|
Name |
Accession |
Description |
Interval |
E-value |
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
5-429 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 905.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 5 EKNDHLMLARQLPLKSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHI 84
Cdd:PRK00725 1 EKNDSLMLARQLTRDTLALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 85 QRGWSFFNEEMNEFVDLLPAQQRMKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCT 164
Cdd:PRK00725 81 QRGWSFFREELGEFVDLLPAQQRVDEENWYRGTADAVYQNLDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 165 VACMPVPIEEASAFGVMAVDENDKIIEFVEKPANPPSMPNDPSKSLASMGIYVFDADYLYELLEEDDRDENSSHDFGKDL 244
Cdd:PRK00725 161 VACLEVPREEASAFGVMAVDENDRITAFVEKPANPPAMPGDPDKSLASMGIYVFNADYLYELLEEDAEDPNSSHDFGKDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 245 IPKITEAGLAYAHPFPLSCVQSDPDAEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTYNESLPPAKFVQDRSG 324
Cdd:PRK00725 241 IPKIVEEGKVYAHPFSDSCVRSDPEEEPYWRDVGTLDAYWQANLDLASVTPELDLYDRNWPIWTYQEQLPPAKFVFDRSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 325 SHGMTLNSLVSGGCVISGSVVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDA 404
Cdd:PRK00725 321 RRGMAINSLVSGGCIISGAVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGMVIGEDPEEDA 400
|
410 420
....*....|....*....|....*
6SHJ_A 405 RRFYRSEEGIVLVTREMLRKLGHKQ 429
Cdd:PRK00725 401 KRFRRSEEGIVLVTREMLDKLGGKQ 425
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
19-422 |
0e+00 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 609.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 19 KSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRG--WSFFNEemN 96
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGkpWDLDRK--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 97 EFVDLLPAQQRMKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEAS 176
Cdd:COG0448 79 GGVFILPPYQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 177 AFGVMAVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVFDADYLYELLEEDdrDENSSHDFGKDLIPKITEAGLAYA 256
Cdd:COG0448 159 RFGVMEVDEDGRITEFEEKPKDPKS-------ALASMGIYVFNKDVLIELLEED--APNSSHDFGKDIIPRLLDRGKVYA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 257 HPFplscvqsdpdaEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTYNESLPPAKFVQDrsgshGMTLNSLVSG 336
Cdd:COG0448 230 YEF-----------DGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFVRG-----GKVKNSLVSN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 337 GCVISGSvVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDARRFYRSeEGIVL 416
Cdd:COG0448 294 GCIISGT-VENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIGEDPEEDRKRFTVS-SGIVV 371
|
....*.
6SHJ_A 417 VTREML 422
Cdd:COG0448 372 VGKGAV 377
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
22-398 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273965 [Multi-domain] Cd Length: 361 Bit Score: 593.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEeMNEFVDL 101
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDGF-IDGFVTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRMKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEASAFGVM 181
Cdd:TIGR02091 80 LPAQQRESGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGVM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 182 AVDENDKIIEFVEKPANPPSMPNDPSKSLASMGIYVFDADYLYELLEEDDRDENSSHDFGKDLIPKITEAGLAYAHPFpl 261
Cdd:TIGR02091 160 QVDEDGRIVDFEEKPANPPSIPGMPDFALASMGIYIFDKDVLKELLEEDADDPESSHDFGKDIIPRALEEGSVQAYLF-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 262 scvqsdpdaEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTYNESLPPAKFVqdrsGSHGMTLNSLVSGGCVIS 341
Cdd:TIGR02091 238 ---------SGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFV----DSDAQVVDSLVSEGCIIS 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
6SHJ_A 342 GSVVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGE 398
Cdd:TIGR02091 305 GATVSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKNVRIGEGVVIGN 361
