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Conserved domains on  [gi|292668835|gb|ADE41073|]
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granule-bound starch synthase, partial [Solanum monachophyllum]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 1-324 6.38e-114

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03791:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 474  Bit Score: 338.00  E-value: 6.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   1 VRVGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKVWGKtaskiygPKAGQDYLDNELRFSLLCQAALEAPRVLnlncskyf 80
Cdd:cd03791   61 VKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-------- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  81 sgpYGEDVLFIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGHEKPv 160
Cdd:cd03791  126 ---GFQPDIIHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY- 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 161 kgRKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDiTTVM 238
Cdd:cd03791  197 --GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRARAgkLSGILNGIDYDEWNPATDKLIPANYS-ANDL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 239 DAKPLLKEALQATVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAK 318
Cdd:cd03791  273 EGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVA 352


                 ....*.
gi 292668835 319 GVAKFN 324
Cdd:cd03791  353 VVIGFD 358
 
Name Accession Description Interval E-value
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 1-324 6.38e-114

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 338.00  E-value: 6.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   1 VRVGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKVWGKtaskiygPKAGQDYLDNELRFSLLCQAALEAPRVLnlncskyf 80
Cdd:cd03791   61 VKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-------- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  81 sgpYGEDVLFIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGHEKPv 160
Cdd:cd03791  126 ---GFQPDIIHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY- 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 161 kgRKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDiTTVM 238
Cdd:cd03791  197 --GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRARAgkLSGILNGIDYDEWNPATDKLIPANYS-ANDL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 239 DAKPLLKEALQATVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAK 318
Cdd:cd03791  273 EGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVA 352


                 ....*.
gi 292668835 319 GVAKFN 324
Cdd:cd03791  353 VVIGFD 358
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 1-324 7.04e-105

glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273969 [Multi-domain]  Cd Length: 473  Bit Score: 314.97  E-value: 7.04e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835    1 VRVGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKVwgktaSKIYGPkagqDYLDNELRFSLLCQAALEAPRVLNlncskyf 80
Cdd:TIGR02095  63 LSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDRP-----GGIYGD----DYPDNAERFAFFSRAAAELLSGLG------- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   81 sgpYGEDVlFIANDWHTALIPCYLKSMYQSrgiyLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGSFDFIDGHEkpv 160
Cdd:TIGR02095 127 ---WQPDV-VHAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGR--- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  161 kgrkINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvM 238
Cdd:TIGR02095 196 ----VNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADD-L 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  239 DAKPLLKEALQATVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAK 318
Cdd:TIGR02095 270 AGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVR 349


                  ....*.
gi 292668835  319 GVAKFN 324
Cdd:TIGR02095 350 VIIGYD 355
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
1-316 3.78e-91

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 279.67  E-value: 3.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   1 VRVGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktaSKIYGPkAGQDYLDNELRFSLLCQAALEAPRVLNLNCskyf 80
Cdd:COG0297   62 VPLGGRTYYARVLEGPDDGVPVYFIDNPELFDR------PGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP---- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  81 sgpygeDVLFiANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGHEKPv 160
Cdd:COG0297  131 ------DIIH-CHDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEFY- 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 161 kGrKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvM 238
Cdd:COG0297  198 -G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD-L 273

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 292668835 239 DAKPLLKEALQATVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 316
Cdd:COG0297  274 EGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
glgA PRK00654
glycogen synthase GlgA;
10-316 2.60e-76

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 241.18  E-value: 2.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  10 VRFFHCYKRGVDRVFVDHPMFlekvwgktaskiYGPKAGQDYLDNELRFSLLCQAALEAprvlnlnCSKYFSGPygeDVL 89
Cdd:PRK00654  65 VLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF-------AEGLDPRP---DIV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  90 FiANDWHTALIPCYLKSMYQSRgiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFR--GSFDFiDGHekpvkgrkINW 167
Cdd:PRK00654 123 H-AHDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEAFhlEGLEF-YGQ--------ISF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 168 MKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLK 245
Cdd:PRK00654 191 LKAGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENK 268

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 292668835 246 EALQATVGLPVDrKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 316
Cdd:PRK00654 269 RALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGK 338
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
3-205 1.75e-56

