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Conserved domains on  [gi|75261422|sp|Q6K973|]
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RecName: Full=Sucrose synthase 6; Short=OsSUS6; AltName: Full=Sucrose-UDP glucosyltransferase 6

Protein Classification

sucrose synthase( domain architecture ID 11476401)

sucrose synthase is a sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
 1-814 0e+00

sucrose synthase


:

Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1647.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    1 MAVGLRRSDSIADMMPEALRQSRYQMKRCFQRYVSQGKRLMKRQQLLDELDKSVDDKADKDQLLQGFLGYVISSTQEAAV 80
Cdd:PLN00142   3 AAPVLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVIDDDEERKKLLDGPFGDILRSTQEAIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   81 LPPFVAFAVRMNPGIWEFVKVHSANLSVEQMTPSDYLKNKEALVDDKWgayDDDSQLEVDFGALDLSTPHLTLPSSIGKG 160
Cdd:PLN00142  83 LPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSW---NDNFVLELDFEPFNASFPRPTLSSSIGNG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  161 AHLVSRFMSSKL---TDNKKPLLDYLLALSHRGDKLMINDILDTVDKLQTALLLAEVYVAGLHPDTNYSEFEQKFQEWGL 237
Cdd:PLN00142 160 VQFLNRHLSSKLfrdKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  238 EKGWGDTAETCKETLSSLSEVLQAPDPINMEKFFSTVPCVFTVVIFSIHGYFGQEKVLGMPDTGGQVVYILDQVRALEDE 317
Cdd:PLN00142 240 EKGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  318 LLQRIKQQGLNATPKILVLTRLIPEAKGTKCNVELEPIENTKHSNILRVPFKTEDGkVLPQWVSRFDIYPYLERYAQDSS 397
Cdd:PLN00142 320 MLLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKG-ILRKWISRFDVWPYLETFAEDAA 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  398 VKILEILEGKPDLVIGNYTDGNLVASLLTSKLGVTQGTIAHALEKTKYEDSDIKWRELDHKYHFSCQFTADMIAMNTSDF 477
Cdd:PLN00142 399 SEILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADF 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  478 IIASTYQEIAGSKEKPGQYESHYAFTMPGLCRYATGINVFDPKFNIAAPGADQSVYFPFTQKQKRLTDLHPQIEELLYSK 557
Cdd:PLN00142 479 IITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSP 558

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  558 EDNNEHIGHLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGLLDPSQSKDREEIEEINKMHSLINKY 637
Cdd:PLN00142 559 EQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDPSKSKDREEIAEIKKMHSLIEKY 638

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  638 QLVGQIRWIKGQTDRVRNGELYRCIADTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLN 717
Cdd:PLN00142 639 NLKGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYH 718

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  718 GKEASDKIADFFQKCKEDLIYWSKMSTAGLQRIYECYTWQIYATKVLNMASIYGFWRTLDKEERQAKQHYLHMFYNLQFR 797
Cdd:PLN00142 719 GDEAANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFR 798

                        810
                 ....*....|....*..
gi 75261422  798 KLAKNVPTLGEQPAQPT 814
Cdd:PLN00142 799 ELAKTVPLAVDDPQPPK 815
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
 1-814 0e+00

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1647.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    1 MAVGLRRSDSIADMMPEALRQSRYQMKRCFQRYVSQGKRLMKRQQLLDELDKSVDDKADKDQLLQGFLGYVISSTQEAAV 80
Cdd:PLN00142   3 AAPVLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVIDDDEERKKLLDGPFGDILRSTQEAIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   81 LPPFVAFAVRMNPGIWEFVKVHSANLSVEQMTPSDYLKNKEALVDDKWgayDDDSQLEVDFGALDLSTPHLTLPSSIGKG 160
Cdd:PLN00142  83 LPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSW---NDNFVLELDFEPFNASFPRPTLSSSIGNG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  161 AHLVSRFMSSKL---TDNKKPLLDYLLALSHRGDKLMINDILDTVDKLQTALLLAEVYVAGLHPDTNYSEFEQKFQEWGL 237
Cdd:PLN00142 160 VQFLNRHLSSKLfrdKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  238 EKGWGDTAETCKETLSSLSEVLQAPDPINMEKFFSTVPCVFTVVIFSIHGYFGQEKVLGMPDTGGQVVYILDQVRALEDE 317
Cdd:PLN00142 240 EKGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  318 LLQRIKQQGLNATPKILVLTRLIPEAKGTKCNVELEPIENTKHSNILRVPFKTEDGkVLPQWVSRFDIYPYLERYAQDSS 397
Cdd:PLN00142 320 MLLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKG-ILRKWISRFDVWPYLETFAEDAA 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  398 VKILEILEGKPDLVIGNYTDGNLVASLLTSKLGVTQGTIAHALEKTKYEDSDIKWRELDHKYHFSCQFTADMIAMNTSDF 477
Cdd:PLN00142 399 SEILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADF 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  478 IIASTYQEIAGSKEKPGQYESHYAFTMPGLCRYATGINVFDPKFNIAAPGADQSVYFPFTQKQKRLTDLHPQIEELLYSK 557
Cdd:PLN00142 479 IITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSP 558

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  558 EDNNEHIGHLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGLLDPSQSKDREEIEEINKMHSLINKY 637
Cdd:PLN00142 559 EQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDPSKSKDREEIAEIKKMHSLIEKY 638

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  638 QLVGQIRWIKGQTDRVRNGELYRCIADTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLN 717
Cdd:PLN00142 639 NLKGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYH 718

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  718 GKEASDKIADFFQKCKEDLIYWSKMSTAGLQRIYECYTWQIYATKVLNMASIYGFWRTLDKEERQAKQHYLHMFYNLQFR 797
Cdd:PLN00142 719 GDEAANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFR 798

