|
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 ... |
1-353 |
3.84e-130 |
|
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: 380.37 E-value: 3.84e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 1 DAWDTSVVV---EVKVGDRIESVRFFHCYKRGVDRVFVDHPMFLEKVWGKtgskiygPKTGQDYLDNEIRFSLLCQAALK 77
Cdd:cd03791 48 DELDGYLRVlglEVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 78 APRVLNLKcskyfsgpygDDVlFIINDWHTALIPCYLKSMYQSRGiYVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYr 157
Cdd:cd03791 121 LLRRLGFQ----------PDI-IHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 158 gsfDFIDGYEKPvkgRKINWMKAGILESHRVVTVSPYYAQELVSAAdKGVELDNVLRKTS--ITGIVNGMDTQEWNPATD 235
Cdd:cd03791 188 ---FHIDGLEFY---GQINFLKAGIVYADRVTTVSPTYAKEILTPE-YGEGLDGVLRARAgkLSGILNGIDYDEWNPATD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 236 KYTDVKYDiTTVMDAKPLLKEALQAAAGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQE 315
Cdd:cd03791 261 KLIPANYS-ANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQA 339
|
330 340 350
....*....|....*....|....*....|....*...
gi 67037830 316 IEQLEVLYPNKAKGVAKFNAPLAHMIIAGADFMLIPSR 353
Cdd:cd03791 340 FRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSR 377
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
4-353 |
4.81e-115 |
|
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: 341.94 E-value: 4.81e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 4 DTSVVVEVKVGDRIESVRFFHCYKRGVDRVFVDHPMFLEKvwgktGSKIYGPktgqDYLDNEIRFSLLCQAALKAPRVLN 83
Cdd:TIGR02095 56 KVVELVDLSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDR-----PGGIYGD----DYPDNAERFAFFSRAAAELLSGLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 84 lkcskyfsgpYGDDVlFIINDWHTALIPCYLKSMYQSrgiyVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYRGSFDFI 163
Cdd:TIGR02095 127 ----------WQPDV-VHAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 164 DGyekpvkgRKINWMKAGILESHRVVTVSPYYAQELVSAaDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVK 241
Cdd:TIGR02095 192 FY-------GRVNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKAN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 242 YDITTvMDAKPLLKEALQAAAGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEV 321
Cdd:TIGR02095 264 YSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAE 342
|
330 340 350
....*....|....*....|....*....|..
gi 67037830 322 LYPNKAKGVAKFNAPLAHMIIAGADFMLIPSR 353
Cdd:TIGR02095 343 RYPGNVRVIIGYDEALAHLIYAGADFILMPSR 374
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
9-353 |
1.93e-104 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 314.72 E-value: 1.93e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 9 VEVKVGDRIESVRFFHCYKRGVDRVFVDHPMFLEkvwgktGSKIYGPkTGQDYLDNEIRFSLLCQAALKAPRVLNLKCsk 88
Cdd:COG0297 60 LEVPLGGRTYYARVLEGPDDGVPVYFIDNPELFD------RPGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 89 yfsgpygdDVLFIiNDWHTALIPCYLKSMYQSRGiYVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYrgsfDFIDGYEK 168
Cdd:COG0297 131 --------DIIHC-HDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 169 PvkGrKINWMKAGILESHRVVTVSPYYAQELVSAAdKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITT 246
Cdd:COG0297 197 Y--G-QINFLKAGIVYADRVTTVSPTYAREIQTPE-FGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 247 vMDAKPLLKEALQAAAGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 326
Cdd:COG0297 273 -LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
|
330 340
....*....|....*....|....*..