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 182.92  E-value: 1.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835    3 VGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktaSKIYGPKaGQDYLDNELRFSLLCQAALEAPRVLNlncskyfsg 82
Cdd:pfam08323  64 VPVRPLTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKLG--------- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   83 pYGEDVLfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGsfdfIDGHEKPvkg 162
Cdd:pfam08323 128 -WIPDII-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY--- 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 292668835  163 RKINWMKAGILESDRVVTVSPYYAQELVSAVDkGVELDNVLRK 205
Cdd:pfam08323 198 GQINFLKAGIVYADAVTTVSPTYAEEIQTPEF-GGGLDGLLRE 239
 
Name Accession Description Interval E-value
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 1-324 6.38e-114

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 338.00  E-value: 6.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   1 VRVGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKVWGKtaskiygPKAGQDYLDNELRFSLLCQAALEAPRVLnlncskyf 80
Cdd:cd03791   61 VKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRL-------- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  81 sgpYGEDVLFIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGHEKPv 160
Cdd:cd03791  126 ---GFQPDIIHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY- 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 161 kgRKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDiTTVM 238
Cdd:cd03791  197 --GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRARAgkLSGILNGIDYDEWNPATDKLIPANYS-ANDL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 239 DAKPLLKEALQATVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAK 318
Cdd:cd03791  273 EGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVA 352


                 ....*.
gi 292668835 319 GVAKFN 324
Cdd:cd03791  353 VVIGFD 358
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 1-324 7.04e-105

glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273969 [Multi-domain]  Cd Length: 473  Bit Score: 314.97  E-value: 7.04e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835    1 VRVGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKVwgktaSKIYGPkagqDYLDNELRFSLLCQAALEAPRVLNlncskyf 80
Cdd:TIGR02095  63 LSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDRP-----GGIYGD----DYPDNAERFAFFSRAAAELLSGLG------- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   81 sgpYGEDVlFIANDWHTALIPCYLKSMYQSrgiyLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGSFDFIDGHEkpv 160
Cdd:TIGR02095 127 ---WQPDV-VHAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGR--- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  161 kgrkINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvM 238
Cdd:TIGR02095 196 ----VNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADD-L 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  239 DAKPLLKEALQATVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAK 318
Cdd:TIGR02095 270 AGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVR 349


                  ....*.
gi 292668835  319 GVAKFN 324
Cdd:TIGR02095 350 VIIGYD 355
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
1-316 3.78e-91

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 279.67  E-value: 3.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   1 VRVGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktaSKIYGPkAGQDYLDNELRFSLLCQAALEAPRVLNLNCskyf 80
Cdd:COG0297   62 VPLGGRTYYARVLEGPDDGVPVYFIDNPELFDR------PGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP---- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  81 sgpygeDVLFiANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGHEKPv 160
Cdd:COG0297  131 ------DIIH-CHDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEFY- 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 161 kGrKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvM 238
Cdd:COG0297  198 -G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD-L 273

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 292668835 239 DAKPLLKEALQATVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 316
Cdd:COG0297  274 EGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
glgA PRK00654
glycogen synthase GlgA;
10-316 2.60e-76

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 241.18  E-value: 2.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  10 VRFFHCYKRGVDRVFVDHPMFlekvwgktaskiYGPKAGQDYLDNELRFSLLCQAALEAprvlnlnCSKYFSGPygeDVL 89
Cdd:PRK00654  65 VLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF-------AEGLDPRP---DIV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  90 FiANDWHTALIPCYLKSMYQSRgiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFR--GSFDFiDGHekpvkgrkINW 167
Cdd:PRK00654 123 H-AHDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEAFhlEGLEF-YGQ--------ISF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 168 MKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLK 245
Cdd:PRK00654 191 LKAGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENK 268

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 292668835 246 EALQATVGLPVDrKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 316
Cdd:PRK00654 269 RALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGK 338
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
3-205 1.75e-56