                        810
                 ....*....|....*..
gi 75261422  798 KLAKNVPTLGEQPAQPT 814
Cdd:PLN00142 799 ELAKTVPLAVDDPQPPK 815
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
 23-804 0e+00

sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274149 [Multi-domain]  Cd Length: 784  Bit Score: 1355.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    23 RYQMKRCFQRYVSQGKRLMKRQQLLDELDKSVDDKADKDQLLQGFLGYVISSTQEAAVLPPFVAFAVRMNPGIWEFVKVH 102
Cdd:TIGR02470   1 RAELRQLLSRYVSQGKRYLLRHQLLDEFEQYCSDADKEKKLSESPLGKLIFSTQEAIVLPPWVALAVRPRIGVWEYVRVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   103 SANLSVEQMTPSDYLKNKEALVDdkwGAYDDDSQLEVDFGALDLSTPHLTLPSSIGKGAHLVSRFMSSKLTDNK---KPL 179
Cdd:TIGR02470  81 VEELSVEELTISEYLDFKEQLVN---GHANDPNVLELDFEPFNASFPRPSDSKSIGNGVQFLNRHLSSKLFQDPesmEPL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   180 LDYLLALSHRGDKLMINDILDTVDKLQTALLLAEVYVAGLHPDTNYSEFEQKFQEWGLEKGWGDTAETCKETLSSLSEVL 259
Cdd:TIGR02470 158 LNFLRVHNYNGIQLMINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   260 QAPDPINMEKFFSTVPCVFTVVIFSIHGYFGQEKVLGMPDTGGQVVYILDQVRALEDELLQRIKQQGLNATPKILVLTRL 339
Cdd:TIGR02470 238 EAPDPSVLEAFLGRIPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   340 IPEAKGTKCNVELEPIENTKHSNILRVPFKTEDGKVLPQWVSRFDIYPYLERYAQDSSVKILEILEGKPDLVIGNYTDGN 419
Cdd:TIGR02470 318 IPDAEGTTCNQRLEKVYGTEHAWILRVPFRTENGIILRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   420 LVASLLTSKLGVTQGTIAHALEKTKYEDSDIKWRELDHKYHFSCQFTADMIAMNTSDFIIASTYQEIAGSKEKPGQYESH 499
Cdd:TIGR02470 398 LVASLLARKLGVTQCTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESH 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   500 YAFTMPGLCRYATGINVFDPKFNIAAPGADQSVYFPFTQKQKRLTDLHPQIEELLYSKEDNNEHIGHLADRSKPIIFSMA 579
Cdd:TIGR02470 478 QAFTMPGLYRVVHGIDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMA 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   580 RLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGLLDPSQSKDREEIEEINKMHSLINKYQLVGQIRWIKGQTDRVRNGELY 659
Cdd:TIGR02470 558 RLDRVKNLTGLVECYGRSPKLRELVNLVVVAGKLDAKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELY 637

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   660 RCIADTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKIADFFQKCKEDLIYW 739
Cdd:TIGR02470 638 RYIADTKGIFVQPALYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYW 717

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75261422   740 SKMSTAGLQRIYECYTWQIYATKVLNMASIYGFWRTLDKEERQAKQHYLHMFYNLQFRKLAKNVP 804
Cdd:TIGR02470 718 QKISQGGLQRIYEKYTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVP 782
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
 15-555 0e+00

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


Pssm-ID: 395692  Cd Length: 540  Bit Score: 1001.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    15 MPEALRQSRYQMKRCFQRYVSQGKRLMKRQQLLDELDKSVDDKADKDQLLQGFLGYVISSTQEAAVLPPFVAFAVRMNPG 94
Cdd:pfam00862   1 VPDALSQSRNELKRLLSRYVAQGKRLMKRHELLDEFEKVIEDKKERSKLMEGLLGKILHSTQEAIVLPPWVAFAVRPRPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    95 IWEFVKVHSANLSVEQMTPSDYLKNKEALVDDKWgayDDDSQLEVDFGALDLSTPHLTLPSSIGKGAHLVSRFMSSKLTD 174
Cdd:pfam00862  81 VWEYVRVNADELSVEELTVSEYLKFKERLVDESW---NDENALELDFGPFNASFPRLTLPSSIGNGVQFLNRHLSSKLFR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   175 NK---KPLLDYLLALSHRGDKLMINDILDTVDKLQTALLLAEVYVAGLHPDTNYSEFEQKFQEWGLEKGWGDTAETCKET 251
Cdd:pfam00862 158 DSeslEPLLDFLRSHNYDGESLMINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKET 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   252 LSSLSEVLQAPDPINMEKFFSTVPCVFTVVIFSIHGYFGQEKVLGMPDTGGQVVYILDQVRALEDELLQRIKQQGLNATP 331
Cdd:pfam00862 238 MHLLSELLQAPDPSTLEKFLGRIPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKP 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   332 KILVLTRLIPEAKGTKCNVELEPIENTKHSNILRVPFKTEDGkVLPQWVSRFDIYPYLERYAQDSSVKILEILEGKPDLV 411
Cdd:pfam00862 318 QILVVTRLIPEARGTTCNQELEKISGTKHSHILRVPFRTENG-ILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLI 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   412 IGNYTDGNLVASLLTSKLGVTQGTIAHALEKTKYEDSDIKWRELDHKYHFSCQFTADMIAMNTSDFIIASTYQEIAGSKE 491
Cdd:pfam00862 397 IGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKD 476

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75261422   492 KPGQYESHYAFTMPGLCRYATGINVFDPKFNIAAPGADQSVYFPFTQKQKRLTDLHPQIEELLY 555
Cdd:pfam00862 477 RVGQYESHTAFTLPGLYRVVSGIDVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 280-765 8.45e-129

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: 391.60  E-value: 8.45e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 280 VVIFSIHGYFGQEkvLGMPDTGGQVVYILDQVRALedellqrikqqgLNATPKILVLTRLIPEAKGtkcnvelEPIENTK 359
Cdd:cd03800   2 IALISVHGSPLAQ--PGGADTGGQNVYVLELARAL------------AELGYQVDIFTRRISPADP-------EVVEIAP 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 360 HSNILRVPFKTEDGkvlpqwVSRFDIYPYLERYAQDSSVKILEILeGKPDLVIGNYTDGNLVASLLTSKLGVTQGTIAHA 439
Cdd:cd03800  61 GARVIRVPAGPPEY------LPKEELWPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 440 LEKTKYEDSDIKWReldhkYHFSCQFTADMIAMNTSDFIIASTYQEIAGSKekpgqyeSHYAftmpglcryatginVFDP 519
Cdd:cd03800 134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELI-------SLYG--------------ADPS 187

