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Conserved domains on  [gi|22329337|ref|NP_171984|]
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sucrose phosphate synthase 3F [Arabidopsis thaliana]

Protein Classification

sucrsPsyn_pln family protein( domain architecture ID 11494298)

sucrsPsyn_pln family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 1-1058 0e+00

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: 2023.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337      1 MAGNEWINGYLEAILDSQAQGIEETqqkpqASVNLREGDGQYFNPTKYFVEEVVTGVDETDLHRTWLKVVATRNSRERNS 80
Cdd:TIGR02468    1 MAGNDWINSYLEAILDVGPGLDDAK-----SSALLLLRERGRFSPTRYFVEEVITGFDETDLHRTWVKAVATRSPQERNT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337     81 RLENMCWRIWHLTRKKKQLEWEDSQRIANRRLEREQGRRDATEDLSEDLSEGEKGDGLGEI-VQPETP--RRQLQRNLSN 157
Cdd:TIGR02468   76 RLENMCWRIWNLARKKKQLEWEEAQRLAKRRLERERGRREATADMSEDLSEGEKGDVAGDIsVAGGEPstKGRLPRISSN 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    158 LEI--WSDDKKENRLYVVLISLHGLVRGENMELGSDSDTGGQVKYVVELARALARMPGVYRVDLFTRQICSSEVDWSYAE 235
Cdd:TIGR02468  156 LEMetWSDQQKEKKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDWSYGE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    236 PTEMLT-TAEDCDGDETGESSGAYIIRIPFGPRDKYLNKEILWPFVQEFVDGALAHILNMSKVLGEQIGKGKPVWPYVIH 314
Cdd:TIGR02468  236 PTEMLTpRSSENDGDEMGESSGAYIIRIPFGPRDKYIPKEELWPYIPEFVDGALSHIVNMSKVLGEQIGSGHPVWPYVIH 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    315 GHYADAGDSAALLSGALNVPMVLTGHSLGRNKLEQLLKQGRQSKEDINSTYKIKRRIEAEELSLDAAELVITSTRQEIDE 394
Cdd:TIGR02468  316 GHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQLLKQGRMSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEIEE 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    395 QWGLYDGFDVKLEKVLRARARRGVNCHGRFMPRMAVIPPGMDFTNVEVqedtpeGDGDLASLVGGTEGSSPKAVPTIWSE 474
Cdd:TIGR02468  396 QWGLYDGFDVILERKLRARARRGVSCYGRFMPRMAVIPPGMEFSHIVP------HDGDMDGETEGNEEHPAKPDPPIWSE 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    475 VMRFFTNPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRDDIDELSSGNASVLTTVLKLIDKYDLYGS 554
Cdd:TIGR02468  470 IMRFFTNPRKPMILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNRDDIDEMSSGSSSVLTSVLKLIDKYDLYGQ 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    555 VAYPKHHKQSDVPDIYRLAANTKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIAN 634
Cdd:TIGR02468  550 VAYPKHHKQSDVPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIAD 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    635 ALLKLVSEKNLWHECRINGWKNIHLFSWPEHCRTYLTRIAACRMRHPQWQTDADEVAAQDDEFSLNDSLKDVQDMSLRLS 714
Cdd:TIGR02468  630 ALLKLVADKQLWAECRQNGLKNIHLFSWPEHCKTYLSRIASCRPRHPQWQRDTDDGEEASEDESPGDSLRDIQDISLNLS 709

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    715 MDGDKPSLNGSLEPN----SADPVKQIMSRMRTPEiKSKPELQGKKQSDNLGSKYPVLRRRERLVVLAVDCYDNEGapde 790
Cdd:TIGR02468  710 VDGDKESNNGSSNVEgsgpPADRVAKIENAVRSWS-KSPKGSSAKAQQGSGAGKYPALRRRKRLFVIAVDCYDDKD---- 784

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    791 kaMVPMIQNIIKAVRSDpQMAKNSGFAISTSMPLDELTRFLKSAKIQVSEFDTLICSSGSEVYYPG---GEEGKLLPDPD 867
Cdd:TIGR02468  785 --LLQIIKNIFEAVRKE-RMEGSSGFILSTSMTISEIQSFLKSGGLNPTDFDALICNSGSELYYPSlngSEEGKLVADQD 861

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    868 YSSHIDYRWGMEGLKNTVWKLMNTTAvggEARNKGSPSLIQEDQASSNSHCVAYMIKDRSKVMRVDDLRQKLRLRGLRCH 947
Cdd:TIGR02468  862 YHSHIEYRWGGEGLRKTLVKWAASIN---EKKGENEEQIVEEDEESSTDHCYAFKVKDPSKVPPVKELRKLLRIQGLRCH 938

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    948 PMYCRNSTRMQIVPLLASRSQALRYLFVRWRLNVANMYVVVGDRGDTDYEELISGTHKTVIVKGLVTLGSDALLrSTD-- 1025
Cdd:TIGR02468  939 AVYCRNGTRLNVIPLLASRSQALRYLFVRWGIELANMAVFVGESGDTDYEGLLGGLHKTVILKGVVSRGSEQLH-ANRsy 1017

                         1050      1060      1070
                   ....*....|....*....|....*....|...
gi 22329337   1026 LRDDIVPSESPFIGFLKVDSPVKEITDIFKQLS 1058
Cdd:TIGR02468 1018 PLDDVVPLDSPNIVQATGGSSSDDISDALKKLS 1050
 
Name Accession Description Interval E-value
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 1-1058 0e+00

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: 2023.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337      1 MAGNEWINGYLEAILDSQAQGIEETqqkpqASVNLREGDGQYFNPTKYFVEEVVTGVDETDLHRTWLKVVATRNSRERNS 80
Cdd:TIGR02468    1 MAGNDWINSYLEAILDVGPGLDDAK-----SSALLLLRERGRFSPTRYFVEEVITGFDETDLHRTWVKAVATRSPQERNT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337     81 RLENMCWRIWHLTRKKKQLEWEDSQRIANRRLEREQGRRDATEDLSEDLSEGEKGDGLGEI-VQPETP--RRQLQRNLSN 157
Cdd:TIGR02468   76 RLENMCWRIWNLARKKKQLEWEEAQRLAKRRLERERGRREATADMSEDLSEGEKGDVAGDIsVAGGEPstKGRLPRISSN 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    158 LEI--WSDDKKENRLYVVLISLHGLVRGENMELGSDSDTGGQVKYVVELARALARMPGVYRVDLFTRQICSSEVDWSYAE 235
Cdd:TIGR02468  156 LEMetWSDQQKEKKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDWSYGE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    236 PTEMLT-TAEDCDGDETGESSGAYIIRIPFGPRDKYLNKEILWPFVQEFVDGALAHILNMSKVLGEQIGKGKPVWPYVIH 314
Cdd:TIGR02468  236 PTEMLTpRSSENDGDEMGESSGAYIIRIPFGPRDKYIPKEELWPYIPEFVDGALSHIVNMSKVLGEQIGSGHPVWPYVIH 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    315 GHYADAGDSAALLSGALNVPMVLTGHSLGRNKLEQLLKQGRQSKEDINSTYKIKRRIEAEELSLDAAELVITSTRQEIDE 394
Cdd:TIGR02468  316 GHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQLLKQGRMSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEIEE 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    395 QWGLYDGFDVKLEKVLRARARRGVNCHGRFMPRMAVIPPGMDFTNVEVqedtpeGDGDLASLVGGTEGSSPKAVPTIWSE 474
Cdd:TIGR02468  396 QWGLYDGFDVILERKLRARARRGVSCYGRFMPRMAVIPPGMEFSHIVP------HDGDMDGETEGNEEHPAKPDPPIWSE 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    475 VMRFFTNPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRDDIDELSSGNASVLTTVLKLIDKYDLYGS 554
Cdd:TIGR02468  470 IMRFFTNPRKPMILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNRDDIDEMSSGSSSVLTSVLKLIDKYDLYGQ 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    555 VAYPKHHKQSDVPDIYRLAANTKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIAN 634
Cdd:TIGR02468  550 VAYPKHHKQSDVPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIAD 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    635 ALLKLVSEKNLWHECRINGWKNIHLFSWPEHCRTYLTRIAACRMRHPQWQTDADEVAAQDDEFSLNDSLKDVQDMSLRLS 714
Cdd:TIGR02468  630 ALLKLVADKQLWAECRQNGLKNIHLFSWPEHCKTYLSRIASCRPRHPQWQRDTDDGEEASEDESPGDSLRDIQDISLNLS 709

