|
Name |
Accession |
Description |
Interval |
E-value |
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
1-1048 |
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: 1582.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 1 MARNDWINSYLEAILDVGTSKKKRFESNSKIVQKLGDinskdhqekvfgdmngkdhqekvFSPIKYFVEEVVNSFDESDL 80
Cdd:TIGR02468 1 MAGNDWINSYLEAILDVGPGLDDAKSSALLLLRERGR-----------------------FSPTRYFVEEVITGFDETDL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 81 YKTWIKVIATRNTRERSNRLENICWRIWHLARKKKQIVWDDGVRLSKRRIEREQGRNDAEEDLLSELSEGEKDKNDGEKE 160
Cdd:TIGR02468 58 HRTWVKAVATRSPQERNTRLENMCWRIWNLARKKKQLEWEEAQRLAKRRLERERGRREATADMSEDLSEGEKGDVAGDIS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 161 KSEVVTTLEPprdHMPRIRS--EMQIWSEDDKSsRNLYIVLISMHGLVRGENMELGRDSDTGGQVKYVVELARALANTEG 238
Cdd:TIGR02468 138 VAGGEPSTKG---RLPRISSnlEMETWSDQQKE-KKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELARALGSMPG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 239 VHRVDLLTRQISSPEVDYSYGEPVEMLSCPPEGSD------SCGSYIIRIPCGSRDKYIPKESLWPHIPEFVDGALNHIV 312
Cdd:TIGR02468 214 VYRVDLLTRQVSSPDVDWSYGEPTEMLTPRSSENDgdemgeSSGAYIIRIPFGPRDKYIPKEELWPYIPEFVDGALSHIV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 313 SIARSLGEQVNGGKPIWPYVIHGHYADAGEVAAHLAGALNVPMVLTGHSLGRNKFEQLLQQGRITREDIDRTYKIMRRIE 392
Cdd:TIGR02468 294 NMSKVLGEQIGSGHPVWPYVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQLLKQGRMSKEEINSTYKIMRRIE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 393 AEEQSLDAAEMVVTSTRQEIDAQWGLYDGFDIKLERKLRVRRRRGVSCLGRYMPRMVVIPPGMDFSYVLTQDsqepdGDL 472
Cdd:TIGR02468 374 AEELSLDASEIVITSTRQEIEEQWGLYDGFDVILERKLRARARRGVSCYGRFMPRMAVIPPGMEFSHIVPHD-----GDM 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 473 KSLIGPDRNQIKKPVPPIWSEIMRFFSNPHKPTILALSRPDHKKNVTTLVKAFGECQPLRELANLVLILGNRDDIEEMPN 552
Cdd:TIGR02468 449 DGETEGNEEHPAKPDPPIWSEIMRFFTNPRKPMILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNRDDIDEMSS 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 553 SSSVVLMNVLKLIDQYDLYGQVAYPKHHKQSEVPDIYRLAAKTKGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVD 632
Cdd:TIGR02468 529 GSSSVLTSVLKLIDKYDLYGQVAYPKHHKQSDVPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVD 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 633 IVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNIHRFSWPEHCRNYLSHVEHCRNRHP----TSSLDIMK 708
Cdd:TIGR02468 609 IHRVLDNGLLVDPHDQQAIADALLKLVADKQLWAECRQNGLKNIHLFSWPEHCKTYLSRIASCRPRHPqwqrDTDDGEEA 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 709 VPEELTSDSLRDVDDISLRFSTEGDFTLNGE-------LDAGTRQKKLVDAISQMNSMKGCSAA----------IYSPGR 771
Cdd:TIGR02468 689 SEDESPGDSLRDIQDISLNLSVDGDKESNNGssnvegsGPPADRVAKIENAVRSWSKSPKGSSAkaqqgsgagkYPALRR 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 772 RQMLFVVAVDSYDDNGnikanLNEIIKNMIKAADLTSGKGKIGFVLASGSSLQEVVDITQKNLINLEDFDAIVCNSGSEI 851
Cdd:TIGR02468 769 RKRLFVIAVDCYDDKD-----LLQIIKNIFEAVRKERMEGSSGFILSTSMTISEIQSFLKSGGLNPTDFDALICNSGSEL 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 852 YYP------WRDMMVDADYETHVEYKWPGESIRSVILRLICT-----EPAAEDDITEYASSCSTRCYAISVKQGVKTRRV 920
Cdd:TIGR02468 844 YYPslngseEGKLVADQDYHSHIEYRWGGEGLRKTLVKWAASinekkGENEEQIVEEDEESSTDHCYAFKVKDPSKVPPV 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 921 DDLRQRLRMRGLRCNIVYTHAATRLNVIPLCASRIQALRYLSIRWGIDMSKTVFFLGEKGDTDYEDLLGGLHKTIILKGV 1000
Cdd:TIGR02468 924 KELRKLLRIQGLRCHAVYCRNGTRLNVIPLLASRSQALRYLFVRWGIELANMAVFVGESGDTDYEGLLGGLHKTVILKGV 1003
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*...