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 520 KFNIAAPGADQSVYFPFTQKQKRLTDLhpqieellyskednnehighLADRSKPIIFSMARLDKIKNITGLVEWYGQNKR 599
Cdd:cd03800 188 RINVVPPGVDLERFFPVDRAEARRARL--------------------LLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 600 LRDLVNLVIVGGLLDPSQSKDREEIEEINKMHSLINKYQLVGQIRwikgqtdRVRNGELYRCiadtKGAFVQPALYEAFG 679
Cdd:cd03800 248 LRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVS-------RDDLPELYRA----ADVFVVPSLYEPFG 316

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 680 LTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKIADFFQKCKedliYWSKMSTAGLQRIYECYTWQIY 759
Cdd:cd03800 317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPA----LWQRLSRAGLERARAHYTWESV 392


                ....*.
gi 75261422 760 ATKVLN 765
Cdd:cd03800 393 ADQLLT 398
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 641-766 5.38e-20

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 86.20  E-value: 5.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 641 GQIRWIKGQTDRVRngELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKE 720
Cdd:COG0438   2 GRLVPRKGLDLLLE--ALLAA-AD---VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEA 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 75261422 721 ASDKIADFFqkckEDLIYWSKMSTAGLQRIYECYTWQIYATKVLNM 766
Cdd:COG0438  76 LAEAILRLL----EDPELRRRLGEAARERAEERFSWEAIAERLLAL 117
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
 1-814 0e+00

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1647.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    1 MAVGLRRSDSIADMMPEALRQSRYQMKRCFQRYVSQGKRLMKRQQLLDELDKSVDDKADKDQLLQGFLGYVISSTQEAAV 80
Cdd:PLN00142   3 AAPVLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVIDDDEERKKLLDGPFGDILRSTQEAIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   81 LPPFVAFAVRMNPGIWEFVKVHSANLSVEQMTPSDYLKNKEALVDDKWgayDDDSQLEVDFGALDLSTPHLTLPSSIGKG 160
Cdd:PLN00142  83 LPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSW---NDNFVLELDFEPFNASFPRPTLSSSIGNG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  161 AHLVSRFMSSKL---TDNKKPLLDYLLALSHRGDKLMINDILDTVDKLQTALLLAEVYVAGLHPDTNYSEFEQKFQEWGL 237
Cdd:PLN00142 160 VQFLNRHLSSKLfrdKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  238 EKGWGDTAETCKETLSSLSEVLQAPDPINMEKFFSTVPCVFTVVIFSIHGYFGQEKVLGMPDTGGQVVYILDQVRALEDE 317
Cdd:PLN00142 240 EKGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  318 LLQRIKQQGLNATPKILVLTRLIPEAKGTKCNVELEPIENTKHSNILRVPFKTEDGkVLPQWVSRFDIYPYLERYAQDSS 397
Cdd:PLN00142 320 MLLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKG-ILRKWISRFDVWPYLETFAEDAA 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  398 VKILEILEGKPDLVIGNYTDGNLVASLLTSKLGVTQGTIAHALEKTKYEDSDIKWRELDHKYHFSCQFTADMIAMNTSDF 477
Cdd:PLN00142 399 SEILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADF 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  478 IIASTYQEIAGSKEKPGQYESHYAFTMPGLCRYATGINVFDPKFNIAAPGADQSVYFPFTQKQKRLTDLHPQIEELLYSK 557
Cdd:PLN00142 479 IITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSP 558

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  558 EDNNEHIGHLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGLLDPSQSKDREEIEEINKMHSLINKY 637
Cdd:PLN00142 559 EQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDPSKSKDREEIAEIKKMHSLIEKY 638

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  638 QLVGQIRWIKGQTDRVRNGELYRCIADTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLN 717
Cdd:PLN00142 639 NLKGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYH 718

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  718 GKEASDKIADFFQKCKEDLIYWSKMSTAGLQRIYECYTWQIYATKVLNMASIYGFWRTLDKEERQAKQHYLHMFYNLQFR 797
Cdd:PLN00142 719 GDEAANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFR 798

                        810
                 ....*....|....*..
gi 75261422  798 KLAKNVPTLGEQPAQPT 814
Cdd:PLN00142 799 ELAKTVPLAVDDPQPPK 815
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
 23-804 0e+00

sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274149 [Multi-domain]  Cd Length: 784  Bit Score: 1355.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    23 RYQMKRCFQRYVSQGKRLMKRQQLLDELDKSVDDKADKDQLLQGFLGYVISSTQEAAVLPPFVAFAVRMNPGIWEFVKVH 102
Cdd:TIGR02470   1 RAELRQLLSRYVSQGKRYLLRHQLLDEFEQYCSDADKEKKLSESPLGKLIFSTQEAIVLPPWVALAVRPRIGVWEYVRVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   103 SANLSVEQMTPSDYLKNKEALVDdkwGAYDDDSQLEVDFGALDLSTPHLTLPSSIGKGAHLVSRFMSSKLTDNK---KPL 179
Cdd:TIGR02470  81 VEELSVEELTISEYLDFKEQLVN---GHANDPNVLELDFEPFNASFPRPSDSKSIGNGVQFLNRHLSSKLFQDPesmEPL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   180 LDYLLALSHRGDKLMINDILDTVDKLQTALLLAEVYVAGLHPDTNYSEFEQKFQEWGLEKGWGDTAETCKETLSSLSEVL 259
Cdd:TIGR02470 158 LNFLRVHNYNGIQLMINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   260 QAPDPINMEKFFSTVPCVFTVVIFSIHGYFGQEKVLGMPDTGGQVVYILDQVRALEDELLQRIKQQGLNATPKILVLTRL 339
Cdd:TIGR02470 238 EAPDPSVLEAFLGRIPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   340 IPEAKGTKCNVELEPIENTKHSNILRVPFKTEDGKVLPQWVSRFDIYPYLERYAQDSSVKILEILEGKPDLVIGNYTDGN 419
Cdd:TIGR02470 318 IPDAEGTTCNQRLEKVYGTEHAWILRVPFRTENGIILRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   420 LVASLLTSKLGVTQGTIAHALEKTKYEDSDIKWRELDHKYHFSCQFTADMIAMNTSDFIIASTYQEIAGSKEKPGQYESH 499
Cdd:TIGR02470 398 LVASLLARKLGVTQCTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESH 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   500 YAFTMPGLCRYATGINVFDPKFNIAAPGADQSVYFPFTQKQKRLTDLHPQIEELLYSKEDNNEHIGHLADRSKPIIFSMA 579
Cdd:TIGR02470 478 QAFTMPGLYRVVHGIDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMA 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   580 RLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGLLDPSQSKDREEIEEINKMHSLINKYQLVGQIRWIKGQTDRVRNGELY 659
Cdd:TIGR02470 558 RLDRVKNLTGLVECYGRSPKLRELVNLVVVAGKLDAKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELY 637