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    715 MDGDKPSLNGSLEPN----SADPVKQIMSRMRTPEiKSKPELQGKKQSDNLGSKYPVLRRRERLVVLAVDCYDNEGapde 790
Cdd:TIGR02468  710 VDGDKESNNGSSNVEgsgpPADRVAKIENAVRSWS-KSPKGSSAKAQQGSGAGKYPALRRRKRLFVIAVDCYDDKD---- 784

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    791 kaMVPMIQNIIKAVRSDpQMAKNSGFAISTSMPLDELTRFLKSAKIQVSEFDTLICSSGSEVYYPG---GEEGKLLPDPD 867
Cdd:TIGR02468  785 --LLQIIKNIFEAVRKE-RMEGSSGFILSTSMTISEIQSFLKSGGLNPTDFDALICNSGSELYYPSlngSEEGKLVADQD 861

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    868 YSSHIDYRWGMEGLKNTVWKLMNTTAvggEARNKGSPSLIQEDQASSNSHCVAYMIKDRSKVMRVDDLRQKLRLRGLRCH 947
Cdd:TIGR02468  862 YHSHIEYRWGGEGLRKTLVKWAASIN---EKKGENEEQIVEEDEESSTDHCYAFKVKDPSKVPPVKELRKLLRIQGLRCH 938

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    948 PMYCRNSTRMQIVPLLASRSQALRYLFVRWRLNVANMYVVVGDRGDTDYEELISGTHKTVIVKGLVTLGSDALLrSTD-- 1025
Cdd:TIGR02468  939 AVYCRNGTRLNVIPLLASRSQALRYLFVRWGIELANMAVFVGESGDTDYEGLLGGLHKTVILKGVVSRGSEQLH-ANRsy 1017

                         1050      1060      1070
                   ....*....|....*....|....*....|...
gi 22329337   1026 LRDDIVPSESPFIGFLKVDSPVKEITDIFKQLS 1058
Cdd:TIGR02468 1018 PLDDVVPLDSPNIVQATGGSSSDDISDALKKLS 1050
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 171-671 4.52e-164

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: 489.06  E-value: 4.52e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  171 YVVLISLHGLVRGENMElgsdSDTGGQVKYVVELARALArmPGVYRVDLFTRQICSSEVDWSYAEPtemlttaedcdgde 250
Cdd:cd03800    1 RIALISVHGSPLAQPGG----ADTGGQNVYVLELARALA--ELGYQVDIFTRRISPADPEVVEIAP-------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  251 tgessGAYIIRIPFGPRDkYLNKEILWPFVQEFVDGALAHILNMskvlgeqigkgkPVWPYVIHGHYADAGDSAALLSGA 330
Cdd:cd03800   61 -----GARVIRVPAGPPE-YLPKEELWPYLEEFADGLLRFIARE------------GGRYDLIHSHYWDSGLVGALLARR 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  331 LNVPMVLTGHSLGRNKLEQLLKQGrqskedinsTYKIKRRIEAEELSLDAAELVITSTRQEIDEQWGLYDGFDvklekvl 410
Cdd:cd03800  123 LGVPLVHTFHSLGRVKYRHLGAQD---------TYHPSLRITAEEQILEAADRVIASTPQEADELISLYGADP------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  411 rararrgvnchgrfmPRMAVIPPGMDFTNVEVQEDTPEgdgdlaslvggtegsspkavptiwsEVMRFFTNPHKPMILAL 490
Cdd:cd03800  187 ---------------SRINVVPPGVDLERFFPVDRAEA-------------------------RRARLLLPPDKPVVLAL 226

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  491 SRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRDDIDELSSGNASVLTTVLKLIDKYDlygsvaYPKHHKQSDVPDIY 570
Cdd:cd03800  227 GRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVR------FPGRVSRDDLPELY 300

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  571 RLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEKNLWHECR 650
Cdd:cd03800  301 RAA----DVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLS 376

                        490       500
                 ....*....|....*....|..
gi 22329337  651 INGWKNI-HLFSWPEHCRTYLT 671
Cdd:cd03800  377 RAGLERArAHYTWESVADQLLT 398
PLN00142 PLN00142
sucrose synthase
 172-658 2.86e-32

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 135.49  E-value: 2.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   172 VVLISLHGLVRGENMeLGSdSDTGGQVKYVVELARA-----LARMPG-----VYRVDLFTRQI-------CSSEVdwsya 234
Cdd:PLN00142  282 VVIFSPHGYFGQANV-LGL-PDTGGQVVYILDQVRAlenemLLRIKQqgldiKPQILIVTRLIpdakgttCNQRL----- 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   235 eptemlttaEDCDGDETgessgAYIIRIPFGPRDKYLNKEI----LWPFVQEFVDGAlahilnMSKVLGEQIGKgkpvwP 310
Cdd:PLN00142  355 ---------EKVSGTEH-----SHILRVPFRTEKGILRKWIsrfdVWPYLETFAEDA------ASEILAELQGK-----P 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   311 YVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRNKLEQllkqgrqskEDI-----NSTYKIKRRIEAEELSLDAAELVI 385
Cdd:PLN00142  410 DLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPD---------SDIywkkfDDKYHFSCQFTADLIAMNHADFII 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   386 TSTRQEI---DEQWGLYDG---FDVK-LEKVLRararrGVNChgrFMPRMAVIPPGMD----FTNVEVQEDTPEGDGDLA 454
Cdd:PLN00142  481 TSTYQEIagsKDTVGQYEShtaFTLPgLYRVVH-----GIDV---FDPKFNIVSPGADmsiyFPYTEKQKRLTSLHPSIE 552

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   455 SLVGGTEGSSpkavptiwsEVMRFFTNPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRD-----DID 529
Cdd:PLN00142  553 ELLYSPEQND---------EHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDpskskDRE 623

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   530 ELSSgnasvLTTVLKLIDKYDLYGSVAYPKhhKQSDVP---DIYRLAANTKGVFINPALVEPFGLTLIEAAAHGLPMVAT 606
Cdd:PLN00142  624 EIAE-----IKKMHSLIEKYNLKGQFRWIA--AQTNRVrngELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFAT 696