gi 79325049 1001 VGSDSEKLLrSEENFKREDAVPQESPNISYVKENGGSQEIMSTLEAYG 1048
Cdd:TIGR02468 1004 VSRGSEQLH-ANRSYPLDDVVPLDSPNIVQATGGSSSDDISDALKKLS 1050
|
|
| sucr_P_syn_N |
TIGR02472 |
sucrose-phosphate synthase, putative, glycosyltransferase domain; This family consists of the ... |
195-693 |
0e+00 |
|
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: 549.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 195 LYIVLISMHGLVRGENMELGRDSDTGGQVKYVVELARALANTEGVHRVDLLTRQISSPEVDYSYGEPVEMLScpPegsds 274
Cdd:TIGR02472 1 LYLLLLSLHGLIRGHDLELGRDADTGGQTKYVLELARALARRSEVEQVDLVTRLIKDAKVSPDYAQPIERIA--P----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 275 cGSYIIRIPCGSRdKYIPKESLWPHIPEFVDGALNHIvsiarslgeQVNGGKPIWpyvIHGHYADAGEVAAHLAGALNVP 354
Cdd:TIGR02472 74 -GARIVRLPFGPR-RYLRKELLWPYLDELADNLLQHL---------RQQGHLPDL---IHAHYADAGYVGARLSRLLGVP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 355 MVLTGHSLGRNKFEQLLQQGRiTREDIDRTYKIMRRIEAEEQSLDAAEMVVTSTRQEIDAQWGLYDGFDIKlerklrvrr 434
Cdd:TIGR02472 140 LIFTGHSLGREKRRRLLAAGL-KPQQIEKQYNISRRIEAEEETLAHASLVITSTHQEIEEQYALYDSYQPE--------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 435 rrgvsclgrympRMVVIPPGMDFSYVLTQDSQEPDgdlksligpdrnqikkpvPPIWSEIMRFFSNPHKPTILALSRPDH 514
Cdd:TIGR02472 210 ------------RMQVIPPGVDLSRFYPPQSSEET------------------SEIDNLLAPFLKDPEKPPILAISRPDR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 515 KKNVTTLVKAFGECQPLRELANLVLILGNRDDIEEMPNSSSVVLMNVLKLIDQYDLYGQVAYPKHHKQSEVPDIYRLAAK 594
Cdd:TIGR02472 260 RKNIPSLVEAYGRSPKLQEMANLVLVLGCRDDIRKMESQQREVLQKVLLLIDRYDLYGKVAYPKHHRPDDVPELYRLAAR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 595 TKGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLK 674
Cdd:TIGR02472 340 SRGIFVNPALTEPFGLTLLEAAACGLPIVATDDGGPRDIIANCRNGLLVDVLDLEAIASALEDALSDSSQWQLWSRNGIE 419
|
490 500
....*....|....*....|
gi 79325049 675 NIHR-FSWPEHCRNYLSHVE 693
Cdd:TIGR02472 420 GVRRhYSWDAHVEKYLRILQ 439
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
196-690 |
1.50e-158 |
|
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: 474.42 E-value: 1.50e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 196 YIVLISMHGLVRGENMElgrdSDTGGQVKYVVELARALANTegVHRVDLLTRQISSPEVDYSYGEPvemlscppegsdsc 275
Cdd:cd03800 1 RIALISVHGSPLAQPGG----ADTGGQNVYVLELARALAEL--GYQVDIFTRRISPADPEVVEIAP-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 276 GSYIIRIPCGSRDkYIPKESLWPHIPEFVDGALNHIvsiARSLGeqvnggkpiWPYVIHGHYADAGEVAAHLAGALNVPM 355
Cdd:cd03800 61 GARVIRVPAGPPE-YLPKEELWPYLEEFADGLLRFI---AREGG---------RYDLIHSHYWDSGLVGALLARRLGVPL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 356 VLTGHSLGRNKFEQLLQQGritredidrTYKIMRRIEAEEQSLDAAEMVVTSTRQEIDAQWGLYDGFDiklerklrvrrr 435
Cdd:cd03800 128 VHTFHSLGRVKYRHLGAQD---------TYHPSLRITAEEQILEAADRVIASTPQEADELISLYGADP------------ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 436 rgvsclgrymPRMVVIPPGMDFsyvltqdsqepdgdlksligpdrnQIKKPVPPIWSEIMRFFSNPHKPTILALSRPDHK 515
Cdd:cd03800 187 ----------SRINVVPPGVDL------------------------ERFFPVDRAEARRARLLLPPDKPVVLALGRLDPR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 516 KNVTTLVKAFGECQPLRELANLVLILGNRDDIEEMPNSSSVVLMNVLKLIDQYDlygqvaYPKHHKQSEVPDIYRLAakt 595
Cdd:cd03800 233 KGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVR------FPGRVSRDDLPELYRAA--- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 596 kGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKN 675
Cdd:cd03800 304 -DVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLER 382
|
490
....*....|....*.
gi 79325049 676 IHR-FSWPEHCRNYLS 690
Cdd:cd03800 383 ARAhYTWESVADQLLT 398
|
|
| HAD_SPS |
cd16419 |
sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; ... |
775-1000 |
4.13e-86 |
|
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: 274.89 E-value: 4.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 775 LFVVAVDSYDDNGNIKanlNEIIKNMIKAADLTSGKGKIGFVLASGSSLQEVVDITQKNLINLEDFDAIVCNSGSEIYYP 854
Cdd:cd16419 1 LFVIAVDCYDSSGLPA---LRVIKNILKAVRSDSGGGSTGFVLSTSLTLSETVSLLKSAGISVTDFDALICNSGSELYYP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 855 WRDMMVDADYETHVEykwpgesirsvilrlictepaaedditeyasscstrcyaisvkqgvktrRVDDLRQRLRMRGLRC 934
Cdd:cd16419 78 SPSGDDDSDYELIPD-------------------------------------------------PVKELRKLLRMRGLRC 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79325049 935 NIVYTHAATRLNVIPLCASRIQALRYLSIRWGIDMSKTVFFLGEKGDTDYEDLLGGLHKTIILKGV 1000
Cdd:cd16419 109 HLVYCRNGTRLHVLPLLASRSQALRYLFVRWGIDLSNMVVFVGESGDTDYEELLGGLHKTVILKGV 174
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
197-681 |
1.62e-36 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 148.97 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 197 IVLISMHGLVRGENMeLGRdSDTGGQVKYVVELARALAN-------TEGVH---RVDLLTRQIssPE-VDYSYGEPVEml 265
Cdd:PLN00142 282 VVIFSPHGYFGQANV-LGL-PDTGGQVVYILDQVRALENemllrikQQGLDikpQILIVTRLI--PDaKGTTCNQRLE-- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 266 scPPEGSDScgSYIIRIPCGSRD----KYIPKESLWPHIPEFVDGALNHIVSIArslgeqvnGGKPiwpYVIHGHYADAG 341
Cdd:PLN00142 356 --KVSGTEH--SHILRVPFRTEKgilrKWISRFDVWPYLETFAEDAASEILAEL--------QGKP---DLIIGNYSDGN 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 342 EVAAHLAGALNVPMVLTGHSLGRNKFEQllqqGRITREDIDRTYKIMRRIEAEEQSLDAAEMVVTSTRQEIDA------Q 415
Cdd:PLN00142 421 LVASLLAHKLGVTQCTIAHALEKTKYPD----SDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEIAGskdtvgQ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 416 W---------GLY------DGFDiklerklrvrrrrgvsclgrymPRMVVIPPGMDFS-YVLTQDSQEPDGDLKSLI--- 476
Cdd:PLN00142 497 YeshtaftlpGLYrvvhgiDVFD----------------------PKFNIVSPGADMSiYFPYTEKQKRLTSLHPSIeel 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 477 --GPDRNQikkpvppiwsEIMRFFSNPHKPTILALSRPDHKKNVTTLVKAFGECQPLRELANLVLILGNRD-----DIEE 549