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 182.92  E-value: 1.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835    3 VGDNIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktaSKIYGPKaGQDYLDNELRFSLLCQAALEAPRVLNlncskyfsg 82
Cdd:pfam08323  64 VPVRPLTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKLG--------- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   83 pYGEDVLfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGsfdfIDGHEKPvkg 162
Cdd:pfam08323 128 -WIPDII-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY--- 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 292668835  163 RKINWMKAGILESDRVVTVSPYYAQELVSAVDkGVELDNVLRK 205
Cdd:pfam08323 198 GQINFLKAGIVYADAVTTVSPTYAEEIQTPEF-GGGLDGLLRE 239
PRK14099 PRK14099
glycogen synthase GlgA;
48-314 1.12e-50

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 174.91  E-value: 1.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  48 GQDYLDNELRFSLLCQAALEAPRVLnlncskyfSGPYGEDVLFiANDWHTALIPCYLKsmYQSRGiylNAKVAFCIHNIA 127
Cdd:PRK14099 104 GKDWPDNAQRFAALARAAAAIGQGL--------VPGFVPDIVH-AHDWQAGLAPAYLH--YSGRP---APGTVFTIHNLA 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 128 YQGRFAFSDFPLLNLPDEfrgSFDfIDGHEkpVKGrKINWMKAGILESDRVVTVSPYYAQELVSAvDKGVELDNVLRKTS 207
Cdd:PRK14099 170 FQGQFPRELLGALGLPPS---AFS-LDGVE--YYG-GIGYLKAGLQLADRITTVSPTYALEIQGP-EAGMGLDGLLRQRA 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 208 --ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQATVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKF 285
Cdd:PRK14099 242 drLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTL 320

                        250       260
                 ....*....|....*....|....*....
gi 292668835 286 IGLDVQIVVLGTGKKKFEQEIEQLEVLYP 314
Cdd:PRK14099 321 LGEGAQLALLGSGDAELEARFRAAAQAYP 349
PRK14098 PRK14098
starch synthase;
93-316 3.44e-47

starch synthase;


Pssm-ID: 172588 [Multi-domain]  Cd Length: 489  Bit Score: 165.68  E-value: 3.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  93 NDWHTALIPCYLKSMYQSRGIYLNAKVAFCIHNIAYQGRFAFSDFPLLnLPDEFRGSFDfidghekpVKGRKINWMKAGI 172
Cdd:PRK14098 148 HDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEVCSGLH--------REGDEVNMLYTGV 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 173 LESDRVVTVSPYYAQELVSAVDKGVELDNVL--RKTSITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQA 250
Cdd:PRK14098 219 EHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLE 297

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 292668835 251 TVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 316
Cdd:PRK14098 298 EVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQ 363
PLN02939 PLN02939
transferase, transferring glycosyl groups
 53-297 5.90e-28

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 114.23  E-value: 5.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  53 DNELRFSLLCQAALEaprvLNLNCSKYFsgpygeDVLFiANDWHTALI-PCYLkSMYQSRGIYlNAKVAFCIHNIAYQGR 131
Cdd:PLN02939 588 DDFKRFSYFSRAALE----LLYQSGKKP------DIIH-CHDWQTAFVaPLYW-DLYAPKGFN-SARICFTCHNFEYQGT 654

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 132 FAFSDFPL-------LNLPDEFRgsfDFIDGHEKPVKGrkinwmkaGILESDRVVTVSPYYAQELVSAVDKGVELDNVLR 204
Cdd:PLN02939 655 APASDLAScgldvhqLDRPDRMQ---DNAHGRINVVKG--------AIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFH 723

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 205 KTSITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQATVGLP-VDRKIPLIGFIGRLEEQKGSDILVAAIH 283
Cdd:PLN02939 724 SKKFVGILNGIDTDTWNPSTDRFLKVQYNAND-LQGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIY 802

                        250
                 ....*....|....
gi 292668835 284 KFIGLDVQIVVLGT 297
Cdd:PLN02939 803 KTAELGGQFVLLGS 816
PLN02316 PLN02316
synthase/transferase
 42-297 1.32e-18