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   660 RCIADTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKIADFFQKCKEDLIYW 739
Cdd:TIGR02470 638 RYIADTKGIFVQPALYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYW 717

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75261422   740 SKMSTAGLQRIYECYTWQIYATKVLNMASIYGFWRTLDKEERQAKQHYLHMFYNLQFRKLAKNVP 804
Cdd:TIGR02470 718 QKISQGGLQRIYEKYTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVP 782
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
 15-555 0e+00

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


Pssm-ID: 395692  Cd Length: 540  Bit Score: 1001.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    15 MPEALRQSRYQMKRCFQRYVSQGKRLMKRQQLLDELDKSVDDKADKDQLLQGFLGYVISSTQEAAVLPPFVAFAVRMNPG 94
Cdd:pfam00862   1 VPDALSQSRNELKRLLSRYVAQGKRLMKRHELLDEFEKVIEDKKERSKLMEGLLGKILHSTQEAIVLPPWVAFAVRPRPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    95 IWEFVKVHSANLSVEQMTPSDYLKNKEALVDDKWgayDDDSQLEVDFGALDLSTPHLTLPSSIGKGAHLVSRFMSSKLTD 174
Cdd:pfam00862  81 VWEYVRVNADELSVEELTVSEYLKFKERLVDESW---NDENALELDFGPFNASFPRLTLPSSIGNGVQFLNRHLSSKLFR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   175 NK---KPLLDYLLALSHRGDKLMINDILDTVDKLQTALLLAEVYVAGLHPDTNYSEFEQKFQEWGLEKGWGDTAETCKET 251
Cdd:pfam00862 158 DSeslEPLLDFLRSHNYDGESLMINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKET 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   252 LSSLSEVLQAPDPINMEKFFSTVPCVFTVVIFSIHGYFGQEKVLGMPDTGGQVVYILDQVRALEDELLQRIKQQGLNATP 331
Cdd:pfam00862 238 MHLLSELLQAPDPSTLEKFLGRIPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKP 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   332 KILVLTRLIPEAKGTKCNVELEPIENTKHSNILRVPFKTEDGkVLPQWVSRFDIYPYLERYAQDSSVKILEILEGKPDLV 411
Cdd:pfam00862 318 QILVVTRLIPEARGTTCNQELEKISGTKHSHILRVPFRTENG-ILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLI 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   412 IGNYTDGNLVASLLTSKLGVTQGTIAHALEKTKYEDSDIKWRELDHKYHFSCQFTADMIAMNTSDFIIASTYQEIAGSKE 491
Cdd:pfam00862 397 IGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKD 476

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75261422   492 KPGQYESHYAFTMPGLCRYATGINVFDPKFNIAAPGADQSVYFPFTQKQKRLTDLHPQIEELLY 555
Cdd:pfam00862 477 RVGQYESHTAFTLPGLYRVVSGIDVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 280-765 8.45e-129

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: 391.60  E-value: 8.45e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 280 VVIFSIHGYFGQEkvLGMPDTGGQVVYILDQVRALedellqrikqqgLNATPKILVLTRLIPEAKGtkcnvelEPIENTK 359
Cdd:cd03800   2 IALISVHGSPLAQ--PGGADTGGQNVYVLELARAL------------AELGYQVDIFTRRISPADP-------EVVEIAP 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 360 HSNILRVPFKTEDGkvlpqwVSRFDIYPYLERYAQDSSVKILEILeGKPDLVIGNYTDGNLVASLLTSKLGVTQGTIAHA 439
Cdd:cd03800  61 GARVIRVPAGPPEY------LPKEELWPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 440 LEKTKYEDSDIKWReldhkYHFSCQFTADMIAMNTSDFIIASTYQEIAGSKekpgqyeSHYAftmpglcryatginVFDP 519
Cdd:cd03800 134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELI-------SLYG--------------ADPS 187

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 520 KFNIAAPGADQSVYFPFTQKQKRLTDLhpqieellyskednnehighLADRSKPIIFSMARLDKIKNITGLVEWYGQNKR 599
Cdd:cd03800 188 RINVVPPGVDLERFFPVDRAEARRARL--------------------LLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 600 LRDLVNLVIVGGLLDPSQSKDREEIEEINKMHSLINKYQLVGQIRwikgqtdRVRNGELYRCiadtKGAFVQPALYEAFG 679
Cdd:cd03800 248 LRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVS-------RDDLPELYRA----ADVFVVPSLYEPFG 316

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 680 LTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKIADFFQKCKedliYWSKMSTAGLQRIYECYTWQIY 759
Cdd:cd03800 317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPA----LWQRLSRAGLERARAHYTWESV 392


                ....*.
gi 75261422 760 ATKVLN 765
Cdd:cd03800 393 ADQLLT 398
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 280-764 2.06e-40