Cdd:PLN00142 555 lySPEQND----------EHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDpskskDREE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 550 MpnsSSVVLMNvlKLIDQYDLYGQV----AYPKHHKQSEvpdIYRLAAKTKGVFINPALVEPFGLTLIEAAAYGLPIVAT 625
Cdd:PLN00142 625 I---AEIKKMH--SLIEKYNLKGQFrwiaAQTNRVRNGE---LYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFAT 696
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79325049 626 RNGGPVDIVKALNNGLLVDP-HDQQA---ISDALLKLVANKHLWAECRKNGLKNIH-RFSW 681
Cdd:PLN00142 697 CQGGPAEIIVDGVSGFHIDPyHGDEAankIADFFEKCKEDPSYWNKISDAGLQRIYeCYTW 757
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
218-693 |
1.86e-33 |
|
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: 133.05 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 218 DTGGQVKYVVELARALAnTEGvHRVDLLTrqisspevdysygepvemlscppegsdscgsyiiriPCGSRDKYIPKESLW 297
Cdd:cd03801 12 PVGGAERHVRELARALA-ARG-HDVTVLT------------------------------------PADPGEPPEELEDGV 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 298 PHIPEFVDGALNHIVSIARSLGEQVNGGKPIwpyVIHGHYADAGEVAAHLAGALNVPMVLTGHSLGRNKFEQLLqqgrit 377
Cdd:cd03801 54 IVPLLPSLAALLRARRLLRELRPLLRLRKFD---VVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLL------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 378 rediDRTYKIMRRIEAEEQSLDAaeMVVTS--TRQEIdaqwglydgfdiklerklrvrrrrgVSCLGRYMPRMVVIPPGM 455
Cdd:cd03801 125 ----AAERRLLARAEALLRRADA--VIAVSeaLRDEL-------------------------RALGGIPPEKIVVIPNGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 456 DFSYVltqdsqEPDGDLKSLIGPDRnqikkpvppiwseimrffsnphkPTILALSRPDHKKNVTTLVKAFGECQPLRELA 535
Cdd:cd03801 174 DLERF------SPPLRRKLGIPPDR-----------------------PVLLFVGRLSPRKGVDLLLEALAKLLRRGPDV 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 536 NLVLIlGNRDDIEEmpnsssvvlmnVLKLIDqYDLYGQVAYPKHHKQSEVPDIYRLAAktkgVFINPALVEPFGLTLIEA 615
Cdd:cd03801 225 RLVIV-GGDGPLRA-----------ELEELE-LGLGDRVRFLGFVPDEELPALYAAAD----VFVLPSRYEGFGLVVLEA 287
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325049 616 AAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNIH-RFSWPEHCRNYLSHVE 693
Cdd:cd03801 288 MAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAeRFSWERVAERLLDLYR 366
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
503-674 |
9.96e-27 |
|
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: 106.97 E-value: 9.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 503 KPTILALSRPDHKKNVTTLVKAFGECQPLRELANLVlILGNRDDIEEMpnsssvvlmnvLKLIDQYDLYGQVAYPKHHKQ 582
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLV-IAGDGEEEKRL-----------KKLAEKLGLGDNVIFLGFVSD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 583 SEVPDIYRLAaktkGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANK 662
Cdd:pfam00534 70 EDLPELLKIA----DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDE 145
|
170
....*....|..
gi 79325049 663 HLWAECRKNGLK 674
Cdd:pfam00534 146 ELRERLGENARK 157
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
588-697 |
2.77e-25 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 101.61 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 588 IYRLAaktkGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAE 667
Cdd:COG0438 17 LLAAA----DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92
|
90 100 110
....*....|....*....|....*....|.
gi 79325049 668 CRKNGLKNI-HRFSWPEHCRNYLSHVEHCRN 697
Cdd:COG0438 93 LGEAARERAeERFSWEAIAERLLALYEELLA 123
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
471-689 |
2.25e-22 |
|
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: 100.13 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 471 DLKSLIGPDRNQIK--------KPVPPIWSEIMRFFSNPHKPTILALSRPDHKKNVTTLVKAFGECQPLRELANLVLI-- 540
Cdd:cd03809 152 DIIKFYGVPPEKIVviplgvdpSFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVgg 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 541 LGNRDDieempnsssvvlmNVLKLIDQYDLYGQVAYPKHHKQSEVPDIYRLAAktkgVFINPALVEPFGLTLIEAAAYGL 620
Cdd:cd03809 232 KGWEDE-------------ELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGAR----AFVFPSLYEGFGLPVLEAMACGT 294
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325049 621 PIVATrNGGPVDIVkALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNIHRFSWPEHCRNYL 689
Cdd:cd03809 295 PVIAS-NISVLPEV-AGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTL 361
|
|
| S6PP |
pfam05116 |
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ... |
813-1021 |
4.54e-22 |
|
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: 96.57 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 813 IGFVLASGSSLQEVVD-ITQKNLINLedfDAIVCNSGSEIYYpWRDMMVDADYETHVEYKWPGESIRSVILRLICTEPAA 891
Cdd:pfam05116 35 VGLVFATGRSLDSAKElLKEKPLPTP---DYLITSVGTEIYY-GPSLVPDQSWQEHLDYHWDRQAVVEALAKFPGLTLQP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 892 EDDITEYASScstrcyaISVKQGVKTRRVDDLRQRLRMRGLRCNIVYTHAATrLNVIPLCASRIQALRYLSIRWGIDMSK 971
Cdd:pfam05116 111 EEEQRPHKVS-------YFLDPEAAAAVLAELEQLLRKRGLDVKVIYSSGRD-LDILPLRASKGEALRYLALKLGLPLEN 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79325049 972 TVFflgeKGDT--DYEDLLGGLHktiilkGVV--GSDSEKLLRSEENFKREDAV 1021
Cdd:pfam05116 183 TLV----CGDSgnDEELFIGGTR------GVVvgNAQPELLQWYLENARDNPRI 226
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
503-661 |
2.71e-21 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 91.03 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 503 KPTILALSRPDHK-KNVTTLVKAFGECQPLRELANLVLI-LGNRDDIEEMpnsssvvlmnVLKLIDQYDLYGQVAypkhh 580
Cdd:pfam13692 1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVgDGPEEELEEL----------AAGLEDRVIFTGFVE----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 581 kqsEVPDIYRLAAktkgVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKAlNNGLLVDPHDQQAISDALLKLVA 660
Cdd:pfam13692 66 ---DLAELLAAAD----VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDG-ENGLLVPPGDPEALAEAILRLLE 137
|
.