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 22329337   607 KNGGPVDIHRALHNGLLVDP-HDQEA---IANALLKLVSEKNLWHECRINGWKNIH 658
Cdd:PLN00142  697 CQGGPAEIIVDGVSGFHIDPyHGDEAankIADFFEKCKEDPSYWNKISDAGLQRIY 752
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 484-653 1.33e-24

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: 101.20  E-value: 1.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    484 KPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLImGNRDDIDELSsgnasvlttvlKLIDKYDLYGSVAYPKHHKQ 563
Cdd:pfam00534    2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIA-GDGEEEKRLK-----------KLAEKLGLGDNVIFLGFVSD 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    564 SDVPDIYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEK 643
Cdd:pfam00534   70 EDLPELLKIA----DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDE 145

                          170
                   ....*....|
gi 22329337    644 NLWHECRING 653
Cdd:pfam00534  146 ELRERLGENA 155
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 569-670 2.42e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 90.43  E-value: 2.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  569 IYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEKNLWHE 648
Cdd:COG0438   17 LLAAA----DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92

                         90       100
                 ....*....|....*....|...
gi 22329337  649 CRINGWKNI-HLFSWPEHCRTYL 670
Cdd:COG0438   93 LGEAARERAeERFSWEAIAERLL 115
 
Name Accession Description Interval E-value
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 1-1058 0e+00

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: 2023.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337      1 MAGNEWINGYLEAILDSQAQGIEETqqkpqASVNLREGDGQYFNPTKYFVEEVVTGVDETDLHRTWLKVVATRNSRERNS 80
Cdd:TIGR02468    1 MAGNDWINSYLEAILDVGPGLDDAK-----SSALLLLRERGRFSPTRYFVEEVITGFDETDLHRTWVKAVATRSPQERNT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337     81 RLENMCWRIWHLTRKKKQLEWEDSQRIANRRLEREQGRRDATEDLSEDLSEGEKGDGLGEI-VQPETP--RRQLQRNLSN 157
Cdd:TIGR02468   76 RLENMCWRIWNLARKKKQLEWEEAQRLAKRRLERERGRREATADMSEDLSEGEKGDVAGDIsVAGGEPstKGRLPRISSN 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    158 LEI--WSDDKKENRLYVVLISLHGLVRGENMELGSDSDTGGQVKYVVELARALARMPGVYRVDLFTRQICSSEVDWSYAE 235
Cdd:TIGR02468  156 LEMetWSDQQKEKKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDWSYGE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    236 PTEMLT-TAEDCDGDETGESSGAYIIRIPFGPRDKYLNKEILWPFVQEFVDGALAHILNMSKVLGEQIGKGKPVWPYVIH 314
Cdd:TIGR02468  236 PTEMLTpRSSENDGDEMGESSGAYIIRIPFGPRDKYIPKEELWPYIPEFVDGALSHIVNMSKVLGEQIGSGHPVWPYVIH 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    315 GHYADAGDSAALLSGALNVPMVLTGHSLGRNKLEQLLKQGRQSKEDINSTYKIKRRIEAEELSLDAAELVITSTRQEIDE 394
Cdd:TIGR02468  316 GHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQLLKQGRMSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEIEE 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    395 QWGLYDGFDVKLEKVLRARARRGVNCHGRFMPRMAVIPPGMDFTNVEVqedtpeGDGDLASLVGGTEGSSPKAVPTIWSE 474
Cdd:TIGR02468  396 QWGLYDGFDVILERKLRARARRGVSCYGRFMPRMAVIPPGMEFSHIVP------HDGDMDGETEGNEEHPAKPDPPIWSE 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    475 VMRFFTNPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRDDIDELSSGNASVLTTVLKLIDKYDLYGS 554
Cdd:TIGR02468  470 IMRFFTNPRKPMILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNRDDIDEMSSGSSSVLTSVLKLIDKYDLYGQ 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    555 VAYPKHHKQSDVPDIYRLAANTKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIAN 634
Cdd:TIGR02468  550 VAYPKHHKQSDVPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIAD 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    635 ALLKLVSEKNLWHECRINGWKNIHLFSWPEHCRTYLTRIAACRMRHPQWQTDADEVAAQDDEFSLNDSLKDVQDMSLRLS 714
Cdd:TIGR02468  630 ALLKLVADKQLWAECRQNGLKNIHLFSWPEHCKTYLSRIASCRPRHPQWQRDTDDGEEASEDESPGDSLRDIQDISLNLS 709

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    715 MDGDKPSLNGSLEPN----SADPVKQIMSRMRTPEiKSKPELQGKKQSDNLGSKYPVLRRRERLVVLAVDCYDNEGapde 790
Cdd:TIGR02468  710 VDGDKESNNGSSNVEgsgpPADRVAKIENAVRSWS-KSPKGSSAKAQQGSGAGKYPALRRRKRLFVIAVDCYDDKD---- 784

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    791 kaMVPMIQNIIKAVRSDpQMAKNSGFAISTSMPLDELTRFLKSAKIQVSEFDTLICSSGSEVYYPG---GEEGKLLPDPD 867
Cdd:TIGR02468  785 --LLQIIKNIFEAVRKE-RMEGSSGFILSTSMTISEIQSFLKSGGLNPTDFDALICNSGSELYYPSlngSEEGKLVADQD 861

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    868 YSSHIDYRWGMEGLKNTVWKLMNTTAvggEARNKGSPSLIQEDQASSNSHCVAYMIKDRSKVMRVDDLRQKLRLRGLRCH 947
Cdd:TIGR02468  862 YHSHIEYRWGGEGLRKTLVKWAASIN---EKKGENEEQIVEEDEESSTDHCYAFKVKDPSKVPPVKELRKLLRIQGLRCH 938

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    948 PMYCRNSTRMQIVPLLASRSQALRYLFVRWRLNVANMYVVVGDRGDTDYEELISGTHKTVIVKGLVTLGSDALLrSTD-- 1025
Cdd:TIGR02468  939 AVYCRNGTRLNVIPLLASRSQALRYLFVRWGIELANMAVFVGESGDTDYEGLLGGLHKTVILKGVVSRGSEQLH-ANRsy 1017

                         1050      1060      1070
                   ....*....|....*....|....*....|...
gi 22329337   1026 LRDDIVPSESPFIGFLKVDSPVKEITDIFKQLS 1058
Cdd:TIGR02468 1018 PLDDVVPLDSPNIVQATGGSSSDDISDALKKLS 1050
sucr_P_syn_N TIGR02472
sucrose-phosphate synthase, putative, glycosyltransferase domain; This family consists of the ...
 170-670 1.00e-180

sucrose-phosphate synthase, putative, glycosyltransferase domain; This family consists of the N-terminal regions, or in some cases the entirety, of bacterial proteins closely related to plant sucrose-phosphate synthases (SPS). The C-terminal domain (TIGR02471), found with most members of this family, resembles both bona fide plant sucrose-phosphate phosphatases (SPP) and the SPP-like domain of plant SPS. At least two members of this family lack the SPP-like domain, which may have binding or regulatory rather than enzymatic activity by analogy to plant SPS. This enzyme produces sucrose 6-phosphate and UDP from UDP-glucose and D-fructose 6-phosphate, and may be encoded near the gene for fructokinase.