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 161.10  E-value: 2.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    280 VVIFSIHGYF-GQEKVLGM-PDTGGQVVYILDQVRALedellqrikqqglNATP---KILVLTRLI--PEAKGTKCnvel 352
Cdd:TIGR02468  172 IVLISLHGLVrGENMELGRdSDTGGQVKYVVELARAL-------------GSMPgvyRVDLLTRQVssPDVDWSYG---- 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    353 EPIE-----NTKHSN----------ILRVPFKTEDgkvlpQWVSRFDIYPYLERYAQDSSVKIL--------EILEGKP- 408
Cdd:TIGR02468  235 EPTEmltprSSENDGdemgessgayIIRIPFGPRD-----KYIPKEELWPYIPEFVDGALSHIVnmskvlgeQIGSGHPv 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    409 -DLVI-GNYTDGNLVASLLTSKLGVTQGTIAHALEKTKYEDSDIKWR----ELDHKYHFSCQFTADMIAMNTSDFIIAST 482
Cdd:TIGR02468  310 wPYVIhGHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQLLKQGRmskeEINSTYKIMRRIEAEELSLDASEIVITST 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    483 YQEIagsKEKPGQYESHYAFTMPGL-CRYATGINV---FDPKFNIAAPGADqsvyFPFTQKQKRLTDLHPQIEELLYSKE 558
Cdd:TIGR02468  390 RQEI---EEQWGLYDGFDVILERKLrARARRGVSCygrFMPRMAVIPPGME----FSHIVPHDGDMDGETEGNEEHPAKP 462

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    559 DN---NEHIGHLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGlldpsqskDREEIEEINKMHS--- 632
Cdd:TIGR02468  463 DPpiwSEIMRFFTNPRKPMILALARPDPKKNITTLVKAFGECRPLRELANLTLIMG--------NRDDIDEMSSGSSsvl 534

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422    633 -----LINKYQLVGQIRWIK--GQTDRvrnGELYRCIADTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIV 705
Cdd:TIGR02468  535 tsvlkLIDKYDLYGQVAYPKhhKQSDV---PDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHR 611

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75261422    706 DEVSGFHINPlngkEASDKIADFFQKCKEDLIYWSKMSTAGLQRIYEcYTW----QIYATKVL 764
Cdd:TIGR02468  612 VLDNGLLVDP----HDQQAIADALLKLVADKQLWAECRQNGLKNIHL-FSWpehcKTYLSRIA 669
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 572-728 5.27e-28

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 110.44  E-value: 5.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   572 KPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGglldpsqskdreEIEEINKMHSLINKYQLVGQIRWIkGQTD 651
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG------------DGEEEKRLKKLAEKLGLGDNVIFL-GFVS 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75261422   652 RVRNGELYRcIADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKIADF 728
Cdd:pfam00534  69 DEDLPELLK-IAD---VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKL 141
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 566-766 2.87e-21

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: 96.45  E-value: 2.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 566 HLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGlldpsQSKDREEIEEInkmhslinKYQLVGQIRW 645
Cdd:cd03801 186 LGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG-----DGPLRAELEEL--------ELGLGDRVRF 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 646 IkGQTDRVRNGELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPlngkEASDKI 725
Cdd:cd03801 253 L-GFVPDEELPALYAA-AD---VFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPP----DDVEAL 323

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75261422 726 ADFFQKCKEDLIYWSKMSTAGLQRIYECYTWQIYATKVLNM 766
Cdd:cd03801 324 ADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 541-765 1.73e-20

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 93.97  E-value: 1.73e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 541 KRLTDLHPQIEELlYSKEDNNEHIGHLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGlldpsQSKD 620
Cdd:cd03809 162 EKIVVIPLGVDPS-FFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGG-----KGWE 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 621 REEIeeinkmHSLINKYQLVGQIRWikgqTDRVRNGELYRCIADTKgAFVQPALYEAFGLTVIEAMNCGLPTFATNqgGP 700
Cdd:cd03809 236 DEEL------LDLVKKLGLGGRVRF----LGYVSDEDLPALYRGAR-AFVFPSLYEGFGLPVLEAMACGTPVIASN--IS 302

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75261422 701 AeiiVDEVSGFH---INPLNGKEasdkIADFFQKCKEDLIYWSKMSTAGLQRIYEcYTWQIYATKVLN 765
Cdd:cd03809 303 V---LPEVAGDAalyFDPLDPES----IADAILRLLEDPSLREELIRKGLERAKK-FSWEKTAEKTLE 362
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 641-766 5.38e-20

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 86.20  E-value: 5.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 641 GQIRWIKGQTDRVRngELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKE 720
Cdd:COG0438   2 GRLVPRKGLDLLLE--ALLAA-AD---VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEA 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 75261422 721 ASDKIADFFqkckEDLIYWSKMSTAGLQRIYECYTWQIYATKVLNM 766
Cdd:COG0438  76 LAEAILRLL----EDPELRRRLGEAARERAEERFSWEAIAERLLAL 117
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 570-755 6.05e-19

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 89.58  E-value: 6.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 570 RSKPIIFSM-ARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGlldpsqskdreeIEEINKMHSLINKYQLVGQIRWIkG 648
Cdd:cd03808 186 PSEKVVFLFvARLLKDKGIDELIEAAKILKKKGPNVRFLLVGD------------GELENPSEILIEKLGLEGRIEFL-G 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 649 QTDRVRngELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKIADF 728
Cdd:cd03808 253 FRSDVP--ELLAE-SD---VFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKL 326

                       170       180
                ....*....|....*....|....*..
gi 75261422 729 FQkcKEDLIYwsKMSTAGLQRIYECYT 755
Cdd:cd03808 327 IE--DPELRK--EMGEAARKRVEEKFD 349
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 571-750 1.34e-14

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 76.47  E-value: 1.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 571 SKPIIFSMARLDKIKNITGLVEWYG---QNKRLRDLVNLVIVGGLlDPSQSKDREEIEEINkmhSLINKYQLVG-QIRWI 646
Cdd:cd03805 210 NKKFFLSINRFERKKNIALAIEAFAklkQKLPEFENVRLVIAGGY-DPRVAENVEYLEELQ---RLAEELLNVEdQVLFL 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 647 KGQTDRVRNGELYRCIAdtkgafvqpALY----EAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPlNGKEAS 722
Cdd:cd03805 286 RSISDSQKEQLLSSALA---------LLYtpsnEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFA 355