gi 79325049 661 N 661
Cdd:pfam13692 138 D 138
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
281-681 |
2.06e-19 |
|
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: 91.67 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 281 RIPCGSRDKYIPKESLWPHIPEFVDGALnhIVSIARSLGEQVNGGKPIWPYVIHGHYA-DAGEVAAHLAGALNVPMVLTG 359
Cdd:cd03798 49 LLRKLLGEAVPPRDGRRLLPLKPRLRLL--APLRAPSLAKLLKRRRRGPPDLIHAHFAyPAGFAAALLARLYGVPYVVTE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 360 HSLGRNKFeqllqqgritredidRTYKIMRRIEaeEQSLDAAEMVVTSTRQEIDaqwglydgfdiklerklrvrrrrGVS 439
Cdd:cd03798 127 HGSDINVF---------------PPRSLLRKLL--RWALRRAARVIAVSKALAE-----------------------ELV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 440 CLGRYMPRMVVIPPGMDFSYvltqDSQEPDGdlksligpdrnqikkPVPPiwseimrffsnPHKPTILALSRPDHKKNVT 519
Cdd:cd03798 167 ALGVPRDRVDVIPNGVDPAR----FQPEDRG---------------LGLP-----------LDAFVILFVGRLIPRKGID 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 520 TLVKAFGECQPLRELANLvLILGnrDDIEEMPNSSsvvLMNVLKLIDQYDLYGQVayPKHhkqsEVPDIYRLAaktkGVF 599
Cdd:cd03798 217 LLLEAFARLAKARPDVVL-LIVG--DGPLREALRA---LAEDLGLGDRVTFTGRL--PHE----QVPAYYRAC----DVF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 600 INPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVAN---KHLWAECRKNGLKni 676
Cdd:cd03798 281 VLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEpylRELGEAARARVAE-- 358
|
....*
gi 79325049 677 hRFSW 681
Cdd:cd03798 359 -RFSW 362
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
476-676 |
1.44e-17 |
|
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: 85.72 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 476 IGPDRNQIKKPVPPiwseimrffsnPHKPTILALSRPDHKKNVTTLVKAFgecqplRELANL-----VLILGNRDdieem 550
Cdd:cd03808 173 VDLDRFQYSPESLP-----------SEKVVFLFVARLLKDKGIDELIEAA------KILKKKgpnvrFLLVGDGE----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 551 PNSSSVVLMNVLKLIDQYDLYGQVaypkhhkqSEVPDIYRLAaktkGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGP 630
Cdd:cd03808 231 LENPSEILIEKLGLEGRIEFLGFR--------SDVPELLAES----DVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGC 298
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79325049 631 VDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNI 676
Cdd:cd03808 299 RELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRV 344
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
479-680 |
2.58e-17 |
|
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: 84.72 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 479 DRNQIKKPvppiwSEIMRFFSNPHKPTILALSRPDHKKNVTTLVKAFGECQPLRELANLVlILGNRDDIEEmpnsssvvl 558
Cdd:cd03811 169 DIDRIRAL-----AKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLV-ILGDGPLREE--------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 559 mnVLKLIDQYDLYGQVAYPkhhkqSEVPDIYRLAAKTKgVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALN 638
Cdd:cd03811 234 --LEKLAKELGLAERVIFL-----GFQSNPYPYLKKAD-LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGE 305
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 79325049 639 NGLLVDPHDqQAISDALLKLVANKHLWAECRKNGLKNIHRFS 680
Cdd:cd03811 306 NGLLVPDGD-AAALAGILAALLQKKLDAALRERLAKAQEAVF 346
|
|
| sucr_syn_bact_C |
TIGR02471 |
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ... |
811-1047 |
2.63e-17 |
|
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472.
Pssm-ID: 131524 Cd Length: 236 Bit Score: 82.51 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 811 GKIGFVLASGSSLQEVVDITQKnlINLEDFDAIVCNSGSEIYYpWRDMMVDADYETHVEYKWPGESIRSVILRLICTEPA 890
Cdd:TIGR02471 29 DAVGFGIATGRSVESAKSRYAK--LNLPSPDVLIARVGTEIYY-GPELQPDRFWQKHIDHDWRRQAVVEALADIPGLTLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 891 AEDDITEYASScstrcYAI------SVKQgvktrrvddLRQRLRMRGLRCNIVYTHAATrLNVIPLCASRIQALRYLSIR 964
Cdd:TIGR02471 106 DDQEQGPFKIS-----YLLdpegepILPQ---------IRQRLRQQSQAAKVILSCGWF-LDVLPLRASKGLALRYLSYR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 965 WGIDMSKTVFFLGEKGDtdyEDLLGGLHKTIilkgVVGSDSEKLlrseENFKREDAVpqespnisYVKENGGSQEIMSTL 1044
Cdd:TIGR02471 171 WGLPLEQILVAGDSGND---EEMLRGLTLGV----VVGNHDPEL----EGLRHQQRI--------YFANNPHAFGILEGI 231
|
...
gi 79325049 1045 EAY 1047
Cdd:TIGR02471 232 NHY 234
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
460-682 |
8.45e-16 |
|
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: 79.97 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 460 VLTQDSQEpdgDLKSLIGPDRNQIKKPVPPIWSEIMrffSNPHKPTILALSRPDHKKNVTTLVKAFgecqplRELANL-- 537
Cdd:cd03820 144 VLTEADKL---KKYKQPNSNVVVIPNPLSFPSEEPS---TNLKSKRILAVGRLTYQKGFDLLIEAW------ALIAKKhp 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 538 ---VLILGNRDDIEEMpnsssvvlmnvLKLIDQYDLYGQVAYPkhHKQSEVPDIYRLAAktkgVFINPALVEPFGLTLIE 614
Cdd:cd03820 212 dwkLRIYGDGPEREEL-----------EKLIDKLGLEDRVKLL--GPTKNIAEEYANSS----IFVLSSRYEGFPMVLLE 274
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325049 615 AAAYGLPIVAT-RNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNIHRFSWP 682
Cdd:cd03820 275 AMAYGLPIISFdCPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIE 343
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
598-691 |
1.11e-15 |
|
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: 80.03 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 598 VFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNIH 677
Cdd:cd03814 270 VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAE 349
|
90
....*....|....
gi 79325049 678 RFSWPEHCRNYLSH 691
Cdd:cd03814 350 RYSWEAFLDNLLDY 363
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
477-643 |
1.29e-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: 77.44 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 477 GPDRNQIKKPVPPIWSEIMRFFSNPHKptiLALSRPDHKKNVTTLVKAFGECQPLRELANLVLILGNRDDIEEMpnsssv 556
Cdd:cd01635 87 GPDSLESTRSELLALARLLVSLPLADK---VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEE------ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 557 vlmnvlKLIDQYDLYGQVAYPKHHKQSEVPDIYRLAAKtkgVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKA 636
Cdd:cd01635 158 ------ALAAALGLLERVVIIGGLVDDEVLELLLAAAD---VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
....*..