Pssm-ID: 131525 [Multi-domain]  Cd Length: 439  Bit Score: 533.54  E-value: 1.00e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    170 LYVVLISLHGLVRGENMELGSDSDTGGQVKYVVELARALARMPGVYRVDLFTRQICSSEVDWSYAEPTEMLttaedcdgd 249
Cdd:TIGR02472    1 LYLLLLSLHGLIRGHDLELGRDADTGGQTKYVLELARALARRSEVEQVDLVTRLIKDAKVSPDYAQPIERI--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    250 etgeSSGAYIIRIPFGPRdKYLNKEILWPFVQEFVDGALAHIlnmskvlgEQIGKgkpvWPYVIHGHYADAGDSAALLSG 329
Cdd:TIGR02472   72 ----APGARIVRLPFGPR-RYLRKELLWPYLDELADNLLQHL--------RQQGH----LPDLIHAHYADAGYVGARLSR 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    330 ALNVPMVLTGHSLGRNKLEQLLKQGRQSKEdINSTYKIKRRIEAEELSLDAAELVITSTRQEIDEQWGLYDGFDVKlekv 409
Cdd:TIGR02472  135 LLGVPLIFTGHSLGREKRRRLLAAGLKPQQ-IEKQYNISRRIEAEEETLAHASLVITSTHQEIEEQYALYDSYQPE---- 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    410 lrararrgvnchgrfmpRMAVIPPGMD---FTNVEVQEDTPEGDGDLAslvggtegsspkavptiwsevmRFFTNPHKPM 486
Cdd:TIGR02472  210 -----------------RMQVIPPGVDlsrFYPPQSSEETSEIDNLLA----------------------PFLKDPEKPP 250

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    487 ILALSRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRDDIDELSSGNASVLTTVLKLIDKYDLYGSVAYPKHHKQSDV 566
Cdd:TIGR02472  251 ILAISRPDRRKNIPSLVEAYGRSPKLQEMANLVLVLGCRDDIRKMESQQREVLQKVLLLIDRYDLYGKVAYPKHHRPDDV 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    567 PDIYRLAANTKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEKNLW 646
Cdd:TIGR02472  331 PELYRLAARSRGIFVNPALTEPFGLTLLEAAACGLPIVATDDGGPRDIIANCRNGLLVDVLDLEAIASALEDALSDSSQW 410

                          490       500
                   ....*....|....*....|....*
gi 22329337    647 HECRINGWKNIHL-FSWPEHCRTYL 670
Cdd:TIGR02472  411 QLWSRNGIEGVRRhYSWDAHVEKYL 435
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 171-671 4.52e-164

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: 489.06  E-value: 4.52e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  171 YVVLISLHGLVRGENMElgsdSDTGGQVKYVVELARALArmPGVYRVDLFTRQICSSEVDWSYAEPtemlttaedcdgde 250
Cdd:cd03800    1 RIALISVHGSPLAQPGG----ADTGGQNVYVLELARALA--ELGYQVDIFTRRISPADPEVVEIAP-------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  251 tgessGAYIIRIPFGPRDkYLNKEILWPFVQEFVDGALAHILNMskvlgeqigkgkPVWPYVIHGHYADAGDSAALLSGA 330
Cdd:cd03800   61 -----GARVIRVPAGPPE-YLPKEELWPYLEEFADGLLRFIARE------------GGRYDLIHSHYWDSGLVGALLARR 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  331 LNVPMVLTGHSLGRNKLEQLLKQGrqskedinsTYKIKRRIEAEELSLDAAELVITSTRQEIDEQWGLYDGFDvklekvl 410
Cdd:cd03800  123 LGVPLVHTFHSLGRVKYRHLGAQD---------TYHPSLRITAEEQILEAADRVIASTPQEADELISLYGADP------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  411 rararrgvnchgrfmPRMAVIPPGMDFTNVEVQEDTPEgdgdlaslvggtegsspkavptiwsEVMRFFTNPHKPMILAL 490
Cdd:cd03800  187 ---------------SRINVVPPGVDLERFFPVDRAEA-------------------------RRARLLLPPDKPVVLAL 226

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  491 SRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRDDIDELSSGNASVLTTVLKLIDKYDlygsvaYPKHHKQSDVPDIY 570
Cdd:cd03800  227 GRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVR------FPGRVSRDDLPELY 300

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  571 RLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEKNLWHECR 650
Cdd:cd03800  301 RAA----DVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLS 376

                        490       500
                 ....*....|....*....|..
gi 22329337  651 INGWKNI-HLFSWPEHCRTYLT 671
Cdd:cd03800  377 RAGLERArAHYTWESVADQLLT 398
HAD_SPS cd16419
sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; ...
 774-1012 1.35e-81

sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; Sucrose phosphate synthase (SPS; EC 2.4.1.14) also known as UDP-glucose-fructose-phosphate glucosyltransferase, catalyzes the transfer of a hexosyl group from UDP-glucose to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate, this is the rate limiting step of sucrose synthesis. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319856  Cd Length: 174  Bit Score: 262.56  E-value: 1.35e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  774 LVVLAVDCYDNEGAPDekamVPMIQNIIKAVRSDpQMAKNSGFAISTSMPLDELTRFLKSAKIQVSEFDTLICSSGSEVY 853
Cdd:cd16419    1 LFVIAVDCYDSSGLPA----LRVIKNILKAVRSD-SGGGSTGFVLSTSLTLSETVSLLKSAGISVTDFDALICNSGSELY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  854 YPGGEEGKLLPDPDYSshidyrwgmeglkntvwklmnttavggearnkgspsliqedqassnshcvaYMIKDrskvmrvd 933
Cdd:cd16419   76 YPSPSGDDDSDYELIP---------------------------------------------------DPVKE-------- 96

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329337  934 dLRQKLRLRGLRCHPMYCRNSTRMQIVPLLASRSQALRYLFVRWRLNVANMYVVVGDRGDTDYEELISGTHKTVIVKGL 1012
Cdd:cd16419   97 -LRKLLRMRGLRCHLVYCRNGTRLHVLPLLASRSQALRYLFVRWGIDLSNMVVFVGESGDTDYEELLGGLHKTVILKGV 174
PLN00142 PLN00142
sucrose synthase
 172-658 2.86e-32

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 135.49  E-value: 2.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   172 VVLISLHGLVRGENMeLGSdSDTGGQVKYVVELARA-----LARMPG-----VYRVDLFTRQI-------CSSEVdwsya 234
Cdd:PLN00142  282 VVIFSPHGYFGQANV-LGL-PDTGGQVVYILDQVRAlenemLLRIKQqgldiKPQILIVTRLIpdakgttCNQRL----- 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   235 eptemlttaEDCDGDETgessgAYIIRIPFGPRDKYLNKEI----LWPFVQEFVDGAlahilnMSKVLGEQIGKgkpvwP 310
Cdd:PLN00142  355 ---------EKVSGTEH-----SHILRVPFRTEKGILRKWIsrfdVWPYLETFAEDA------ASEILAELQGK-----P 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   311 YVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRNKLEQllkqgrqskEDI-----NSTYKIKRRIEAEELSLDAAELVI 385
Cdd:PLN00142  410 DLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPD---------SDIywkkfDDKYHFSCQFTADLIAMNHADFII 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   386 TSTRQEI---DEQWGLYDG---FDVK-LEKVLRararrGVNChgrFMPRMAVIPPGMD----FTNVEVQEDTPEGDGDLA 454
Cdd:PLN00142  481 TSTYQEIagsKDTVGQYEShtaFTLPgLYRVVH-----GIDV---FDPKFNIVSPGADmsiyFPYTEKQKRLTSLHPSIE 552