gi 67037830 327 AKGVAKFNAPLAHMIIAGADFMLIPSR 353
Cdd:COG0297 352 VAVYIGYDEALAHRIYAGADFFLMPSR 378
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
19-353 |
6.49e-89 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 274.69 E-value: 6.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 19 SVRFFHCYKRGVDRVFVDHPMFlekvwgktgskiYGPKTGQDYLDNEIRFSLLCQAALKAPRVLNLKcskyfsgPygdDV 98
Cdd:PRK00654 64 TVLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPR-------P---DI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 99 LFIiNDWHTALIPCYLKSMYQSRgiYVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYrgsFDfIDGYEKPvkgRKINWM 178
Cdd:PRK00654 122 VHA-HDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEA---FH-LEGLEFY---GQISFL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 179 KAGILESHRVVTVSPYYAQELVSAADkGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKE 256
Cdd:PRK00654 192 KAGLYYADRVTTVSPTYAREITTPEF-GYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 257 ALQAAAGLPVDrKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNAP 336
Cdd:PRK00654 270 ALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEA 348
|
330
....*....|....*..
gi 67037830 337 LAHMIIAGADFMLIPSR 353
Cdd:PRK00654 349 LAHRIYAGADMFLMPSR 365
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
13-215 |
2.39e-54 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 178.29 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 13 VGDRIESVRFFHCYKRGVDRVFVDHPMFLEKvwgktgSKIYGPKtGQDYLDNEIRFSLLCQAALKAPRVLNlkcskyfsg 92
Cdd:pfam08323 64 VPVRPLTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKLG--------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 93 pYGDDVLfIINDWHTALIPCYLKSMYQSRGiYVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYRGsfdfIDGYEKPvkg 172
Cdd:pfam08323 128 -WIPDII-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY--- 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 67037830 173 RKINWMKAGILESHRVVTVSPYYAQELVSAADkGVELDNVLRK 215
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 ... |
1-353 |
3.84e-130 |
|
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: 380.37 E-value: 3.84e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 1 DAWDTSVVV---EVKVGDRIESVRFFHCYKRGVDRVFVDHPMFLEKVWGKtgskiygPKTGQDYLDNEIRFSLLCQAALK 77
Cdd:cd03791 48 DELDGYLRVlglEVKVGGRGEEVGVFELPVDGVDYYFLDNPEFFDRPGLP-------GPPGYDYPDNAERFAFFSRAALE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 78 APRVLNLKcskyfsgpygDDVlFIINDWHTALIPCYLKSMYQSRGiYVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYr 157
Cdd:cd03791 121 LLRRLGFQ----------PDI-IHANDWHTALVPAYLKTRYRGPG-FKKIKTVFTIHNLAYQGLFPLDTLAELGLPPEL- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 158 gsfDFIDGYEKPvkgRKINWMKAGILESHRVVTVSPYYAQELVSAAdKGVELDNVLRKTS--ITGIVNGMDTQEWNPATD 235
Cdd:cd03791 188 ---FHIDGLEFY---GQINFLKAGIVYADRVTTVSPTYAKEILTPE-YGEGLDGVLRARAgkLSGILNGIDYDEWNPATD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 236 KYTDVKYDiTTVMDAKPLLKEALQAAAGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQE 315
Cdd:cd03791 261 KLIPANYS-ANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQA 339
|
330 340 350
....*....|....*....|....*....|....*...
gi 67037830 316 IEQLEVLYPNKAKGVAKFNAPLAHMIIAGADFMLIPSR 353
Cdd:cd03791 340 FRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSR 377
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
4-353 |
4.81e-115 |
|
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: 341.94 E-value: 4.81e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 4 DTSVVVEVKVGDRIESVRFFHCYKRGVDRVFVDHPMFLEKvwgktGSKIYGPktgqDYLDNEIRFSLLCQAALKAPRVLN 83
Cdd:TIGR02095 56 KVVELVDLSVGPRTLYVKVFEGVVEGVPVYFIDNPSLFDR-----PGGIYGD----DYPDNAERFAFFSRAAAELLSGLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 84 lkcskyfsgpYGDDVlFIINDWHTALIPCYLKSMYQSrgiyVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYRGSFDFI 163
Cdd:TIGR02095 127 ----------WQPDV-VHAHDWHTALVPALLKAVYRP----NPIKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 164 DGyekpvkgRKINWMKAGILESHRVVTVSPYYAQELVSAaDKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVK 241
Cdd:TIGR02095 192 FY-------GRVNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKAN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 242 YDITTvMDAKPLLKEALQAAAGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEV 321
Cdd:TIGR02095 264 YSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAE 342
|
330 340 350
....*....|....*....|....*....|..