gi 79325049 637 LNNGLLV 643
Cdd:cd01635 229 GENGLLV 235
|
|
| HAD_SPP |
cd02605 |
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ... |
808-992 |
1.18e-14 |
|
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: 74.69 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 808 SGKGKIGFVLASGSSLQEVVDITQKNliNLEDFDAIVCNSGSEIYYPWRDMMV-DADYETHVEYKWPGESIRSVilrlic 886
Cdd:cd02605 31 TADNDVILVYATGRSPESVLELIKEV--MLPKPDFIISDVGTEIYYGESGYLEpDTYWNEVLSEGWERFLFEAI------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 887 tepaaEDDITEYASSCST--RCYAIS--VKQGVKTRRVDDLRQRLRMRGLRCNIVYTHAATR-LNVIPLCASRIQALRYL 961
Cdd:cd02605 103 -----ADLFKQLKPQSELeqNPHKISfyLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGLAYdLDILPLGAGKGEALRYL 177
|
170 180 190
....*....|....*....|....*....|.
gi 79325049 962 SIRWGIDMSKTVFFlGEKGDtDYEDLLGGLH 992
Cdd:cd02605 178 QEKWNFPPERTLVC-GDSGN-DIALLSTGTR 206
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
488-688 |
1.33e-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: 73.85 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 488 PPIWSEIMRFFSNPHKPTILALSRPDHKKNVTTLVKAFGEcqpLRELANLVLIL-GNRDDIEEMPnsssvvlmnvlKLID 566
Cdd:cd03817 186 PLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAE---LKKEPNIKLVIvGDGPEREELK-----------ELAR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 567 QYDLYGQVAYPKHHKQSEVPDIYRLAaktkGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPh 646
Cdd:cd03817 252 ELGLADKVIFTGFVPREELPEYYKAA----DLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEP- 326
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 79325049 647 DQQAISDALLKLVANKHLWAECRKNGLKNIHRFSWPEHCRNY 688
Cdd:cd03817 327 NDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKL 368
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
501-671 |
2.76e-13 |
|
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: 72.75 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 501 PHKPTILALSRPDHK--KNVTTLVKAfgeCQPLRELANLVLILGNRDDIEEMPNSSSVVLMNVLklidqydlygqvaypk 578
Cdd:cd03825 191 QDKKVILFGAESVTKprKGFDELIEA---LKLLATKDDLLLVVFGKNDPQIVILPFDIISLGYI---------------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 579 hHKQSEVPDIYRLAaktkGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKL 658
Cdd:cd03825 252 -DDDEQLVDIYSAA----DLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWL 326
|
170
....*....|...
gi 79325049 659 VANKHLWAECRKN 671
Cdd:cd03825 327 LANPKERESLGER 339
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
330-693 |
7.87e-13 |
|
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: 71.19 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 330 PYVIHGHYADA---GEVAAHLAGalNVPMVLTGHSLGRNKfeqllqqgritredidRTYKIMRRIEAEEQSLDAAEMVVT 406
Cdd:cd03807 80 PDVVHTWMYHAdliGGLAAKLAG--GVKVIWSVRSSNIPQ----------------RLTRLVRKLCLLLSKFSPATVANS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 407 STRQEIDAQWGlYDGfdiklerklrvrrrrgvsclgrymPRMVVIPPGMDFsYVLTQDSQEPDGDLKSLIGPDrnqikkp 486
Cdd:cd03807 142 SAVAEFHQEQG-YAK------------------------NKIVVIYNGIDL-FKLSPDDASRARARRRLGLAE------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 487 vppiwseimrffsnpHKPTILALSRPDHKKNVTTLVKAFGECQPLRELANLVLIL--GNRDDIEEMPNSSSvvlmnvlkL 564
Cdd:cd03807 189 ---------------DRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGrgPERPNLERLLLELG--------L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 565 IDQYDLYGQvaypkhhkQSEVPDIYRLAaktkGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKAlNNGLLVD 644
Cdd:cd03807 246 EDRVHLLGE--------RSDVPALLPAM----DIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDD-GTGFLVP 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 79325049 645 PHDQQAISDALLKLVANKHLWAECRKNGLKNI-HRFSWPEHCRNYLSHVE 693
Cdd:cd03807 313 AGDPQALADAIRALLEDPEKRARLGRAARERIaNEFSIDAMVRRYETLYY 362
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
295-667 |
1.46e-12 |
|
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: 70.08 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 295 SLWPHIPEFVDGALNHIVSIARSLGEQVNGGKPIW---PYVIHGHYADAGEVAAHLAGALNVPMVLTGHSLGRNKFEQLl 371
Cdd:cd03819 39 PLLPRLRQIGIGLPGLKVPLLRALLGNVRLARLIRrerIDLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPK- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 372 qqgritrediDRTYKIMRRIeaeeqslDAAEMVVTSTRQEIDAQWGLYDGfdiklerklrvrrrrgvsclgrympRMVVI 451
Cdd:cd03819 118 ----------DFALAVRARG-------DRVIAVSELVRDHLIEALGVDPE-------------------------RIRVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 452 PPGMDFSYVLTQDSQEPDGDLksliGPDRNqikkpvppiwseimrffsnphKPTILALSRPDHKKNVTTLVKAFGEcqpL 531
Cdd:cd03819 156 PNGVDTDRFPPEAEAEERAQL----GLPEG---------------------KPVVGYVGRLSPEKGWLLLVDAAAE---L 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 532 RELANLV-LILGnrdDIEEMPNsssvvlmnVLKLIDQYDLYGQVAYPKHHkqSEVPDIYRLAAktkgVFINPALVEPFGL 610
Cdd:cd03819 208 KDEPDFRlLVAG---DGPERDE--------IRRLVERLGLRDRVTFTGFR--EDVPAALAASD----VVVLPSLHEEFGR 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 79325049 611 TLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAE 667
Cdd:cd03819 271 VALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREK 327
|
|
| Sucrose_synth |
pfam00862 |
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ... |
197-412 |
1.69e-11 |
|
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.