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   455 SLVGGTEGSSpkavptiwsEVMRFFTNPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRD-----DID 529
Cdd:PLN00142  553 ELLYSPEQND---------EHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDpskskDRE 623

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   530 ELSSgnasvLTTVLKLIDKYDLYGSVAYPKhhKQSDVP---DIYRLAANTKGVFINPALVEPFGLTLIEAAAHGLPMVAT 606
Cdd:PLN00142  624 EIAE-----IKKMHSLIEKYNLKGQFRWIA--AQTNRVrngELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFAT 696

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 22329337   607 KNGGPVDIHRALHNGLLVDP-HDQEA---IANALLKLVSEKNLWHECRINGWKNIH 658
Cdd:PLN00142  697 CQGGPAEIIVDGVSGFHIDPyHGDEAankIADFFEKCKEDPSYWNKISDAGLQRIY 752
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 193-670 3.75e-29

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: 120.34  E-value: 3.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  193 DTGGQVKYVVELARALARMPgvYRVDLFTRqicssevdwsyaeptemlttaedcdgdetgessgayiiRIPFGPRDKYLN 272
Cdd:cd03801   12 PVGGAERHVRELARALAARG--HDVTVLTP--------------------------------------ADPGEPPEELED 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  273 KEILWPFVQEFVDGALAHILNmskvlgeQIGKGKPVWPY-VIHGHYADAGDSAALLSGALNVPMVLTGHSLGRNKLEQLL 351
Cdd:cd03801   52 GVIVPLLPSLAALLRARRLLR-------ELRPLLRLRKFdVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLL 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  352 KQgrqskedinstykIKRRIEAEELSLDAAELVITSTRQEIDEqwglydgfdvklekvLRARarrgvncHGRFMPRMAVI 431
Cdd:cd03801  125 AA-------------ERRLLARAEALLRRADAVIAVSEALRDE---------------LRAL-------GGIPPEKIVVI 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  432 PPGMDFTNVEVQEDTPEGDGdlaslvggtegsspkavptiwsevmrfftnPHKPMILALSRPDPKKNITTLLKAFGECRP 511
Cdd:cd03801  170 PNGVDLERFSPPLRRKLGIP------------------------------PDRPVLLFVGRLSPRKGVDLLLEALAKLLR 219

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  512 LRELANLTLIMGNRDDIDELSSgnasvlttvlkliDKYDLYGSVAYPKHHKQSDVPDIYRLAAntkgVFINPALVEPFGL 591
Cdd:cd03801  220 RGPDVRLVIVGGDGPLRAELEE-------------LELGLGDRVRFLGFVPDEELPALYAAAD----VFVLPSRYEGFGL 282

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  592 TLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEKNLWHECRINGWKNIH-LFSWPEHCRTYL 670
Cdd:cd03801  283 VVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAeRFSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 484-653 1.33e-24

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: 101.20  E-value: 1.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    484 KPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLImGNRDDIDELSsgnasvlttvlKLIDKYDLYGSVAYPKHHKQ 563
Cdd:pfam00534    2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIA-GDGEEEKRLK-----------KLAEKLGLGDNVIFLGFVSD 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    564 SDVPDIYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEK 643
Cdd:pfam00534   70 EDLPELLKIA----DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDE 145

                          170
                   ....*....|
gi 22329337    644 NLWHECRING 653
Cdd:pfam00534  146 ELRERLGENA 155
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 462-670 2.77e-24

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: 105.91  E-value: 2.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  462 GSSPKAVPTIWSEVMRFFTNPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLtLIMGNRDDIDElssgnasvltT 541
Cdd:cd03809  170 GVDPSFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKL-VIVGGKGWEDE----------E 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  542 VLKLIDKYDLYGSVAYPKHHKQSDVPDIYRLAAntkgVFINPALVEPFGLTLIEAAAHGLPMVATkNGGPvdiHR--ALH 619
Cdd:cd03809  239 LLDLVKKLGLGGRVRFLGYVSDEDLPALYRGAR----AFVFPSLYEGFGLPVLEAMACGTPVIAS-NISV---LPevAGD 310

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 22329337  620 NGLLVDPHDQEAIANALLKLVSEKNLWHECRINGWKNIHLFSWPEHCRTYL 670
Cdd:cd03809  311 AALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTL 361
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 569-670 2.42e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 90.43  E-value: 2.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  569 IYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEKNLWHE 648
Cdd:COG0438   17 LLAAA----DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92

                         90       100
                 ....*....|....*....|...
gi 22329337  649 CRINGWKNI-HLFSWPEHCRTYL 670
Cdd:COG0438   93 LGEAARERAeERFSWEAIAERLL 115
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
484-641 1.31e-20

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 89.11  E-value: 1.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    484 KPMILALSR-PDPKKNITTLLKAFGECRPLRELANLTLI-MGNRDDIDELSSGnasvlttvlkLIDKYDLYGSVAypkhh 561
Cdd:pfam13692    1 RPVILFVGRlHPNVKGVDYLLEAVPLLRKRDNDVRLVIVgDGPEEELEELAAG----------LEDRVIFTGFVE----- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    562 kqsDVPDIYRLAAntkgVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRAlHNGLLVDPHDQEAIANALLKLVS 641
Cdd:pfam13692   66 ---DLAELLAAAD----VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDG-ENGLLVPPGDPEALAEAILRLLE 137
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 811-1009 4.75e-18

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 85.01  E-value: 4.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    811 AKNSGFAISTSMPLDELTRFLKsaKIQVSEFDTLICSSGSEVYYPGGeegkLLPDPDYSSHIDYRWgmeglkntvwklmN 890
Cdd:pfam05116   32 RPDVGLVFATGRSLDSAKELLK--EKPLPTPDYLITSVGTEIYYGPS----LVPDQSWQEHLDYHW-------------D 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    891 TTAVGGEARnkGSPSLIQEDQASSNSHCVAYMIKDRSKVMRVDDLRQKLRLRGLRCHPMYcRNSTRMQIVPLLASRSQAL 970
Cdd:pfam05116   93 RQAVVEALA--KFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLAELEQLLRKRGLDVKVIY-SSGRDLDILPLRASKGEAL 169

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 22329337    971 RYLFVRWRLNVANMyVVVGDRGDtDYEELISGTHkTVIV 1009
Cdd:pfam05116  170 RYLALKLGLPLENT-LVCGDSGN-DEELFIGGTR-GVVV 205
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 309-640 3.48e-17