gi 67037830 322 LYPNKAKGVAKFNAPLAHMIIAGADFMLIPSR 353
Cdd:TIGR02095 343 RYPGNVRVIIGYDEALAHLIYAGADFILMPSR 374
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
9-353 |
1.93e-104 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 314.72 E-value: 1.93e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 9 VEVKVGDRIESVRFFHCYKRGVDRVFVDHPMFLEkvwgktGSKIYGPkTGQDYLDNEIRFSLLCQAALKAPRVLNLKCsk 88
Cdd:COG0297 60 LEVPLGGRTYYARVLEGPDDGVPVYFIDNPELFD------RPGPYGD-PDRDYPDNAERFAFFSRAALELLKGLDWKP-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 89 yfsgpygdDVLFIiNDWHTALIPCYLKSMYQSRGiYVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYrgsfDFIDGYEK 168
Cdd:COG0297 131 --------DIIHC-HDWQTGLIPALLKTRYADDP-FKRIKTVFTIHNLAYQGIFPAEILELLGLPPEL----FTPDGLEF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 169 PvkGrKINWMKAGILESHRVVTVSPYYAQELVSAAdKGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITT 246
Cdd:COG0297 197 Y--G-QINFLKAGIVYADRVTTVSPTYAREIQTPE-FGEGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 247 vMDAKPLLKEALQAAAGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNK 326
Cdd:COG0297 273 -LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGR 351
|
330 340
....*....|....*....|....*..
gi 67037830 327 AKGVAKFNAPLAHMIIAGADFMLIPSR 353
Cdd:COG0297 352 VAVYIGYDEALAHRIYAGADFFLMPSR 378
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
19-353 |
6.49e-89 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 274.69 E-value: 6.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 19 SVRFFHCYKRGVDRVFVDHPMFlekvwgktgskiYGPKTGQDYLDNEIRFSLLCQAALKAPRVLNLKcskyfsgPygdDV 98
Cdd:PRK00654 64 TVLFGHLEGDGVPVYLIDAPHL------------FDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPR-------P---DI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 99 LFIiNDWHTALIPCYLKSMYQSRgiYVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYrgsFDfIDGYEKPvkgRKINWM 178
Cdd:PRK00654 122 VHA-HDWHTGLIPALLKEKYWRG--YPDIKTVFTIHNLAYQGLFPAEILGELGLPAEA---FH-LEGLEFY---GQISFL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 179 KAGILESHRVVTVSPYYAQELVSAADkGVELDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKE 256
Cdd:PRK00654 192 KAGLYYADRVTTVSPTYAREITTPEF-GYGLEGLLRARSgkLSGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 257 ALQAAAGLPVDrKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNAP 336
Cdd:PRK00654 270 ALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEA 348
|
330
....*....|....*..
