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Conserved domains on  [gi|77021585|gb|ABA60651|]
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granule-bound starch synthase, partial [Solanum nitidum]

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 ...
 1-323 3.56e-111

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: 331.06  E-value: 3.56e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   1 EVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKVWGKtdskiygPKAGQDYLDNELRFSLLCQAALEAPRVLNLNCsky 80
Cdd:cd03791  60 EVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRLGFQP--- 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  81 fsgpygeDVFfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGYEKP 160
Cdd:cd03791 130 -------DII-HANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 161 vkgRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRK--TCITGIVNGMDTQEWNPATDKYTDVKYDiTTV 238
Cdd:cd03791 197 ---GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRAraGKLSGILNGIDYDEWNPATDKLIPANYS-AND 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 239 MDAKPLLKEALQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKA 318
Cdd:cd03791 272 LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKV 351


                ....*
gi 77021585 319 KGVAK 323
Cdd:cd03791 352 AVVIG 356
 
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 ...
 1-323 3.56e-111

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: 331.06  E-value: 3.56e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   1 EVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKVWGKtdskiygPKAGQDYLDNELRFSLLCQAALEAPRVLNLNCsky 80
Cdd:cd03791  60 EVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRLGFQP--- 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  81 fsgpygeDVFfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGYEKP 160
Cdd:cd03791 130 -------DII-HANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 161 vkgRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRK--TCITGIVNGMDTQEWNPATDKYTDVKYDiTTV 238
Cdd:cd03791 197 ---GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRAraGKLSGILNGIDYDEWNPATDKLIPANYS-AND 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 239 MDAKPLLKEALQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKA 318
Cdd:cd03791 272 LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKV 351


                ....*
gi 77021585 319 KGVAK 323
Cdd:cd03791 352 AVVIG 356
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 1-323 5.38e-101

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: 304.96  E-value: 5.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585     1 EVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktDSKIYGPkagqDYLDNELRFSLLCQAALEAPRVLNlncsky 80
Cdd:TIGR02095  62 DLSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDR-----PGGIYGD----DYPDNAERFAFFSRAAAELLSGLG------ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585    81 fsgpYGEDVFfIANDWHTALIPCYLKSMYQSrgiyLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGSFDFIDGyekp 160
Cdd:TIGR02095 127 ----WQPDVV-HAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFY---- 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   161 vkgRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVL--RKTCITGIVNGMDTQEWNPATDKYTDVKYDITTv 238
Cdd:TIGR02095 194 ---GRVNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLkaRSGKLRGILNGIDTEVWNPATDPYLKANYSADD- 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   239 MDAKPLLKEALQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKA 318
Cdd:TIGR02095 269 LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNV 348


                  ....*
gi 77021585   319 KGVAK 323
Cdd:TIGR02095 349 RVIIG 353
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
1-317 1.19e-91

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 280.82  E-value: 1.19e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   1 EVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktdSKIYGPkAGQDYLDNELRFSLLCQAALEAPRVLNLNCsky 80
Cdd:COG0297  61 EVPLGGRTYYARVLEGPDDGVPVYFIDNPELFDR------PGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP--- 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  81 fsgpygeDVffI-ANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGYEK 159
Cdd:COG0297 131 -------DI--IhCHDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEF 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 160 PvkGrKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVL--RKTCITGIVNGMDTQEWNPATDKYTDVKYDITT 237
Cdd:COG0297 197 Y--G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLraRSGKLSGILNGIDYDVWNPATDPYLPANYSADD 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 238 vMDAKPLLKEALQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 317
Cdd:COG0297 273 -LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
glgA PRK00654
glycogen synthase GlgA;
11-317 1.68e-75

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 238.86  E-value: 1.68e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   11 VRFFHCYKRGVDRVFVDHPMFlekvwgktdskiYGPKAGQDYLDNELRFSLLCQAALEAprvlnlnCSKYFSGPygeDVF 90
Cdd:PRK00654  65 VLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF-------AEGLDPRP---DIV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   91 FiANDWHTALIPCYLKSMYQSRgiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsFDfIDGYEKPvkgRKINWMK 170
Cdd:PRK00654 123 H-AHDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEA---FH-LEGLEFY---GQISFLK 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  171 AGILESHRVVTVSPYYAQELVSAvDKGVELDNVLR----KtcITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLK 246
Cdd:PRK00654 193 AGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLRarsgK--LSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENK 268