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
22-417 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 546.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEeMNEFVDL 101
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGL-LGNYITP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRMkGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEASAFGVM 181
Cdd:PRK00844 87 VPAQQRL-GKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEASAFGVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 182 AVDENDKIIEFVEKPANPPSMPNDPSKSLASMGIYVFDADYLYELLEEDDRDENSSHDFGKDLIPKITEAGLAYAHPFPL 261
Cdd:PRK00844 166 EVDPDGRIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVERGRAYVYDFST 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 262 SCVQSDPDAEP-YWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTYNESLPPAKFVqDRSGSHGMTLNSLVSGGCVI 340
Cdd:PRK00844 246 NEVPGATERDRgYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNLPPAKFV-DGGGRVGSAQDSLVSAGSII 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
6SHJ_A 341 SGSVVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDARRFYRSEEGIVLV 417
Cdd:PRK00844 325 SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEEDRRRFTVSEGGIVVV 401
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
21-402 |
6.59e-159 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 453.17 E-value: 6.59e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 21 VALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVD 100
Cdd:PRK05293 5 LAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGSPWDLDRINGGVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 101 LLPAQQRMKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEASAFGV 180
Cdd:PRK05293 85 ILPPYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEASRFGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 181 MAVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVFDADYLYELLEEDDRDENSSHDFGKDLIPKITEAGLA-YAHPF 259
Cdd:PRK05293 165 MNTDENMRIVEFEEKPKNPKS-------NLASMGIYIFNWKRLKEYLIEDEKNPNSSHDFGKNVIPLYLEEGEKlYAYPF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 260 plscvqsdpdaEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTYNESLPPAkFVqdrsGSHGMTLNSLVSGGCV 339
Cdd:PRK05293 238 -----------KGYWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQ-YI----AENAKVKNSLVVEGCV 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
6SHJ_A 340 ISGSvVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEE 402
Cdd:PRK05293 302 VYGT-VEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKEV 363
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
19-417 |
1.06e-119 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 355.35 E-value: 1.06e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 19 KSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSF--FNeemN 96
Cdd:PRK02862 3 RVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYNFdgFS---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 97 EFVDLLPAQQRMKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEAS 176
Cdd:PRK02862 80 GFVEVLAAQQTPENPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVDEKDAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 177 AFGVMAVDENDKIIEFVEKP--------ANPPS---MPNDPSKS---LASMGIYVFDADYLYELLEEDDrdenSSHDFGK 242
Cdd:PRK02862 160 GFGLMKTDDDGRITEFSEKPkgdelkamAVDTSrlgLSPEEAKGkpyLASMGIYVFSRDVLFDLLNKNP----EYTDFGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 243 DLIPkitEAGLAY---AHPFplscvqsdpdaEPYWRDVGTLEAYWKANLDLA-SVVPELDMYDRNWPIRTYNESLPPAKF 318
Cdd:PRK02862 236 EIIP---EAIRDYkvqSYLF-----------DGYWEDIGTIEAFYEANLALTqQPNPPFSFYDEKAPIYTRARYLPPSKL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 319 VqdrsGSHgMTlNSLVSGGCVISGSVVVQSVLFSRVRVNSFCNIDSAVLL-------------------PEVWVGRSCRL 379
Cdd:PRK02862 302 L----DAT-IT-ESIIAEGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMgadfyesseereelrkegkPPLGIGEGTTI 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....