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: 84.74  E-value: 3.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  309 WPYVIHGHYA-DAGDSAALLSGALNVPMVLTGHSlgrnkleqllkqgrqskEDIN--STYKIKRRIEAEELSLdaAELVI 385
Cdd:cd03798   95 PPDLIHAHFAyPAGFAAALLARLYGVPYVVTEHG-----------------SDINvfPPRSLLRKLLRWALRR--AARVI 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  386 TSTRQeideqwglydgfdvklekvLRARARRgvncHGRFMPRMAVIPPGMDFTNvevqeDTPEGDGdlaslvggtegssp 465
Cdd:cd03798  156 AVSKA-------------------LAEELVA----LGVPRDRVDVIPNGVDPAR-----FQPEDRG-------------- 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  466 kavptiwsevmrfFTNPHK-PMILALSRPDPKKNITTLLKAFGECRPLRELANLtLIMGNRDDIDELSSgnasvLTTVLK 544
Cdd:cd03798  194 -------------LGLPLDaFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVL-LIVGDGPLREALRA-----LAEDLG 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  545 LIDKYDLYGSVayPKHhkqsDVPDIYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLV 624
Cdd:cd03798  255 LGDRVTFTGRL--PHE----QVPAYYRAC----DVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLV 324

                        330
                 ....*....|....*.
gi 22329337  625 DPHDQEAIANALLKLV 640
Cdd:cd03798  325 PPGDADALAAALRRAL 340
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 473-645 9.82e-16

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: 80.09  E-value: 9.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  473 SEVMRFFTNPHKPMILALSRPDPKKNITTLLKAFGECRPlrELANLTL-IMGNRDDIDELssgnasvlttvLKLIDKYDL 551
Cdd:cd03811  177 AKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRK--KYPDVKLvILGDGPLREEL-----------EKLAKELGL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  552 YGSVAYPKHhkQSDVPDIYRLAAntkgVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDqEA 631
Cdd:cd03811  244 AERVIFLGF--QSNPYPYLKKAD----LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGD-AA 316

                        170
                 ....*....|....
gi 22329337  632 IANALLKLVSEKNL 645
Cdd:cd03811  317 ALAGILAALLQKKL 330
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 481-657 1.16e-15

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: 79.95  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  481 NPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLImGNRDDIDELSSgnasvlttvlkLIDKYDLYGSVAYPKH 560
Cdd:cd03808  186 PSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLV-GDGELENPSEI-----------LIEKLGLEGRIEFLGF 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  561 hkQSDVPDIYRlAANtkgVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLV 640
Cdd:cd03808  254 --RSDVPELLA-ESD---VFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLI 327

                        170
                 ....*....|....*..
gi 22329337  641 SEKNLWHECRINGWKNI 657
Cdd:cd03808  328 EDPELRKEMGEAARKRV 344
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 487-663 6.49e-15

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: 77.66  E-value: 6.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  487 ILALSRPDPKKNITTLLKAFGecRPLRELANLTL-IMGNRDDIDELssgnasvlttvLKLIDKYDLYGSVAYPkhHKQSD 565
Cdd:cd03820  184 ILAVGRLTYQKGFDLLIEAWA--LIAKKHPDWKLrIYGDGPEREEL-----------EKLIDKLGLEDRVKLL--GPTKN 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  566 VPDIYRLAAntkgVFINPALVEPFGLTLIEAAAHGLPMVATK-NGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEKN 644
Cdd:cd03820  249 IAEEYANSS----IFVLSSRYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEE 324

                        170
                 ....*....|....*....
gi 22329337  645 LWHECRINGWKNIHLFSWP 663
Cdd:cd03820  325 LRKKMGKNARKNAERFSIE 343
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 488-624 7.08e-15

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: 75.13  E-value: 7.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  488 LALSRPDPKKNITTLLKAFGECRPLRELANLTLIMGNRDDIDELssgnasvlttvlKLIDKYDLYGSVAYPKHHKQSDVP 567
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEE------------ALAAALGLLERVVIIGGLVDDEVL 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22329337  568 DIYRLAANtkgVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLV 624
Cdd:cd01635  182 ELLLAAAD---VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 482-645 7.00e-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: 71.54  E-value: 7.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  482 PHKPMILALSRPDPKKNITTLLKAFgecRPLRELANLTLIM-GN---RDDIDELSSGnasvlttvLKLIDKYDLYGSVAY 557
Cdd:cd03817  199 PDEPILLYVGRLAKEKNIDFLLRAF---AELKKEPNIKLVIvGDgpeREELKELARE--------LGLADKVIFTGFVPR 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  558 PKhhkqsdVPDIYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPhDQEAIANALL 637
Cdd:cd03817  268 EE------LPEYYKAA----DLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEP-NDETLAEKLL 336


                 ....*...
gi 22329337  638 KLVSEKNL 645
Cdd:cd03817  337 HLRENLEL 344
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 481-646 3.71e-12

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: 68.87  E-value: 3.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  481 NPHKpmILALSRPDPKKNITTLLKAFGECRplRELANLTLimgnrdDIdelsSGNASVLTTVLKLIDKYDLYGSVAYPKH 560
Cdd:cd04949  159 KSNK--IITISRLAPEKQLDHLIEAVAKAV--KKVPEITL------DI----YGYGEEREKLKKLIEELHLEDNVFLKGY 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  561 HKQSDvpDIYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATK-NGGPVDIHRALHNGLLVDPHDQEAIANALLKL 639
Cdd:cd04949  225 HSNLD--QEYQDA----YLSLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEKNNIDALADKIIEL 298


                 ....*..
gi 22329337  640 VSEKNLW 646
Cdd:cd04949  299 LNDPEKL 305
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 495-652 4.05e-12

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: 68.89  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  495 PKKNITTLLKAFGECRPLR-ELanltLIMGNRDDIDELSsgnasvlttvLKLIDKYDLYGSVaypkhhKQSDVPDIYRLA 573
Cdd:cd03823  202 EEKGIDLLVEAFKRLPREDiEL----VIAGHGPLSDERQ----------IEGGRRIAFLGRV------PTDDIKDFYEKI 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  574 AntkgVFINPAL-VEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSEKNLWHECRIN 652
Cdd:cd03823  262 D----VLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAG 337
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 482-667 5.36e-12

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: 68.86  E-value: 5.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  482 PHKPMILALSRPDPKKNITTLLKAFgecRPLRELANLTLIM-GNRDDIDELSSGNASVLTTVLKlidkydlyGSVAYPKH 560
Cdd:cd03814  196 PGRPLLLYVGRLAPEKNLEALLDAD---LPLAASPPVRLVVvGDGPARAELEARGPDVIFTGFL--------TGEELARA 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  561 HKQSDVpdiyrlaantkgvFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLV 640
Cdd:cd03814  265 YASADV-------------FVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALL 331

                        170       180
                 ....*....|....*....|....*..
gi 22329337  641 SEKNLWHECRINGWKNIHLFSWPEHCR 667
Cdd:cd03814  332 EDPELRRRMAARARAEAERYSWEAFLD 358
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 568-642 1.10e-11

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: 67.74  E-value: 1.10e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329337  568 DIYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLVSE 642
Cdd:cd03825  259 DIYSAA----DLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLAN 329
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 483-653 9.45e-11

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: 64.65  E-value: 9.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  483 HKPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLImGnrddiDELSSGNASVLTTVLKLIDKYDLYGsvaypkhhK 562
Cdd:cd03807  189 DRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLV-G-----RGPERPNLERLLLELGLEDRVHLLG--------E 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  563 QSDVPDIYRlAANtkgVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRAlHNGLLVDPHDQEAIANALLKLVSE 642
Cdd:cd03807  255 RSDVPALLP-AMD---IFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDD-GTGFLVPAGDPQALADAIRALLED 329