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77021585  247 EALQAAVGLPVDrKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 317
Cdd:PRK00654 269 RALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGK 338
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
9-206 2.23e-55

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 180.22  E-value: 2.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585     9 EIVRFFHCYKRGVDRVFVDHPMFLEKvwgktdSKIYGPKaGQDYLDNELRFSLLCQAALEAPRVLNlncskyfsgpYGED 88
Cdd:pfam08323  69 LTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKLG----------WIPD 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585    89 VFfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGsfdfIDGYEKPvkgRKINW 168
Cdd:pfam08323 132 II-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY---GQINF 202

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 77021585   169 MKAGILESHRVVTVSPYYAQELVSAVDkGVELDNVLRK 206
Cdd:pfam08323 203 LKAGIVYADAVTTVSPTYAEEIQTPEF-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 ...
 1-323 3.56e-111

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: 331.06  E-value: 3.56e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   1 EVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKVWGKtdskiygPKAGQDYLDNELRFSLLCQAALEAPRVLNLNCsky 80
Cdd:cd03791  60 EVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALELLRRLGFQP--- 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  81 fsgpygeDVFfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGYEKP 160
Cdd:cd03791 130 -------DII-HANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFY 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 161 vkgRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRK--TCITGIVNGMDTQEWNPATDKYTDVKYDiTTV 238
Cdd:cd03791 197 ---GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRAraGKLSGILNGIDYDEWNPATDKLIPANYS-AND 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 239 MDAKPLLKEALQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKA 318
Cdd:cd03791 272 LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKV 351


                ....*
gi 77021585 319 KGVAK 323
Cdd:cd03791 352 AVVIG 356
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 1-323 5.38e-101

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: 304.96  E-value: 5.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585     1 EVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktDSKIYGPkagqDYLDNELRFSLLCQAALEAPRVLNlncsky 80
Cdd:TIGR02095  62 DLSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDR-----PGGIYGD----DYPDNAERFAFFSRAAAELLSGLG------ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585    81 fsgpYGEDVFfIANDWHTALIPCYLKSMYQSrgiyLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGSFDFIDGyekp 160
Cdd:TIGR02095 127 ----WQPDVV-HAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFY---- 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   161 vkgRKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVL--RKTCITGIVNGMDTQEWNPATDKYTDVKYDITTv 238
Cdd:TIGR02095 194 ---GRVNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLkaRSGKLRGILNGIDTEVWNPATDPYLKANYSADD- 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   239 MDAKPLLKEALQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKA 318
Cdd:TIGR02095 269 LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNV 348


                  ....*
gi 77021585   319 KGVAK 323
Cdd:TIGR02095 349 RVIIG 353
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
1-317 1.19e-91

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 280.82  E-value: 1.19e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   1 EVKVGDSIEIVRFFHCYKRGVDRVFVDHPMFLEKvwgktdSKIYGPkAGQDYLDNELRFSLLCQAALEAPRVLNLNCsky 80
Cdd:COG0297  61 EVPLGGRTYYARVLEGPDDGVPVYFIDNPELFDR------PGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP--- 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  81 fsgpygeDVffI-ANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsfDFIDGYEK 159
Cdd:COG0297 131 -------DI--IhCHDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEF 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 160 PvkGrKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVL--RKTCITGIVNGMDTQEWNPATDKYTDVKYDITT 237
Cdd:COG0297 197 Y--G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLraRSGKLSGILNGIDYDVWNPATDPYLPANYSADD 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 238 vMDAKPLLKEALQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 317
Cdd:COG0297 273 -LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
glgA PRK00654
glycogen synthase GlgA;
11-317 1.68e-75

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 238.86  E-value: 1.68e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   11 VRFFHCYKRGVDRVFVDHPMFlekvwgktdskiYGPKAGQDYLDNELRFSLLCQAALEAprvlnlnCSKYFSGPygeDVF 90
Cdd:PRK00654  65 VLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEF-------AEGLDPRP---DIV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   91 FiANDWHTALIPCYLKSMYQSRgiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFrgsFDfIDGYEKPvkgRKINWMK 170
Cdd:PRK00654 123 H-AHDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEA---FH-LEGLEFY---GQISFLK 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  171 AGILESHRVVTVSPYYAQELVSAvDKGVELDNVLR----KtcITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLK 246
Cdd:PRK00654 193 AGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLRarsgK--LSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENK 268