                       170       180
                ....*....|....*....|....*...
gi 75261422 723 DKIADFFqkckEDLIYWSKMSTAGLQRI 750
Cdd:cd03805 356 EAMLKLA----NDPDLADRMGAAGRKRV 379
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 569-762 1.84e-14

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 75.82  E-value: 1.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 569 DRSKPIIFSMARLDKIKNITGLVEWYGQ-NKRLRDLVNLVIVGGLLdpsqskdREEIEEINKMHSLINKYQLVGQirwik 647
Cdd:cd03807 187 AEDRRVIGIVGRLHPVKDHSDLLRAAALlVETHPDLRLLLVGRGPE-------RPNLERLLLELGLEDRVHLLGE----- 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 648 gqtdRVRNGELYRcIADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEiIVDEVSGFHINPlngkEASDKIAD 727
Cdd:cd03807 255 ----RSDVPALLP-AMD---IFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAE-LVDDGTGFLVPA----GDPQALAD 321

                       170       180       190
                ....*....|....*....|....*....|....*
gi 75261422 728 FFQKCKEDLIYWSKMSTAGLQRIYECYTWQIYATK 762
Cdd:cd03807 322 AIRALLEDPEKRARLGRAARERIANEFSIDAMVRR 356
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 572-736 3.41e-14

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: 75.09  E-value: 3.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 572 KPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGglldpsQSKDREEIEEinkmhsLINKYQLVGQIRWiKGQTD 651
Cdd:cd03811 188 GPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG------DGPLREELEK------LAKELGLAERVIF-LGFQS 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 652 RVrngelYRCIADTKgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFhINPLNGKEASDKIADFFQK 731
Cdd:cd03811 255 NP-----YPYLKKAD-LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL-LVPDGDAAALAGILAALLQ 327


                ....*
gi 75261422 732 CKEDL 736
Cdd:cd03811 328 KKLDA 332
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 562-757 1.83e-13

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 72.66  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 562 EHIGHLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGglldpsqskDREEIEEINKmhsLINKYQLVG 641
Cdd:cd03820 171 PSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYG---------DGPEREELEK---LIDKLGLED 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 642 QIRwIKGQTDRVRngELYRciadTKGAFVQPALYEAFGLTVIEAMNCGLPTFATN-QGGPAEIIVDEVSGFHINPLNGKE 720
Cdd:cd03820 239 RVK-LLGPTKNIA--EEYA----NSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDA 311

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75261422 721 ASDKIADFFQkcKEDLIywSKMSTAGLQRIyECYTWQ 757
Cdd:cd03820 312 LAEALLRLME--DEELR--KKMGKNARKNA-ERFSIE 343
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 571-764 2.48e-13

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: 72.41  E-value: 2.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 571 SKPIIFSMARLDKIKNITGLVEWYGQ-NKRLRDLVnLVIVGGllDPSQSKDREEIEEINkmhslinkyqLVGQIRWikgq 649
Cdd:cd03798 199 DAFVILFVGRLIPRKGIDLLLEAFARlAKARPDVV-LLIVGD--GPLREALRALAEDLG----------LGDRVTF---- 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 650 TDRVRNGELYRCI--ADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKIAD 727
Cdd:cd03798 262 TGRLPHEQVPAYYraCD---VFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRR 338

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75261422 728 FFQKckedlIYWSKMSTAGLQRIYECYTWQIYATKVL 764
Cdd:cd03798 339 ALAE-----PYLRELGEAARARVAERFSWVKAADRIA 370
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 577-713 2.57e-13

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: 70.51  E-value: 2.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 577 SMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGlldpsqSKDREEIEEinkmhsLINKYQLVGQIRWIKGQTDRVRNG 656
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGG------GGEREEEEA------LAAALGLLERVVIIGGLVDDEVLE 182

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75261422 657 ELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHI 713
Cdd:cd01635 183 LLLAA-AD---VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
572-727 2.77e-13

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 67.54  E-value: 2.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   572 KPIIFSMARLDK-IKNITGLVE-WygqnKRLR---DLVNLVIVGglldpsqSKDREEIEEINKmhslinkyQLVGQIRWI 646
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEaV----PLLRkrdNDVRLVIVG-------DGPEEELEELAA--------GLEDRVIFT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   647 kGQTDRVRngELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIvDEVSGFHINPLNGKEASDKIA 726
Cdd:pfam13692  62 -GFVEDLA--ELLAA-AD---VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAIL 133


                  .
gi 75261422   727 D 727
Cdd:pfam13692 134 R 134
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 572-752 8.32e-13

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 70.77  E-value: 8.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 572 KPIIFSMARLDKIKNITGLVEWYgqnKRLRDLVN--LVIVGglldpsQSKDREEIEEINKMHSLINKYQLVGQIrwikgq 649
Cdd:cd03817 201 EPILLYVGRLAKEKNIDFLLRAF---AELKKEPNikLVIVG------DGPEREELKELARELGLADKVIFTGFV------ 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 650 tDRVRNGELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHInplngKEASDKIADFF 729
Cdd:cd03817 266 -PREELPEYYKA-AD---LFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLF-----EPNDETLAEKL 335

                       170       180
                ....*....|....*....|...
gi 75261422 730 QKCKEDLIYWSKMSTAGLQRIYE 752
Cdd:cd03817 336 LHLRENLELLRKLSKNAEISARE 358
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 550-752 3.27e-12

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. 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 bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 68.92  E-value: 3.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 550 IEELLYSKEDNNE-HIGHLADRSKPIIFSMARLDKIKNITGLVEWYgqnKRLRDLVN--LVIVGglldpsQSKDREEIEE 626
Cdd:cd04962 173 IDEDVFKRKPAGAlKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVF---ARVRRKIPakLLLVG------DGPERVPAEE 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 627 inkmhsLINKYQLVGQIRWIkGQTDRVrngELYRCIADTkgaFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVD 706
Cdd:cd04962 244 ------LARELGVEDRVLFL-GKQDDV---EELLSIADL---FLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKH 310

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75261422 707 EVSGFHINPLNgkeaSDKIADFFQKCKEDLIYWSKMSTAGLQRIYE 752
Cdd:cd04962 311 GETGFLSDVGD----VDAMAKSALSILEDDELYNRMGRAARKRAAE 352
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 574-729 3.43e-11