Pssm-ID: 395692 Cd Length: 540 Bit Score: 68.06 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 197 IVLISMHGLVrGENMELGRDsDTGGQVKYVVELARALANtEGVHRVDL-----------LTRQIssPE-VDYSYGEPVEM 264
Cdd:pfam00862 266 VVILSPHGYF-GQANVLGLP-DTGGQVVYILDQVRALEN-ELLLRIKQqgldikpqilvVTRLI--PEaRGTTCNQELEK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 265 LscppegSDSCGSYIIRIPC----GSRDKYIPKESLWPHIPEFVDGALNHIVSIArslgeqvnGGKpiwPYVIHGHYADA 340
Cdd:pfam00862 341 I------SGTKHSHILRVPFrtenGILRQWISRFDIWPYLERFTQDAAKEILAEL--------EGK---PDLIIGNYSDG 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79325049 341 GEVAAHLAGALNVPMVLTGHSLGRNKFEqllqQGRITREDIDRTYKIMRRIEAEEQSLDAAEMVVTSTRQEI 412
Cdd:pfam00862 404 NLVASLLAHKLGVTQCTIAHALEKTKYE----DSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEI 471
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
516-676 |
1.94e-11 |
|
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: 66.99 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 516 KNVTTLVKAFGECQplRELANLVLILGNRDDIEEMpnsssvvlmnvLKLIDQYDLYGQVAYpkHHKQSEVPDIYRLAakt 595
Cdd:cd04962 209 KRIDDVVRVFARVR--RKIPAKLLLVGDGPERVPA-----------EELARELGVEDRVLF--LGKQDDVEELLSIA--- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 596 kGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKN 675
Cdd:cd04962 271 -DLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKR 349
|
.
gi 79325049 676 I 676
Cdd:cd04962 350 A 350
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
516-676 |
3.44e-11 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 66.20 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 516 KNVTTLVKAFGECQPLR-ELanlvLILGNRDDIEEMPNSssvvlmnvlkLIDQYDLYGQVaypkhhKQSEVPDIYRLAAk 594
Cdd:cd03823 204 KGIDLLVEAFKRLPREDiEL----VIAGHGPLSDERQIE----------GGRRIAFLGRV------PTDDIKDFYEKID- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 595 tkgVFINPAL-VEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGL 673
Cdd:cd03823 263 ---VLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAE 339
|
...
gi 79325049 674 KNI 676
Cdd:cd03823 340 PPR 342
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
482-685 |
1.08e-10 |
|
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: 64.24 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 482 QIKKPVPPIWSeIMRFFSNPHKPTILALSRPDHK----------KNVTTLVKAFGecQPLRELANLVLILGNRDDIEEMP 551
Cdd:cd04949 130 ERFNKYPPIFT-IPVGYVDQLDTAESNHERKSNKiitisrlapeKQLDHLIEAVA--KAVKKVPEITLDIYGYGEEREKL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 552 NsssvvlmnvlKLIDQYDLYGQVAYPKHHKQseVPDIYRLAaktkGVFINPALVEPFGLTLIEAAAYGLPIVATR-NGGP 630
Cdd:cd04949 207 K----------KLIEELHLEDNVFLKGYHSN--LDQEYQDA----YLSLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGP 270
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79325049 631 VDIVKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNIHRFSwPEHC 685
Cdd:cd04949 271 SELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEKYS-TENV 324
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
478-685 |
2.48e-10 |
|
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: 64.28 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 478 PDRNQIkkpVPP-----IWSEIMRFFSNPHKPTILALSRPDHKKNVTTLVKAFGECQPLRELANLvLILGNRDDIEEMpn 552
Cdd:cd03813 266 PDKTRV---IPNgidiqRFAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEG-WLIGPEDEDPEY-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 553 sssvvLMNVLKLIDQYDLYGQVaypkhhKQSEVPDIYRLAAKTkGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVD 632
Cdd:cd03813 340 -----AQECKRLVASLGLENKV------KFLGFQNIKEYYPKL-GLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRE 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79325049 633 IVKALNN-----GLLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNIHRFSWPEHC 685
Cdd:cd03813 408 LIYGADDalgqaGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGM 465
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
489-689 |
3.35e-09 |
|
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: 60.05 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 489 PIWSEiMRFFSNPHKPTILALSRPDHKKNVTtLVKAFGECQPLRELANLVLILGNRDDIE-----EMPNSSSVVLMNVLK 563
Cdd:cd03794 192 PNWAD-LEEFKPPPKDELRKKLGLDDKFVVV-YAGNIGKAQGLETLLEAAERLKRRPDIRflfvgDGDEKERLKELAKAR 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 564 LIDQYDLYGQVAYpkhhkqSEVPDIYRLAakTKGVFI---NPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNG 640
Cdd:cd03794 270 GLDNVTFLGRVPK------EEVPELLSAA--DVGLVPlkdNPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCG 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79325049 641 LLVDPHDQQAISDALLKLVANKHLWAECRKNGLKNI-HRFSWpEHCRNYL 689
Cdd:cd03794 342 LVVEPGDPEALADAILELLDDPELRRAMGENGRELAeEKFSR-EKLADRL 390
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
602-681 |
4.31e-08 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 57.02 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 602 PALVEPFGLTLIEAAAYG-LPIVAtRNGGPVDIVKALN------NGLLVDPHDQQAISDAL---LKLVANKHLWAECRKN 671
Cdd:COG0297 376 PSRFEPCGLNQMYALRYGtVPIVR-RTGGLADTVIDYNeatgegTGFVFDEYTAEALLAAIrraLALYRDPEAWRKLQRN 454
|
90
....*....|
gi 79325049 672 GLKniHRFSW 681
Cdd:COG0297 455 AMK--QDFSW 462
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
599-681 |
8.87e-08 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 56.03 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 599 FINPALVEPFGLTLIEAAAYG-LPIVAtRNGGPVDIVKALN------NGLLVDPHDQQAISDAL---LKLVANKHLWAEC 668
Cdd:cd03791 372 FLMPSRFEPCGLVQMYAMRYGtLPIVR-RTGGLADTVFDYDpetgegTGFVFEDYDAEALLAALrraLALYRNPELWRKL 450
|
90
....*....|...