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77021585  247 EALQAAVGLPVDrKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 317
Cdd:PRK00654 269 RALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGK 338
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
9-206 2.23e-55

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 180.22  E-value: 2.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585     9 EIVRFFHCYKRGVDRVFVDHPMFLEKvwgktdSKIYGPKaGQDYLDNELRFSLLCQAALEAPRVLNlncskyfsgpYGED 88
Cdd:pfam08323  69 LTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKLG----------WIPD 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585    89 VFfIANDWHTALIPCYLKSMYQSRGiYLNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEFRGsfdfIDGYEKPvkgRKINW 168
Cdd:pfam08323 132 II-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY---GQINF 202

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 77021585   169 MKAGILESHRVVTVSPYYAQELVSAVDkGVELDNVLRK 206
Cdd:pfam08323 203 LKAGIVYADAVTTVSPTYAEEIQTPEF-GGGLDGLLRE 239
PRK14099 PRK14099
glycogen synthase GlgA;
49-315 1.34e-48

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 169.13  E-value: 1.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   49 GQDYLDNELRFSLLCQAALEAPRVLnlncskyfSGPYGEDVFFiANDWHTALIPCYLKsmYQSRGiylNAKVAFCIHNIA 128
Cdd:PRK14099 104 GKDWPDNAQRFAALARAAAAIGQGL--------VPGFVPDIVH-AHDWQAGLAPAYLH--YSGRP---APGTVFTIHNLA 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  129 YQGRFAFSDFPLLNLPDEfrgSFDfIDGYEkpVKGrKINWMKAGILESHRVVTVSPYYAQELVSAvDKGVELDNVLRKTC 208
Cdd:PRK14099 170 FQGQFPRELLGALGLPPS---AFS-LDGVE--YYG-GIGYLKAGLQLADRITTVSPTYALEIQGP-EAGMGLDGLLRQRA 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  209 --ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQAAVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKF 286
Cdd:PRK14099 242 drLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTL 320

                        250       260
                 ....*....|....*....|....*....
gi 77021585  287 IGLDVQIVVLGTGKKKFEQEIEQLEVLYP 315
Cdd:PRK14099 321 LGEGAQLALLGSGDAELEARFRAAAQAYP 349
PRK14098 PRK14098
starch synthase;
94-317 1.12e-45

starch synthase;


Pssm-ID: 172588 [Multi-domain]  Cd Length: 489  Bit Score: 161.44  E-value: 1.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   94 NDWHTALIPCYLKSMYQSRGIYLNAKVAFCIHNIAYQGRFAFSDFPLLnLPDEFrgsfdfIDGYEkpVKGRKINWMKAGI 173
Cdd:PRK14098 148 HDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEV------CSGLH--REGDEVNMLYTGV 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  174 LESHRVVTVSPYYAQELVSAVDKGVELDNVL--RKTCITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQA 251
Cdd:PRK14098 219 EHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLE 297

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77021585  252 AVGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 317
Cdd:PRK14098 298 EVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQ 363
PLN02939 PLN02939
transferase, transferring glycosyl groups
 54-298 4.22e-27

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 111.92  E-value: 4.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   54 DNELRFSLLCQAALEaprvLNLNCSKYFsgpygeDVFFiANDWHTALI-PCYLkSMYQSRGIYlNAKVAFCIHNIAYQGR 132
Cdd:PLN02939 588 DDFKRFSYFSRAALE----LLYQSGKKP------DIIH-CHDWQTAFVaPLYW-DLYAPKGFN-SARICFTCHNFEYQGT 654

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  133 FAFSDFPL-------LNLPDEFRGSfdfidgyekpvKGRKINWMKAGILESHRVVTVSPYYAQELVSAVDKGVELDNVLR 205
Cdd:PLN02939 655 APASDLAScgldvhqLDRPDRMQDN-----------AHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFH 723

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585  206 KTCITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQAAVGLP-VDRKIPLIGFIGRLEEQKGSDILVAAIH 284
Cdd:PLN02939 724 SKKFVGILNGIDTDTWNPSTDRFLKVQYNAND-LQGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIY 802