                        170
                 ....*....|.
gi 22329337  643 KNLWHECRING 653
Cdd:cd03807  330 PEKRARLGRAA 340
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 312-636 1.54e-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: 63.91  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  312 VIHGHYADAGDSAALLSGALNVPMVLTGHSLGRNkleqllkqgrqskedinsTYKIKRRIEAEELSLDAAELVITSTRQE 391
Cdd:cd03819   79 LIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLA------------------TYHPKDFALAVRARGDRVIAVSELVRDH 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  392 IDEQwglydgfdvklekvlrararrgvncHGRFMPRMAVIPPGMDFTNVEvqedtPEGDGDLASLVGGTEGsspkavpti 471
Cdd:cd03819  141 LIEA-------------------------LGVDPERIRVIPNGVDTDRFP-----PEAEAEERAQLGLPEG--------- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  472 wsevmrfftnphKPMILALSRPDPKKNITTLLKAFGEcrpLRELANLTLIMGnrddidelssGNASVLTTVLKLIDKYDL 551
Cdd:cd03819  182 ------------KPVVGYVGRLSPEKGWLLLVDAAAE---LKDEPDFRLLVA----------GDGPERDEIRRLVERLGL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  552 YGSVAYPKHHkqSDVPDIYRLAAntkgVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDI--HRAlhNGLLVDPHDQ 629
Cdd:cd03819  237 RDRVTFTGFR--EDVPAALAASD----VVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIvvHGR--TGLLVPPGDA 308


                 ....*..
gi 22329337  630 EAIANAL 636
Cdd:cd03819  309 EALADAI 315
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 842-1010 2.85e-10

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 61.98  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  842 DTLICSSGSEVYYpgGEEGKLLPDPDYSSHIDYRWGMEGLkntvwklmnttavggEARNKGSPSLIQEDQASSNSHCVAY 921
Cdd:cd02605   62 DFIISDVGTEIYY--GESGYLEPDTYWNEVLSEGWERFLF---------------EAIADLFKQLKPQSELEQNPHKISF 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  922 MIKDRSKVMRVDDLRQKLRLRGLRCHPMYCRNSTR-MQIVPLLASRSQALRYLFVRWRLNVANMyVVVGDRGDtDYEELI 1000
Cdd:cd02605  125 YLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGLAYdLDILPLGAGKGEALRYLQEKWNFPPERT-LVCGDSGN-DIALLS 202

                        170
                 ....*....|
gi 22329337 1001 SGTHkTVIVK 1010
Cdd:cd02605  203 TGTR-GVIVG 211
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
195-434 9.01e-09

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 55.48  E-value: 9.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    195 GGQVKYVVELARALARMpgVYRVDLFTRqicssevdwsyaeptemlttaEDCDGDETGESSGAYIIRIPFGPRDKYLnke 274
Cdd:pfam13579    1 GGIGVYVLELARALAAL--GHEVRVVTP---------------------GGPPGRPELVGDGVRVHRLPVPPRPSPL--- 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    275 ilwpfvqefvdGALAHILNMSKVLGEQigkgkpvWPYVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRNKLEQLLKQg 354
Cdd:pfam13579   55 -----------ADLAALRRLRRLLRAE-------RPDVVHAHSPTAGLAARLARRRRGVPLVVTVHGLALDYGSGWKRR- 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337    355 rqskedinstykikRRIEAEELSLDAAELVITSTRQEideqwglydgfdvklekvlRARARRgvncHGRFMPRMAVIPPG 434
Cdd:pfam13579  116 --------------LARALERRLLRRADAVVVVSEAE-------------------AELLRA----LGVPAARVVVVPNG 158
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 481-653 1.62e-08

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: 57.67  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  481 NPHKPMILALSRPDPKKNITTLLKAfgecrpLRELANLTLIMGN---RDDIDELSSGNASVLTTVLKLIDKYDLYgsvay 557
Cdd:cd03795  188 KKGKKIFLFIGRLVYYKGLDYLIEA------AQYLNYPIVIGGEgplKPDLEAQIELNLLDNVKFLGRVDDEEKV----- 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  558 pKHHKQSDV---PDIYRlaantkgvfinpalVEPFGLTLIEAAAHGLPMVATKNGG---PVDIHRalHNGLLVDPHDQEA 631
Cdd:cd03795  257 -IYLHLCDVfvfPSVLR--------------SEAFGIVLLEAMMCGKPVISTNIGTgvpYVNNNG--ETGLVVPPKDPDA 319

                        170       180
                 ....*....|....*....|..
gi 22329337  632 IANALLKLVSEKNLWHECRING 653
Cdd:cd03795  320 LAEAIDKLLSDEELRESYGENA 341
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 477-648 2.18e-08

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: 57.36  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  477 RFFTNPHKPMILALSRPDPKKNITTLLKAFGECRplRELANLTLIMGNRDDIDelssgNASVLTTVLKLIDKYDLYGsva 556
Cdd:cd04962  189 RLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVR--RKIPAKLLLVGDGPERV-----PAEELARELGVEDRVLFLG--- 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  557 ypkhhKQSDVPDIYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANAL 636
Cdd:cd04962  259 -----KQDDVEELLSIA----DLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSA 329

                        170
                 ....*....|..
gi 22329337  637 LKLVSEKNLWHE 648
Cdd:cd04962  330 LSILEDDELYNR 341
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 469-657 2.40e-08

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: 57.73  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  469 PTIWSEVMRFFTNPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLTLIMGnrDDIDELSSGNASVLTTVLKLIDK 548
Cdd:cd03813  278 IQRFAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGP--EDEDPEYAQECKRLVASLGLENK 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  549 YDLYGSVaypkhhkqsDVPDIYRlaanTKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVD-IHRALHN----GLL 623
Cdd:cd03813  356 VKFLGFQ---------NIKEYYP----KLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRElIYGADDAlgqaGLV 422

                        170       180       190
                 ....*....|....*....|....*....|....
gi 22329337  624 VDPHDQEAIANALLKLVSEKNLWHECRINGWKNI 657
Cdd:cd03813  423 VPPADPEALAEALIKLLRDPELRQAFGEAGRKRV 456
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 191-636 2.78e-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: 50.83  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  191 DSDTGGQVKYVVELARALARMpgvyRVDLFtrqICSSEvdwsyaeptemlttaedcDGDETGESS--GAYIIRIPFGPRD 268
Cdd:cd03821   10 SPKAGGPVKVVLRLAAALAAL----GHEVT---IVSTG------------------DGYESLVVEenGRYIPPQDGFASI 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  269 KYLNKEILWPFVQEFVDGAL-AHILNMSKVLgeqigkgkpvwpyvIHGHYADAGDSAALLSGALNVPMVLTGHSlgrnkl 347
Cdd:cd03821   65 PLLRQGAGRTDFSPGLPNWLrRNLREYDVVH--------------IHGVWTYTSLAACKLARRRGIPYVVSPHG------ 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  348 eQLLKQGRQSKEdinstykIKRRIEA---EELSLDAAELVITSTRQEIDEQWGLYDGfdvklekvlrararrgvnchgrf 424
Cdd:cd03821  125 -MLDPWALQQKH-------WKKRIALhliERRNLNNAALVHFTSEQEADELRRFGLE----------------------- 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  425 mPRMAVIPPGMDftnvevqedTPEGDGDLAslvggteGSSPKAVPtiwsevmrfftnPHKPMILALSRPDPKKNITTLLK 504
Cdd:cd03821  174 -PPIAVIPNGVD---------IPEFDPGLR-------DRRKHNGL------------EDRRIILFLGRIHPKKGLDLLIR 224

