-176 9.18e-44

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 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.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 149.31  E-value: 9.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920   1 ALEKTKYPDSDIYWKkfedkYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHtaftlpglyrvvhgidvfd 80
Cdd:cd03800  133 SLGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSR------------------- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920  81 pkFNIVSPGADMSIYFPFTETNHRltsfhpeieellyssveneeHICVLKDRNKPIIFTMARLDRVKNITGLVEWYGKNA 160
Cdd:cd03800  189 --INVVPPGVDLERFFPVDRAEAR--------------------RARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLP 246
                        170
                 ....*....|....*.
gi 414151920 161 RLRELVNLVVVAGDRR 176
Cdd:cd03800  247 ELRELANLVLVGGPSD 262
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
1-183 5.14e-151

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 437.49  E-value: 5.14e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920   1 ALEKTKYPDSDIYWKKFEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 80
Cdd:PLN00142 440 ALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 519
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920  81 PKFNIVSPGADMSIYFPFTETNHRLTSFHPEIEELLYSSVENEEHICVLKDRNKPIIFTMARLDRVKNITGLVEWYGKNA 160
Cdd:PLN00142 520 PKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNK 599
                        170       180
                 ....*....|....*....|....
gi 414151920 161 RLRELVNLVVVAGD-RRKESKDLE 183
Cdd:PLN00142 600 RLRELVNLVVVGGFiDPSKSKDRE 623
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
1-183 9.35e-134

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]


Pssm-ID: 274149 [Multi-domain]  Cd Length: 784  Bit Score: 392.52  E-value: 9.35e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920    1 ALEKTKYPDSDIYWKKFEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 80
Cdd:TIGR02470 417 ALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAFTMPGLYRVVHGIDVFD 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920   81 PKFNIVSPGADMSIYFPFTETNHRLTSFHPEIEELLYSSVENEEHICVLKDRNKPIIFTMARLDRVKNITGLVEWYGKNA 160
Cdd:TIGR02470 497 PKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLDRVKNLTGLVECYGRSP 576
                         170       180
                  ....*....|....*....|....
gi 414151920  161 RLRELVNLVVVAGDRR-KESKDLE 183
Cdd:TIGR02470 577 KLRELVNLVVVAGKLDaKESKDRE 600
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
1-117 4.96e-96

Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.


Pssm-ID: 395692  Cd Length: 540  Bit Score: 288.39  E-value: 4.96e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920    1 ALEKTKYPDSDIYWKKFEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFD 80
Cdd:pfam00862 424 ALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVGQYESHTAFTLPGLYRVVSGIDVFD 503
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 414151920   81 PKFNIVSPGADMSIYFPFTETNHRLTSFHPEIEELLY 117
Cdd:pfam00862 504 PKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
1-176 9.18e-44

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 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.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 149.31  E-value: 9.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920   1 ALEKTKYPDSDIYWKkfedkYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHtaftlpglyrvvhgidvfd 80
Cdd:cd03800  133 SLGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSR------------------- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 414151920  81 pkFNIVSPGADMSIYFPFTETNHRltsfhpeieellyssveneeHICVLKDRNKPIIFTMARLDRVKNITGLVEWYGKNA 160
Cdd:cd03800  189 --INVVPPGVDLERFFPVDRAEAR--------------------RARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLP 246
                        170
                 ....*....|....*.
gi 414151920 161 RLRELVNLVVVAGDRR 176
Cdd:cd03800  247 ELRELANLVLVGGPSD 262
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
134-175 2.93e-07

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.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 49.39  E-value: 2.93e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 414151920   134 KPIIFTMARLDRVKNITGLVEWYGKNARLRELVNLVVVAGDR 175
Cdd:TIGR02468  479 KPMILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNR 520
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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