                        250
                 ....*....|....
gi 77021585  285 KFIGLDVQIVVLGT 298
Cdd:PLN02939 803 KTAELGGQFVLLGS 816
PLN02316 PLN02316
synthase/transferase
 43-298 4.44e-17

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 82.23  E-value: 4.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585    43 IYGPKagqdylDNELRFSLLCQAALE-------APRVLNlncskyfsgpygedvffiANDWHTALIPCYLKSMYQSRGIy 115
Cdd:PLN02316  682 VYGCR------NDGERFGFFCHAALEfllqsgfHPDIIH------------------CHDWSSAPVAWLFKDHYAHYGL- 736

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   116 LNAKVAFCIHNIayqgrfafsdfpllnlpdEFrgsfdfidgyekpvkgrKINWMKAGILESHRVVTVSPYYAQElvsaVD 195
Cdd:PLN02316  737 SKARVVFTIHNL------------------EF-----------------GANHIGKAMAYADKATTVSPTYSRE----VS 777

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585   196 KGVELDNVLRKtcITGIVNGMDTQEWNPATDKYTDVKYDITTVMDAKPLLKEALQAAVGL-PVDrkIPLIGFIGRLEEQK 274
Cdd:PLN02316  778 GNSAIAPHLYK--FHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLkQAD--LPLVGIITRLTHQK 853

                         250       260
                  ....*....|....*....|....
gi 77021585   275 GSDILVAAIHKFIGLDVQIVVLGT 298
Cdd:PLN02316  854 GIHLIKHAIWRTLERNGQVVLLGS 877
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 147-316 7.91e-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: 7.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 147 FRGSFDFIDGYEKPVKGRKINWMKAGILESHRVVTVSPYYAQELVSAvdkgveldNVLRKTCITGIVNGMDTQEWNPATD 226
Cdd:cd03801 112 LHGAEPGRLLLLLAAERRLLARAEALLRRADAVIAVSEALRDELRAL--------GGIPPEKIVVIPNGVDLERFSPPLR 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 227 KytdvkydittvmdakpllkealqaavGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTGKKKFE 304
Cdd:cd03801 184 R--------------------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLrrGPDVRLVIVGGDGPLRA 237

                       170
                ....*....|..
gi 77021585 305 QEIEQLEVLYPN 316
Cdd:cd03801 238 ELEELELGLGDR 249
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 258-310 9.90e-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: 40.42  E-value: 9.90e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 77021585 258 DRKIPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQL 310
Cdd:cd03811 185 PEDGPVILAVGRLDPQKGHDLLIEAFAKLRkkYPDVKLVILGDGplREELEKLAKEL 241
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 175-314 1.00e-03

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: 40.69  E-value: 1.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 175 ESHRVVTVSPYYAQELVSAVDKGVELDNVlrktcitgIVNGMDTQEWNPATDKytdvkydittvmdakpllkEALQAAVG 254
Cdd:cd03800 163 AADRVIASTPQEADELISLYGADPSRINV--------VPPGVDLERFFPVDRA-------------------EARRARLL 215

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77021585 255 LPVDRKIPLigFIGRLEEQKGSDILVAAIHKFIGLDVQ---IVVLGT---GKKKFEQEIEQLEVLY 314
Cdd:cd03800 216 LPPDKPVVL--ALGRLDPRKGIDTLVRAFAQLPELRELanlVLVGGPsddPLSMDREELAELAEEL 279
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 178-310 4.88e-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: 38.51  E-value: 4.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77021585 178 RVVTVSPYYAQELVSAvdkGVELDNVlrktciTGIVNGMDTQEWNPATdkytdvkydittvmdakpllkealqAAVGLPV 257
Cdd:cd03798 153 RVIAVSKALAEELVAL---GVPRDRV------DVIPNGVDPARFQPED-------------------------RGLGLPL 198

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 77021585 258 DRkiPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQL 310
Cdd:cd03798 199 DA--FVILFVGRLIPRKGIDLLLEAFARLAkaRPDVVLLIVGDGplREALRALAEDL 253
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
262-311 6.94e-03

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 36.34  E-value: 6.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 77021585   262 PLIGFIGRL-EEQKGSDILVAAIHKFI--GLDVQIVVLGTGK-KKFEQEIEQLE 311
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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