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  505 AFgeCRPLRELANLTLIMGNRDDIDELssgnasvltTVLKLIDKYDLYGSVAYPKHHKQSDVPDIYRLAAntkgVFINPA 584
Cdd:cd03821  225 AA--RKLAEQGRDWHLVIAGPDDGAYP---------AFLQLQSSLGLGDRVTFTGPLYGEAKWALYASAD----LFVLPS 289

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22329337  585 LVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRAlHNGLLVDPHDQ---EAIANAL 636
Cdd:cd03821  290 YSENFGNVVAEALACGLPVVITDKCGLSELVEA-GCGVVVDPNVSslaEALAEAL 343
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 571-639 4.96e-06

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: 49.98  E-value: 4.96e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329337  571 RLAANTKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPhdQEAIANALLKL 639
Cdd:cd03802  235 ELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS--VEEMAEAIANI 301
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 463-661 5.03e-06

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: 50.28  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  463 SSPKAVPTIWSEVMRFFTNphKPMILALSRPDPKKNITTLLKAFGECRP-LRELANLTLIMG---------NRDDIDELS 532
Cdd:cd03805  192 SFDSTSEDPDPGDLIAKSN--KKFFLSINRFERKKNIALAIEAFAKLKQkLPEFENVRLVIAggydprvaeNVEYLEELQ 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  533 SgnasvLTTVLKLIDKYDLYgsvaypkhhkQSDVPDIYR--LAANTKGVFINPAlVEPFGLTLIEAAAHGLPMVATKNGG 610
Cdd:cd03805  270 R-----LAEELLNVEDQVLF----------LRSISDSQKeqLLSSALALLYTPS-NEHFGIVPLEAMYAGKPVIACNSGG 333

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 22329337  611 PVDIHRALHNGLLVDPhDQEAIANALLKLVSEKNLWHECRINGWKNIH-LFS 661
Cdd:cd03805  334 PLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKeKFS 384
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 546-641 1.84e-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: 48.39  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  546 IDKYDLYGSV---AYPKHHKQSDVpdiyrlaANTKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGpvdIHRALHNGL 622
Cdd:cd03796  243 REKYQLQDRVellGAVPHEEVRDV-------LVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGG---IPEVLPPDM 312

                         90       100
                 ....*....|....*....|.
gi 22329337  623 LV--DPhDQEAIANALLKLVS 641
Cdd:cd03796  313 ILlaEP-DPEDIVRKLEEAIS 332
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 462-653 5.35e-05

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: 46.95  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  462 GSSPKAVPTIWSEVMRFFTNPHKPMILALSR-PDPKKNITTLLKAFGEcrpLRELANL-TLIMGNRDDIDELSSGNASvl 539
Cdd:cd03794  194 WADLEEFKPPPKDELRKKLGLDDKFVVVYAGnIGKAQGLETLLEAAER---LKRRPDIrFLFVGDGDEKERLKELAKA-- 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  540 ttvlKLIDKYDLYGSV---AYPKHHKQSDV---P----DIYRLAANTKgvfinpalvepfgltLIEAAAHGLPMVATkNG 609
Cdd:cd03794  269 ----RGLDNVTFLGRVpkeEVPELLSAADVglvPlkdnPANRGSSPSK---------------LFEYMAAGKPILAS-DD 328

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 22329337  610 GPVDIHRALHN-GLLVDPHDQEAIANALLKLVSEKNLWHECRING 653
Cdd:cd03794  329 GGSDLAVEINGcGLVVEPGDPEALADAILELLDDPELRRAMGENG 373
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 486-610 7.07e-05

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: 46.28  E-value: 7.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  486 MILALSRPDPKKNITTLLKAFGECrPLRELANLTLIMGN---RDDIDELssgnasvlttvlklIDKYDLYGSVAYPKHHk 562
Cdd:cd04951  190 VILNVGRLTEAKDYPNLLLAISEL-ILSKNDFKLLIAGDgplRNELERL--------------ICNLNLVDRVILLGQI- 253

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 22329337  563 qSDVPDIYRLAantkGVFINPALVEPFGLTLIEAAAHGLPMVATKNGG 610
Cdd:cd04951  254 -SNISEYYNAA----DLFVLSSEWEGFGLVVAEAMACERPVVATDAGG 296
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 481-674 7.59e-05

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: 46.16  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  481 NPHKPMILALSRPDPKKNITTLLKAFGECRPLRELANLtLIMGN--RDDIDelssgnasvlttvlklidkydlyGSVAYP 558
Cdd:cd03792  194 DPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQL-VICGHgaVDDPE-----------------------GSVVYE 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  559 K-HHKQSDVPDIYRLAANTKGVFINP-----------ALVEPFGLTLIEAAAHGLPMVATKNGG-PVDIhRALHNGLLVD 625
Cdd:cd03792  250 EvMEYAGDDHDIHVLRLPPSDQEINAlqraatvvlqlSTREGFGLTVSEALWKGKPVIATPAGGiPLQV-IDGETGFLVN 328

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 22329337  626 PHDQEAIanALLKLVSEKNLWHECRINGWKNI-HLFSWPEHCRTYLTRIA 674
Cdd:cd03792  329 SVEGAAV--RILRLLTDPELRRKMGLAAREHVrDNFLITGNLRAWLYLIA 376
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 567-648 2.39e-04

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: 44.75  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337  567 PDIYRLAANTKgVFINPALVEPFG------LTLIEAAAHGLPMVATKNGGPVDIHRALHNGLLVDPHDQEAIANALLKLV 640
Cdd:cd03799  242 EEIIEILDEAD-IFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLI 320


                 ....*...
gi 22329337  641 SEKNLWHE 648
Cdd:cd03799  321 EHPAIWPE 328
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
482-645 1.12e-03

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 42.47  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   482 PHKPMILALSRPDPKKNITTLLKAFGECRPLRElaNLTL-IMGnrdDIDELSSGNAS-----VLTTVLKLIDKYDLYGSV 555
Cdd:PRK15484  191 PDETVLLYAGRISPDKGILLLMQAFEKLATAHS--NLKLvVVG---DPTASSKGEKAayqkkVLEAAKRIGDRCIMLGGQ 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   556 AYPKHHKqsdvpdIYRLAantKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDIHRALHNGL-LVDPHDQEAIAN 634
Cdd:PRK15484  266 PPEKMHN------YYPLA---DLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIIS 336

                         170
                  ....*....|.
gi 22329337   635 ALLKLVSEKNL 645
Cdd:PRK15484  337 DINRTLADPEL 347
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 563-614 1.82e-03

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 41.89  E-value: 1.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22329337  563 QSDVPDIYrlaaNTKGVFINPALVEPFGLTLIEAAAHGLPMVATKNGGP-VDI 614
Cdd:cd03812  256 RNDVSEIL----SAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKeCDI 304
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 579-645 2.18e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 42.01  E-value: 2.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329337   579 VFINPALVEPFGLTLIEAAAHGLPMVATKNGGPVDI---HRALHNGLLVDPHDQEAIANALLKLVSEKNL 645
Cdd:PLN02871  334 VFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIippDQEGKTGFLYTPGDVDDCVEKLETLLADPEL 403
 
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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