gi 67037830 337 LAHMIIAGADFMLIPSR 353
Cdd:PRK00654 349 LAHRIYAGADMFLMPSR 365
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
49-353 |
3.20e-57 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 193.01 E-value: 3.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 49 GSKIYGPKtGQDYLDNEIRFSLLCQAALKAPRVLnlkcskyfSGPYGDDVLFIiNDWHTALIPCYLKsmYQSRGiyvNAK 128
Cdd:PRK14099 96 GNPYVGPD-GKDWPDNAQRFAALARAAAAIGQGL--------VPGFVPDIVHA-HDWQAGLAPAYLH--YSGRP---APG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 129 VAFCIHNIAYQGRFAFSDFPLLNLPDEyrgSFDfIDGYEkpVKGrKINWMKAGILESHRVVTVSPYYAQElVSAADKGVE 208
Cdd:PRK14099 161 TVFTIHNLAFQGQFPRELLGALGLPPS---AFS-LDGVE--YYG-GIGYLKAGLQLADRITTVSPTYALE-IQGPEAGMG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 209 LDNVLRKTS--ITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQAAAGLPVDRKIPLIGFIGRLEEQKGSD 286
Cdd:PRK14099 233 LDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLD 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67037830 287 ILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNAPLAHMIIAGADFMLIPSR 353
Cdd:PRK14099 312 LLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSR 378
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
13-215 |
2.39e-54 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 178.29 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 13 VGDRIESVRFFHCYKRGVDRVFVDHPMFLEKvwgktgSKIYGPKtGQDYLDNEIRFSLLCQAALKAPRVLNlkcskyfsg 92
Cdd:pfam08323 64 VPVRPLTVGVARLELDGVDVYFLDNPDYFDR------PGLYGDD-GRDYEDNAERFAFFSRAALELAKKLG--------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 93 pYGDDVLfIINDWHTALIPCYLKSMYQSRGiYVNAKVAFCIHNIAYQGRFAFSDFPLLNLPDEYRGsfdfIDGYEKPvkg 172
Cdd:pfam08323 128 -WIPDII-HCHDWHTALVPAYLKEAYADDP-FKNIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFY--- 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 67037830 173 RKINWMKAGILESHRVVTVSPYYAQELVSAADkGVELDNVLRK 215
Cdd:pfam08323 198 GQINFLKAGIVYADAVTTVSPTYAEEIQTPEF-GGGLDGLLRE 239
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
103-353 |
9.90e-53 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 181.47 E-value: 9.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 103 NDWHTALIPCYLKSMYQSRGIYVNAKVAFCIHNIAYQGRFAFSDFPLLnLPDEyrgsfdFIDGYEkpVKGRKINWMKAGI 182
Cdd:PRK14098 148 HDWYAGLVPLLLKTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEE------VCSGLH--REGDEVNMLYTGV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 183 LESHRVVTVSPYYAQELVSAADKGVELDNVL--RKTSITGIVNGMDTQEWNPATDKYTDVKYDITTvMDAKPLLKEALQA 260
Cdd:PRK14098 219 EHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 261 AAGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGVAKFNAPLAHM 340
Cdd:PRK14098 298 EVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHL 377
|
250
....*....|...
gi 67037830 341 IIAGADFMLIPSR 353
Cdd:PRK14098 378 AIAGLDMLLMPGK 390
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
34-352 |
1.49e-32 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 128.87 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 34 FVDHPMFLEKVWGKT--GSKIY--GPK-------TGQDY--LDNEIRFSLLCQAALKAprvlnlkcsKYFSGPYGDdvlf 100
Cdd:PLN02939 546 YFDGNLFKNKIWTGTveGLPVYfiEPQhpskffwRAQYYgeHDDFKRFSYFSRAALEL---------LYQSGKKPD---- 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 101 IIN--DWHTALI-PCYLkSMYQSRGiYVNAKVAFCIHNIAYQGRFAFSDFPL-------LNLPDEYRGSfdfidgyekpv 170
Cdd:PLN02939 613 IIHchDWQTAFVaPLYW-DLYAPKG-FNSARICFTCHNFEYQGTAPASDLAScgldvhqLDRPDRMQDN----------- 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 171 KGRKINWMKAGILESHRVVTVSPYYAQELVSAADKGVELDNVLRKTSITGIVNGMDTQEWNPATDKYTDVKYDITTvMDA 250
Cdd:PLN02939 680 AHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNAND-LQG 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 251 KPLLKEALQAAAGLP-VDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTG-----KKKFEQEIEQLEvlYP 324
Cdd:PLN02939 759 KAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSpvphiQREFEGIADQFQ--SN 836
|
330 340
....*....|....*....|....*...