gi 79325049 669 RKNGLKniHRFSW 681
Cdd:cd03791 451 QKNAMK--QDFSW 461
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
220-454 |
3.54e-07 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 50.86 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 220 GGQVKYVVELARALAntEGVHRVDLLTRQisspevDYSYGEPVEMLSCPpegsdscgsyIIRIPCGSRDKYIpkeslwph 299
Cdd:pfam13579 1 GGIGVYVLELARALA--ALGHEVRVVTPG------GPPGRPELVGDGVR----------VHRLPVPPRPSPL-------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 300 ipefvdGALNHIVSIARSLGEQvnggkpiWPYVIHGHYADAGEVAAHLAGALNVPMVLTGHSLGRNkfEQLLQQGRItre 379
Cdd:pfam13579 55 ------ADLAALRRLRRLLRAE-------RPDVVHAHSPTAGLAARLARRRRGVPLVVTVHGLALD--YGSGWKRRL--- 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79325049 380 didrtykimrRIEAEEQSLDAAEMVVTSTRQEIDAqwglydgfdiklerklrvrrrrgVSCLGRYMPRMVVIPPG 454
Cdd:pfam13579 117 ----------ARALERRLLRRADAVVVVSEAEAEL-----------------------LRALGVPAARVVVVPNG 158
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
606-658 |
4.19e-07 |
|
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: 53.06 E-value: 4.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 79325049 606 EPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPhdQQAISDALLKL 658
Cdd:cd03802 251 EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS--VEEMAEAIANI 301
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
606-661 |
4.87e-07 |
|
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: 53.05 E-value: 4.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 79325049 606 EPFGLTLIEAAAYGLPIVATR-NGGPVDIVKALNNGLLVDPHDQQAISDALLKLVAN 661
Cdd:cd03795 274 EAFGIVLLEAMMCGKPVISTNiGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSD 330
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
216-682 |
7.94e-07 |
|
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: 52.76 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 216 DSDTGGQVKYVVELARALANtEGvHRVDLltrqisspevdYSYGEPVEMLSCPPEGsdscgsyiiripcgsrdKYIPKES 295
Cdd:cd03821 10 SPKAGGPVKVVLRLAAALAA-LG-HEVTI-----------VSTGDGYESLVVEENG-----------------RYIPPQD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 296 LWPHIPEFVDGALNHIVSIarSLGEQVNGGKPIWPYV-IHGHYADAGEVAAHLAGALNVPMVLTGH-SLGRNKFEQLLQQ 373
Cdd:cd03821 60 GFASIPLLRQGAGRTDFSP--GLPNWLRRNLREYDVVhIHGVWTYTSLAACKLARRRGIPYVVSPHgMLDPWALQQKHWK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 374 GRITREDIdrtykimrrieaEEQSLDAAEMVVTSTRQEIDAQWGLYDGfdiklerklrvrrrrgvsclgrymPRMVVIPP 453
Cdd:cd03821 138 KRIALHLI------------ERRNLNNAALVHFTSEQEADELRRFGLE------------------------PPIAVIPN 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 454 GMDfsyvltqdsqepdgdLKSLIGPDRNQIKKPVPPiwseimrffsnpHKPTILALSRPDHKKNVTTLVKAFgecqplRE 533
Cdd:cd03821 182 GVD---------------IPEFDPGLRDRRKHNGLE------------DRRIILFLGRIHPKKGLDLLIRAA------RK 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 534 LANL-----VLILGNRDDIEEMpnsssvvlmnVLKLIDQYDLYGQVAYPKHHKQSEVPDIYRLAAktkgVFINPALVEPF 608
Cdd:cd03821 229 LAEQgrdwhLVIAGPDDGAYPA----------FLQLQSSLGLGDRVTFTGPLYGEAKWALYASAD----LFVLPSYSENF 294
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79325049 609 GLTLIEAAAYGLPIVATRNGGPVDIVKAlNNGLLVDPHDqQAISDALLKLVANKHLWAECRKNGLKNIH---RFSWP 682
Cdd:cd03821 295 GNVVAEALACGLPVVITDKCGLSELVEA-GCGVVVDPNV-SSLAEALAEALRDPADRKRLGEMARRARQveeNFSWE 369
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
496-661 |
1.52e-06 |
|
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: 51.86 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 496 RFFSNPHKP-----TILALSRPDHKKNVTTLVKAFGE-CQPLRelaNLVLILGN----RDDIEEMpnsssvvlmnvlklI 565
Cdd:cd03796 181 DFTPDPSKPdpnkiTIVVISRLVYRKGIDLLVGIIPRiCKKHP---NVRFIIGGdgpkRIELEEM--------------R 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 566 DQYDLYGQV---AYPKHHkqsEVPDIYRlaaktKG-VFINPALVEPFGLTLIEAAAYGLPIVATRNGG-----PVDIVka 636
Cdd:cd03796 244 EKYQLQDRVellGAVPHE---EVRDVLV-----QGhIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGipevlPPDMI-- 313
|
170 180
....*....|....*....|....*
gi 79325049 637 lnngLLVDPhDQQAISDALLKLVAN 661
Cdd:cd03796 314 ----LLAEP-DPEDIVRKLEEAISI 333
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
560-672 |
1.89e-06 |
|
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: 51.30 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 560 NVLKLIDQYDLYGQVAYPKHHKQSEVPDIYRLAAktkgVFINPALVEPFG------LTLIEAAAYGLPIVATRNGGPVDI 633
Cdd:cd03799 219 QLQQLIQELNIGDCVKLLGWKPQEEIIEILDEAD----IFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPEL 294
|
90 100 110
....*....|....*....|....*....|....*....
gi 79325049 634 VKALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNG 672
Cdd:cd03799 295 VEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAG 333
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
598-681 |
4.64e-06 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 50.48 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 598 VFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIV---KALNNGLLVDPHDQQAISDALLKLVANKHLWAECRKNGLK 674
Cdd:PLN02871 334 VFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAARE 413
|
....*..
gi 79325049 675 NIHRFSW 681
Cdd:PLN02871 414 EVEKWDW 420
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
504-664 |
4.81e-06 |
|
glycosyltransferase family 4 proteins; 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 glycosyltransferase family 4 (GT4). 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.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 50.14 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 504 PTILALSRPDHKKNVTTLVKAFGECQPLRELANLVLIlgnrDDIEEMPnsssvvlmnvlKLIDQYDLYGQVAYPKHHKQS 583
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIA----GDGPLRP-----------ALQALAAALGRVRFLGALPHA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 584 EVPDIYRLAAktkgVFINPALV------EPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLK 657
Cdd:cd05844 255 EVQDWMRRAE----IFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQA 330
|
....*..
gi 79325049 658 LVANKHL 664
Cdd:cd05844 331 LLADRAL 337
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
500-689 |
1.11e-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: 48.86 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 500 NPHKPTILALSRPDHKKNVTTLVKAFGECQPLRELANLVLILGNRDDIEEmpnsSSVVLMNVLKLIDQYDLYGQVAYPKH 579
Cdd:cd03792 194 DPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDPE----GSVVYEEVMEYAGDDHDIHVLRLPPS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 580 HKqsEVPDIYRlAAKtkgVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISdaLLKLV 659
Cdd:cd03792 270 DQ--EINALQR-AAT---VVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVR--ILRLL 341
|
170 180 190
....*....|....*....|....*....|.