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general 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 in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 65.93  E-value: 3.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 574 IIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVG-GLLdpsqskdREEIEEINKMHSLINKYQLVGQIRWIKGqtdr 652
Cdd:cd04951 190 VILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGdGPL-------RNELERLICNLNLVDRVILLGQISNISE---- 258

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75261422 653 vrngelYRCIADTkgaFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDevSGFHINPLNGKEASDKIADFF 729
Cdd:cd04951 259 ------YYNAADL---FVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HNYVVPVSDPQLLAEKIKEIF 324
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 675-770 5.40e-11

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: 65.04  E-value: 5.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 675 YEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEasdkIADFFQKCKEDLIYWSKMSTAGLQRiyecy 754
Cdd:cd03823 271 PEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAED----LAAAMRRLLTDPALLERLRAGAEPP----- 341

                        90
                ....*....|....*.
gi 75261422 755 twQIYATKVLNMASIY 770
Cdd:cd03823 342 --RSTESQAEEYLKLY 355
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 641-727 8.90e-11

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 64.23  E-value: 8.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 641 GQIRWIkGQTDRVRNGELyrcIADTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLngKE 720
Cdd:cd03802 220 PRIEFI-GEVGHDEKQEL---LGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSV--EE 293


                ....*..
gi 75261422 721 ASDKIAD 727
Cdd:cd03802 294 MAEAIAN 300
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 668-756 3.85e-10

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 62.70  E-value: 3.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 668 AFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKIADFF---QKCKEdliywskMST 744
Cdd:cd03814 270 VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLedpELRRR-------MAA 342

                        90
                ....*....|..
gi 75261422 745 AGLQRIyECYTW 756
Cdd:cd03814 343 RARAEA-ERYSW 353
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 568-725 4.48e-10

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 61.99  E-value: 4.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 568 ADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVnLVIVGglldpsqskdreEIEEINKMHSLINKYQLVGQIRwIK 647
Cdd:cd03819 178 LPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFR-LLVAG------------DGPERDEIRRLVERLGLRDRVT-FT 243

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75261422 648 GQTDRVRNgeLYRcIADTkgaFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNGKEASDKI 725
Cdd:cd03819 244 GFREDVPA--ALA-ASDV---VVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAI 315
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 569-755 1.45e-09

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 60.80  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 569 DRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGGLL--DPSQSKDREEIEEINKMHSLINKYQLvgqirwi 646
Cdd:cd03792 194 DPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAvdDPEGSVVYEEVMEYAGDDHDIHVLRL------- 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 647 kGQTDRVRNgelyrCIADTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPlnGKEASDKIA 726
Cdd:cd03792 267 -PPSDQEIN-----ALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS--VEGAAVRIL 338

                       170       180
                ....*....|....*....|....*....
gi 75261422 727 DFFQkcKEDLiyWSKMSTAGLQRIYECYT 755
Cdd:cd03792 339 RLLT--DPEL--RRKMGLAAREHVRDNFL 363
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 642-711 4.77e-09

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: 59.27  E-value: 4.77e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75261422 642 QIRWIKGQ-------TDRVRNGELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGF 711
Cdd:cd03825 237 QIVILPFDiislgyiDDDEQLVDIYSA-AD---LFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGY 309
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 566-697 3.53e-07

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 53.17  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   566 HLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGG--LLDpsQSKDREEIEEInkMHSLinkyQLVGQI 643
Cdd:TIGR04047 187 RLGLRGGPYVLAVGGIEPRKNTIDLLEAFALLRARRPQAQLVIAGGatLFD--YDAYRREFRAR--AAEL----GVDPGP 258

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 75261422   644 RWIKGQTDRVRNGELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQ 697
Cdd:TIGR04047 259 VVITGPVPDADLPALYRC-AD---AFAFPSLKEGFGLVVLEALASGIPVVASDI 308
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 574-715 3.95e-07

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 53.19  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422   574 IIFSMARLDKIKNITGLVEWYGQ-NKRLRDLVN---LVIVGgllDPSQskdREEIEEINKMHSLinkyqlvGQIRWIKGQ 649
Cdd:TIGR03088 196 VVGTVGRLQAVKDQPTLVRAFALlVRQLPEGAErlrLVIVG---DGPA---RGACEQMVRAAGL-------AHLVWLPGE 262

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75261422   650 TDRVrnGELYRciadTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINP 715
Cdd:TIGR03088 263 RDDV--PALMQ----ALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPP 322
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 550-755 1.54e-06

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. 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 bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 51.12  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 550 IEELLYSKEDNNEHIGHLADRSKPIIFSMARLDKIKNITGLVEwygqNKRLRDLVnLVIVGglldpsqskdreEIEEINK 629
Cdd:cd03795 169 IDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIE----AAQYLNYP-IVIGG------------EGPLKPD 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 630 MHSLInKYQLVGQIRWIKGQTDRVRNgeLYRCIADtkgAFVQPALY--EAFGLTVIEAMNCGLPTFATNQGGPAEIIV-D 706
Cdd:cd03795 232 LEAQI-ELNLLDNVKFLGRVDDEEKV--IYLHLCD---VFVFPSVLrsEAFGIVLLEAMMCGKPVISTNIGTGVPYVNnN 305

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75261422 707 EVSGFHINPLNGK---EASDKIADFFQKCKEdliywskMSTAGLQRIYECYT 755
Cdd:cd03795 306 GETGLVVPPKDPDalaEAIDKLLSDEELRES-------YGENAKKRFEELFT 350
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 682-764 2.89e-06

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 50.42  E-value: 2.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 682 VIEAMNCGLPTFATNQGGPAEIIVDEVSGFHINPLNgkeaSDKIADFFQKCKEDLIYWSKMSTAGLQRIYECYTWQIYAT 761
Cdd:cd03794 313 LFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGD----PEALADAILELLDDPELRRAMGENGRELAEEKFSREKLAD 388


                ...
gi 75261422 762 KVL 764
Cdd:cd03794 389 RLL 391
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 563-707 4.50e-06