gi 67037830 325 NKAKGVAKFNAPLAHMIIAGADFMLIPS 352
Cdd:PLN02939 837 NNIRLILKYDEALSHSIYAASDMFIIPS 864
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
52-352 |
2.26e-25 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 107.65 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 52 IYGPKtgqdylDNEIRFSLLCQAALKAPRVlnlkcskyfSGPYGDdvlfIIN--DWHTALIPCYLKSMYQSRGIyVNAKV 129
Cdd:PLN02316 682 VYGCR------NDGERFGFFCHAALEFLLQ---------SGFHPD----IIHchDWSSAPVAWLFKDHYAHYGL-SKARV 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 130 AFCIHNIAYqgrfafsdfpllnlpdeyrgsfdfidgyekpvkgrKINWMKAGILESHRVVTVSPYYAQELVSAADKGVEL 209
Cdd:PLN02316 742 VFTIHNLEF-----------------------------------GANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHL 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 210 dnvlrkTSITGIVNGMDTQEWNPATDKYTDVKYDITTVMDAKPLLKEALQAAAGL-PVDrkIPLIGFIGRLEEQKGSDIL 288
Cdd:PLN02316 787 ------YKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLkQAD--LPLVGIITRLTHQKGIHLI 858
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67037830 289 VAAIHKFIGLDVQIVVLGTG-----KKKFEQEIEQLEVLYPNKAKGVAKFNAPLAHMIIAGADFMLIPS 352
Cdd:PLN02316 859 KHAIWRTLERNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPS 927
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
158-353 |
1.47e-08 |
|
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: 55.62 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 158 GSFDFIDGYEKPVKGRKINWMKAGILESHRVVTVSPYYAQELVSAadkgveldNVLRKTSITGIVNGMDTQEWNPATdky 237
Cdd:cd03801 114 GAEPGRLLLLLAAERRLLARAEALLRRADAVIAVSEALRDELRAL--------GGIPPEKIVVIPNGVDLERFSPPL--- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 238 tdvkydittvmdakpllkealqaAAGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTGkkkfEQE 315
Cdd:cd03801 183 -----------------------RRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLrrGPDVRLVIVGGD----GPL 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 67037830 316 IEQLEVLYPNKAKGVaKF----NAPLAHMIIAGADFMLIPSR 353
Cdd:cd03801 236 RAELEELELGLGDRV-RFlgfvPDEELPALYAAADVFVLPSR 276
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
187-353 |
4.63e-04 |
|
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: 41.60 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 187 RVVTVSPYYAQELVSAadkGVELDNVlrktsiTGIVNGMDTQEWNPATdkytdvkydittvmdakpllkealqAAAGLPV 266
Cdd:cd03798 153 RVIAVSKALAEELVAL---GVPRDRV------DVIPNGVDPARFQPED-------------------------RGLGLPL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 267 DRkiPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQLevlypNKAKGVaKFNAPLAHMII 342
Cdd:cd03798 199 DA--FVILFVGRLIPRKGIDLLLEAFARLAkaRPDVVLLIVGDGplREALRALAEDL-----GLGDRV-TFTGRLPHEQV 270
|
170
....*....|....*
gi 67037830 343 AG----ADFMLIPSR 353
Cdd:cd03798 271 PAyyraCDVFVLPSR 285
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
273-353 |
6.61e-04 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 41.16 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 273 IGFIGRLEEQKGSDILVAAIHKFIGLDVQIVVLGTGKkkfEQEIEQLEVLYPNKAKGVAKFNAPLAHMiiAGADFMLIPS 352
Cdd:cd03823 194 FGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGP---LSDERQIEGGRRIAFLGRVPTDDIKDFY--EKIDVLVVPS 268
|
.