gi 79325049 660 ANKHLWAECRKNGLKNI-HRFSWPEHCRNYL 689
Cdd:cd03792 342 TDPELRRKMGLAAREHVrDNFLITGNLRAWL 372
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
506-659 |
3.10e-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: 47.44 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 506 ILALSRPDHKKNVTTLVKAFGECqPLRELANLVLILGN---RDDIEEmpnsssvvLMNVLKLIDQYDLYGQVaypkhhkq 582
Cdd:cd04951 191 ILNVGRLTEAKDYPNLLLAISEL-ILSKNDFKLLIAGDgplRNELER--------LICNLNLVDRVILLGQI-------- 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79325049 583 SEVPDIYRLAaktkGVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNngLLVDPHDQQAISDALLKLV 659
Cdd:cd04951 254 SNISEYYNAA----DLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHN--YVVPVSDPQLLAEKIKEIF 324
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
446-687 |
5.29e-05 |
|
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: 46.81 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 446 PRMVVIPPgMDFSYvltQDSQEPDGDLKsligpdrnqikkpVPPIWSEimrffsnphKPTILALSRPDHKKNVTTLVKAF 525
Cdd:cd03805 180 PPEVLYPC-VDTDS---FDSTSEDPDPG-------------DLIAKSN---------KKFFLSINRFERKKNIALAIEAF 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 526 GE-CQPLRELANLVLIL--GNRDDIEEmpnssSVVLMNVLKLI--DQYDLYGQVAYpkhhkQSEVPDIYR--LAAKTKGV 598
Cdd:cd03805 234 AKlKQKLPEFENVRLVIagGYDPRVAE-----NVEYLEELQRLaeELLNVEDQVLF-----LRSISDSQKeqLLSSALAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 599 FINPAlVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPhDQQAISDALLKLVANKHLWAECRKNGLKNIH- 677
Cdd:cd03805 304 LYTPS-NEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKe 381
|
250
....*....|
gi 79325049 678 RFSWPEHCRN 687
Cdd:cd03805 382 KFSREAFAER 391
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
546-676 |
1.61e-04 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 45.14 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 546 DIEEMPNSSSVVLMNVLKLIDQYDLYGQVAYpkhhkqsevpdiyrlaaktkGVFINPALVEPFGLTLIEAAAYGLPIVAT 625
Cdd:cd04946 275 LAENKLENVKVNFTGEVSNKEVKQLYKENDV--------------------DVFVNVSESEGIPVSIMEAISFGIPVIAT 334
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 79325049 626 RNGGPVDIVKALNNGLLVD----PHDqqaISDALLKLVANKHLWAECRKNGLKNI 676
Cdd:cd04946 335 NVGGTREIVENETNGLLLDkdptPNE---IVSSIMKFYLDGGDYKTMKISARECW 386
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
598-689 |
2.12e-04 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 45.11 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 598 VFINPALVEPFGLTLIEAAAYG-LPIVAtRNGGPVDIVKALN------NGLLVDPHDQQAISDAL---LKLVANKHLWAE 667
Cdd:PRK00654 359 MFLMPSRFEPCGLTQLYALRYGtLPIVR-RTGGLADTVIDYNpedgeaTGFVFDDFNAEDLLRALrraLELYRQPPLWRA 437
|
90 100
....*....|....*....|..
gi 79325049 668 CRKNGLKniHRFSWPEHCRNYL 689
Cdd:PRK00654 438 LQRQAMA--QDFSWDKSAEEYL 457
|
|
| PLN02382 |
PLN02382 |
probable sucrose-phosphatase |
841-961 |
5.37e-04 |
|
probable sucrose-phosphatase
Pssm-ID: 178008 [Multi-domain] Cd Length: 413 Bit Score: 43.82 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 841 DAIVCNSGSEIYYPwrDMMV-DADYETHVEYKWPGESIRSVILRLICTEPAAEDDITEYASSCStrcyaISVKQGVKTRR 919
Cdd:PLN02382 72 DITIMSVGTEIAYG--ESMVpDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFY-----VDKKKAQEVIK 144
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 79325049 920 VddLRQRLRMRGLRCNIVYTHAATrLNVIPLCASRIQALRYL 961
Cdd:PLN02382 145 E--LSERLEKRGLDVKIIYSGGID-LDVLPQGAGKGQALAYL 183
|
|
| Cof |
COG0561 |
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ... |
813-981 |
1.03e-03 |
|
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440327 [Multi-domain] Cd Length: 192 Bit Score: 41.27 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 813 IGFVLASGSSLQEVVDItqknLINLEDFDAIVCNSGSEIYYPwrdmmvdadyethveykwPGESIRSVILrlictepAAE 892
Cdd:COG0561 36 IKVVIATGRPLRSALPL----LEELGLDDPLITSNGALIYDP------------------DGEVLYERPL-------DPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 893 DditeyasscstrcyaisvkqgvktrrVDDLRQRLRMRGLRCNIVYTHAATRLNVIPLCASRIQALRYLSIRWGIDMSKT 972
Cdd:COG0561 87 D--------------------------VREILELLREHGLHLQVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEV 140
|
....*....
gi 79325049 973 VFFlgekGD 981
Cdd:COG0561 141 IAF----GD 145
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
588-680 |
1.30e-03 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 42.27 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 588 IYRLAAKTKGvFINPAlVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGLLVDPHDQQAISDALLKLVANKHLW-- 665
Cdd:cd03804 259 LKELLSKARA-FVFAA-EEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQNFDRFkp 336
|
90
....*....|....*
gi 79325049 666 AECRKNGLknihRFS 680
Cdd:cd03804 337 QAIRANAE----RFS 347
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
501-681 |
4.15e-03 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 40.93 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 501 PHKPTILALSRPDHKKNVTTLVKAFGECQPLRELANLVLIlgnrDDIEEMPNS-----SSVVLMNVLKLIDQYDLYGQVA 575
Cdd:PRK15484 191 PDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVV----GDPTASSKGekaayQKKVLEAAKRIGDRCIMLGGQP 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 576 YPKHHKqsevpdIYRLAAKtkgVFINPALVEPFGLTLIEAAAYGLPIVATRNGGPVDIVKALNNGL-LVDPHDQQAISDA 654
Cdd:PRK15484 267 PEKMHN------YYPLADL---VVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISD 337
|
170 180
....*....|....*....|....*...
gi 79325049 655 LLKLVANKHLwAECRKNGLKNI-HRFSW 681
Cdd:PRK15484 338 INRTLADPEL-TQIAEQAKDFVfSKYSW 364
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
602-688 |
5.11e-03 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 40.47 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325049 602 PALVEPFGLTLIEAAAYG-LPIVAtRNGGPVDIVKALN---------NGLLVDPHDQQAISDALLK---LVANKHLWAEC 668
Cdd:PRK14099 376 PSRFEPCGLTQLCALRYGaVPVVA-RVGGLADTVVDANemaiatgvaTGVQFSPVTADALAAALRKtaaLFADPVAWRRL 454
|
90 100
....*....|....*....|
gi 79325049 669 RKNGLKNihRFSWPEHCRNY 688
Cdd:PRK14099 455 QRNGMTT--DVSWRNPAQHY 472
|
|
| |