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 49.67  E-value: 4.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 563 HIGHLADRskPIIFSMARLDKIKNITGLVE-WYGQNKRLRDlVNLVIVGgllDPSQSKDREeieeinkMHsLINKYQLVG 641
Cdd:cd03821 197 KHNGLEDR--RIILFLGRIHPKKGLDLLIRaARKLAEQGRD-WHLVIAG---PDDGAYPAF-------LQ-LQSSLGLGD 262

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75261422 642 QIRWIKGQTDRVRnGELYRCiADtkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDE 707
Cdd:cd03821 263 RVTFTGPLYGEAK-WALYAS-AD---LFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG 323
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
569-713 4.74e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 49.79  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  569 DRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVGgllDPSQSKDREEIEEINKMHSLINkyQLVGQIRWIKG 648
Cdd:PRK15484 190 SPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVG---DPTASSKGEKAAYQKKVLEAAK--RIGDRCIMLGG 264

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75261422  649 QT-DRVRNgelYRCIADTkgAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGFHI 713
Cdd:PRK15484 265 QPpEKMHN---YYPLADL--VVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHL 325
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 530-725 4.84e-06

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general 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 in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 49.61  E-value: 4.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 530 QSVYFPFTQKQKRLTDLHPQIEELL--------YSKEDNNEHIGHlaDRSKPIIFSMARLDKIKNITGLVEWYGQNKRLR 601
Cdd:cd04949 112 NKYDAIIVSTEQQKQDLSERFNKYPpiftipvgYVDQLDTAESNH--ERKSNKIITISRLAPEKQLDHLIEAVAKAVKKV 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 602 DLVNLVIVGglldpsQSKDREEIEEinkmhsLINKYQLVGQIRwIKGQTDrvrngELYRCIADTKgAFVQPALYEAFGLT 681
Cdd:cd04949 190 PEITLDIYG------YGEEREKLKK------LIEELHLEDNVF-LKGYHS-----NLDQEYQDAY-LSLLTSQMEGFGLT 250

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75261422 682 VIEAMNCGLPTFATN-QGGPAEIIVDEVSGFHINPLNGKEASDKI 725
Cdd:cd04949 251 LMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEKNNIDALADKI 295
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 550-714 1.68e-05

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: 48.05  E-value: 1.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 550 IEELLYSKEDNNEHIGHLADRSKPIIFSMARLDKIKNITGLVEWYGQNKRLRDLVNLVIVG-GLLdpsqskdREEIEEIN 628
Cdd:cd03812 169 IEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGeGEL-------KEKIKEKV 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 629 KMHSLINKYQLVGQirwikgqtdRVRNGELYRciadTKGAFVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEV 708
Cdd:cd03812 242 KELGLEDKVIFLGF---------RNDVSEILS----AMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNV 308


                ....*.
gi 75261422 709 SGFHIN 714
Cdd:cd03812 309 EFLPLN 314
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 604-703 5.50e-05

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 46.46  E-value: 5.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 604 VNLVIVGGllDPSqskdREEIEEINKMHSLINKYQLVGQIRwikgqTDRVRN----GELyrciadtkgaFVQPALYEAFG 679
Cdd:cd03796 225 VRFIIGGD--GPK----RIELEEMREKYQLQDRVELLGAVP-----HEEVRDvlvqGHI----------FLNTSLTEAFC 283

                        90       100
                ....*....|....*....|....
gi 75261422 680 LTVIEAMNCGLPTFATNQGGPAEI 703
Cdd:cd03796 284 IAIVEAASCGLLVVSTRVGGIPEV 307
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
668-731 1.14e-04

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 45.47  E-value: 1.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75261422  668 AFVQPALYEAFGLTVIEAMNCGLPTFATN-QGGPAEIIVDEVSGFHINPLNGKEASDKIADFFQK 731
Cdd:PRK09922 260 ALLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVISG 324
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 676-755 4.26e-04

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. 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 bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 43.86  E-value: 4.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 676 EAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEV-----SGFHINPLNGKeasdKIADFFQKCKEDLIYWSKMSTAGLQRI 750
Cdd:cd03813 381 EGQPLVILEAMASGVPVVATDVGSCRELIYGADdalgqAGLVVPPADPE----ALAEALIKLLRDPELRQAFGEAGRKRV 456


                ....*
gi 75261422 751 YECYT 755
Cdd:cd03813 457 EKYYT 461
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 643-711 1.23e-03

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 41.89  E-value: 1.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75261422 643 IRWIKGQTDRVRNGELYRCiadtkGAFVQPAlYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSGF 711
Cdd:cd03804 248 VEFLGYQPDEVLKELLSKA-----RAFVFAA-EEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGI 310
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 669-774 1.29e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 42.01  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422  669 FVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDE---VSGFHINPLNGKEASDKIADFFQKCKEDliywSKMSTA 745
Cdd:PLN02871 335 FVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDqegKTGFLYTPGDVDDCVEKLETLLADPELR----ERMGAA 410

                         90       100       110
                 ....*....|....*....|....*....|.
gi 75261422  746 GLQRIyECYTWQIYATKVLNM--ASIYGFWR 774
Cdd:PLN02871 411 AREEV-EKWDWRAATRKLRNEqySAAIWFWR 440
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 669-710 1.99e-03

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 41.29  E-value: 1.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 75261422 669 FVQPALYEAFGLTVIEAMNCGLPTFATNQGGPAEIIVDEVSG 710
Cdd:cd04946 308 FVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNG 349
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 628-754 3.93e-03

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 40.51  E-value: 3.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75261422 628 NKMHSLINKYQLVGQIRWI--KGQTDRVRngelyrcIADTKGAFVQPALYEAFG------LTVIEAMNCGLPTFATNQGG 699
Cdd:cd03799 218 EQLQQLIQELNIGDCVKLLgwKPQEEIIE-------ILDEADIFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGG 290

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75261422 700 PAEIIVDEVSGFHInPLNGKEASDKIADFFQKCKEDliyWSKMSTAGLQRIYECY 754
Cdd:cd03799 291 IPELVEDGVSGFLV-PERDAEAIAEKLTYLIEHPAI---WPEMGKAGRARVEEEY 341
 
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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