gi 67037830 353 R 353
Cdd:cd03823 269 I 269
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
267-353 |
7.92e-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: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 267 DRKIPLIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQL----EVLYPNKAKGVAKFnapla 338
Cdd:cd03811 185 PEDGPVILAVGRLDPQKGHDLLIEAFAKLRkkYPDVKLVILGDGplREELEKLAKELglaeRVIFLGFQSNPYPY----- 259
|
90
....*....|....*
gi 67037830 339 hmiIAGADFMLIPSR 353
Cdd:cd03811 260 ---LKKADLFVLSSR 271
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
271-353 |
9.40e-04 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 39.03 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 271 PLIGFIGRL-EEQKGSDILVAAIHKFI--GLDVQIVVLGTGkkkfeqEIEQLEVLYPNKAKGVaKFNAPLAHM--IIAGA 345
Cdd:pfam13692 2 PVILFVGRLhPNVKGVDYLLEAVPLLRkrDNDVRLVIVGDG------PEEELEELAAGLEDRV-IFTGFVEDLaeLLAAA 74
|
....*...
gi 67037830 346 DFMLIPSR 353
Cdd:pfam13692 75 DVFVLPSL 82
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
275-353 |
4.95e-03 |
|
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.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 38.15 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 275 FIGRLEEQKGSDILVAAIHK----FIGLDVQIVVLGTGKKKFEQEIEQLEVLYPNKAKGvAKFNAPLAHMIIAGADFMLI 350
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALlkarLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIG-GLVDDEVLELLLAAADVFVL 193
|
...
gi 67037830 351 PSR 353
Cdd:cd01635 194 PSR 196
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
173-353 |
5.63e-03 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 38.47 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 173 RKINWMKAGILEshrVVTVSPYYAQELVSAAdkgveldnVLRKTSITGIVNGMDTQEWNPAtDKytdvkydittvMDAKP 252
Cdd:cd03825 129 RKREALAKKRLT---IVAPSRWLADMVRRSP--------LLKGLPVVVIPNGIDTEIFAPV-DK-----------AKARK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 253 LLkealqaaaGLPVDRKIPLIGFIGRLEEQKGSDILVAAIHKFIGLD-VQIVVLG-TGKKKFEQEIEQLEVLYPNkakgv 330
Cdd:cd03825 186 RL--------GIPQDKKVILFGAESVTKPRKGFDELIEALKLLATKDdLLLVVFGkNDPQIVILPFDIISLGYID----- 252
|
170 180
....*....|....*....|...
gi 67037830 331 akfNAPLAHMIIAGADFMLIPSR 353
Cdd:cd03825 253 ---DDEQLVDIYSAADLFVHPSL 272
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
272-352 |
6.21e-03 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).
Pssm-ID: 340840 [Multi-domain] Cd Length: 357 Bit Score: 38.04 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 272 LIGFIGRLEEQKGSDILVAAIHKFI--GLDVQIVVLGTG--KKKFEQEIEQLE----VLYPNKAKGVAKFnapLAHMiia 343
Cdd:cd03812 193 VLGHVGRFNEQKNHSFLIDIFEELKkkNPNVKLVLVGEGelKEKIKEKVKELGledkVIFLGFRNDVSEI---LSAM--- 266
|
....*....
gi 67037830 344 gaDFMLIPS 352
Cdd:cd03812 267 --DVFLFPS 273
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
184-323 |
6.51e-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: 37.99 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67037830 184 ESHRVVTVSPYYAQEL---VSAADKGVELdnvlrktsitgIVNGMDTQEWNPATDKytdvkydittvmdakpllkEALQA 260
Cdd:cd03800 163 AADRVIASTPQEADELislYGADPSRINV-----------VPPGVDLERFFPVDRA-------------------EARRA 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67037830 261 AAGLPVDRKIPLigFIGRLEEQKGSDILVAAIHKFIGLDVQ---IVVLGT---GKKKFEQEIEQLEVLY 323
Cdd:cd03800 213 RLLLPPDKPVVL--ALGRLDPRKGIDTLVRAFAQLPELRELanlVLVGGPsddPLSMDREELAELAEEL 279
|
|
| |