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 86.85  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835   42 IYGPKagqdylDNELRFSLLCQAALEAPRvlnlncskyfSGPYGEDVLFiANDWHTALIPCYLKSMYQSRGIyLNAKVAF 121
Cdd:PLN02316  682 VYGCR------NDGERFGFFCHAALEFLL----------QSGFHPDIIH-CHDWSSAPVAWLFKDHYAHYGL-SKARVVF 743

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  122 CIHNIayqgrfafsdfpllnlpdEFrgsfdfidghekpvkgrKINWMKAGILESDRVVTVSPYYAQELV--SAVdkgvel 199
Cdd:PLN02316  744 TIHNL------------------EF-----------------GANHIGKAMAYADKATTVSPTYSREVSgnSAI------ 782

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835  200 dnVLRKTSITGIVNGMDTQEWNPATDKYTDVKYDITTVMDAKPLLKEALQATVGL-PVDrkIPLIGFIGRLEEQKGSDIL 278
Cdd:PLN02316  783 --APHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLkQAD--LPLVGIITRLTHQKGIHLI 858

                         250
                  ....*....|....*....
gi 292668835  279 VAAIHKFIGLDVQIVVLGT 297
Cdd:PLN02316  859 KHAIWRTLERNGQVVLLGS 877
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 146-315 6.65e-07

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 50.23  E-value: 6.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 146 FRGSFDFIDGHEKPVKGRKINWMKAGILESDRVVTVSPYYAQELVSAVdkGVELDNVLRktsitgIVNGMDTQEWNPATD 225
Cdd:cd03801  112 LHGAEPGRLLLLLAAERRLLARAEALLRRADAVIAVSEALRDELRALG--GIPPEKIVV------IPNGVDLERFSPPLR 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 226 KytdvkydittvmdakpllkealqatvGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTGKKKFE 303
Cdd:cd03801  184 R--------------------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLrrGPDVRLVIVGGDGPLRA 237

                        170
                 ....*....|..
gi 292668835 304 QEIEQLEVLYPN 315
Cdd:cd03801  238 ELEELELGLGDR 249
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 174-313 2.35e-04

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: 42.61  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 174 ESDRVVTVSPYYAQELVSAVDKGVELDNVlrktsitgIVNGMDTQEWNPATDKytdvkydittvmdakpllkEALQATVG 253
Cdd:cd03800  163 AADRVIASTPQEADELISLYGADPSRINV--------VPPGVDLERFFPVDRA-------------------EARRARLL 215

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 292668835 254 LPVDRKIPLigFIGRLEEQKGSDILVAAIHKFIGLDVQ---IVVLGT---GKKKFEQEIEQLEVLY 313
Cdd:cd03800  216 LPPDKPVVL--ALGRLDPRKGIDTLVRAFAQLPELRELanlVLVGGPsddPLSMDREELAELAEEL 279
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 228-309 8.63e-04

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 40.80  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 228 TDVKYDITTVMDAKPLLKEALQATvglpvDRKIPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFE 303
Cdd:cd03811  161 IEVIYNPIDIDRIRALAKEPILNE-----PEDGPVILAVGRLDPQKGHDLLIEAFAKLRkkYPDVKLVILGDGplREELE 235


                 ....*.
gi 292668835 304 QEIEQL 309
Cdd:cd03811  236 KLAKEL 241
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 174-309 1.09e-03

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 40.44  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 174 ESDRVVTVSPYYAQELVSAvdkGVELDNVlrktsiTGIVNGMDTQEWNPATdkytdvkydittvmdakpllkealqATVG 253
Cdd:cd03798  150 RAARVIAVSKALAEELVAL---GVPRDRV------DVIPNGVDPARFQPED-------------------------RGLG 195

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 292668835 254 LPVDRkiPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQL 309
Cdd:cd03798  196 LPLDA--FVILFVGRLIPRKGIDLLLEAFARLAkaRPDVVLLIVGDGplREALRALAEDL 253
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
261-310 7.10e-03

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 36.34  E-value: 7.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 292668835  261 PLIGFIGRL-EEQKGSDILVAAIHKFI--GLDVQIVVLGTGK-KKFEQEIEQLE 310
Cdd:pfam13692   2 PVILFVGRLhPNVKGVDYLLEAVPLLRkrDNDVRLVIVGDGPeEELEELAAGLE 55
 
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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