6SHJ_A 380 RRCVIDRACVIPEGMVIG-----ENAEEDARRFY-RSeeGIVLV 417
Cdd:PRK02862 376 KRAIIDKNARIGNNVRIVnkdnvEEADREDQGFYiRD--GIVVV 417
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
19-417 |
2.07e-109 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 329.12 E-value: 2.07e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 19 KSV-ALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNE 97
Cdd:PLN02241 2 KSVaAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFGNGGNFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 98 --FVDLLPAQQRMKGENWYRGTADAVTQNLDIIRRYKA---EYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPI 172
Cdd:PLN02241 82 dgFVEVLAATQTPGEKGWFQGTADAVRQFLWLFEDAKNknvEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLPVDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 173 EEASAFGVMAVDENDKIIEFVEKP--ANPPSM----------PNDPSKS--LASMGIYVFDADYLYELLeedDRDENSSH 238
Cdd:PLN02241 162 SRASDFGLMKIDDTGRIIEFSEKPkgDELKAMqvdttvlglsPEEAKEKpyIASMGIYVFKKDVLLKLL---RWRFPTAN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 239 DFGKDLIPKITEAGL---AYAHPfplscvqsdpdaePYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTYNESLPP 315
Cdd:PLN02241 239 DFGSEIIPGAIKEGYnvqAYLFD-------------GYWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYTSPRFLPP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 316 AKFVQDRsgshgmTLNSLVSGGCVISGSVVVQSVLFSRVRVNSFCNIDSAVLL-------------------PEVWVGRS 376
Cdd:PLN02241 306 SKIEDCR------ITDSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMgadyyeteeeiasllaegkVPIGIGEN 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
6SHJ_A 377 CRLRRCVIDRACVIPEGMVI--GENAEEDARR---FYRSeEGIVLV 417
Cdd:PLN02241 380 TKIRNAIIDKNARIGKNVVIinKDGVQEADREeegYYIR-SGIVVI 424
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
22-277 |
2.61e-100 |
|
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.
Pssm-ID: 133002 [Multi-domain] Cd Length: 200 Bit Score: 297.53 E-value: 2.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDL 101
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRKNGGLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRmKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMpvpieeasafgvm 181
Cdd:cd02508 81 LPPQQR-KGGDWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVVYK------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 182 avdendkiiefvekpanppsmpndpskslASMGIYVFDADYLYELLEEDDRDenSSHDFGKDLIPKITEAGLAYAHPFPl 261
Cdd:cd02508 147 -----------------------------ASMGIYIFSKDLLIELLEEDAAD--GSHDFGKDIIPAMLKKLKIYAYEFN- 194
|
250
....*....|....*.
6SHJ_A 262 scvqsdpdaePYWRDV 277
Cdd:cd02508 195 ----------GYWADI 200
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
21-291 |
8.43e-86 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 261.80 E-value: 8.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 21 VALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVI-TQYQSHTLVQHIQRGWSFFNEEmnefv 99
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREIIVIlTQEHRFMLNELLGDGSKFGVQI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 100 dlLPAQQRMKgenwyRGTADAVTQNLDIIRRYKAEyVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEASAFG 179
Cdd:pfam00483 76 --TYALQPEG-----KGTAPAVALAADFLGDEKSD-VLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 180 VMAVDENDKIIEFVEKPANPpsmpndPSKSLASMGIYVFDADYLYELLeEDDRDENSSHDFGKDLIPKITEAG-LAYAHP 258
Cdd:pfam00483 148 VVEFDDNGRVIRFVEKPKLP------KASNYASMGIYIFNSGVLDFLA-KYLEELKRGEDEITDILPKALEDGkLAYAFI 220
|
250 260 270
....*....|....*....|....*....|...
6SHJ_A 259 FPLSCvqsdpdaepyWRDVGTLEAYWKANLDLA 291
Cdd:pfam00483 221 FKGYA----------WLDVGTWDSLWEANLFLL 243
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
22-278 |
1.09e-45 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 157.36 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFneemnefVDL 101
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGK-PILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFG-------VNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRMKgenwyRGTADAVTQNLDIIrryKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVpiEEASAFGVM 181
Cdd:cd04181 73 EYVVQEEP-----LGTAGAVRNAEDFL---GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEV--EDPSRYGVV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 182 AVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVFDadylYELLEEDDRDENSSHDFGKDLIPKITEAGLAYAHPFPL 261
Cdd:cd04181 143 ELDDDGRVTRFVEKPTLPES-------NLANAGIYIFE----PEILDYIPEILPRGEDELTDAIPLLIEEGKVYGYPVDG 211
|
250
....*....|....*..
6SHJ_A 262 scvqsdpdaepYWRDVG 278
Cdd:cd04181 212 -----------YWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
22-292 |
1.20e-42 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 149.92 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGwSFFNEEMnEFVDl 101
Cdd:COG1208 2 AVILAGGLGTRLRPLTDTRPKPLLPVGGK-PLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDG-SRFGVRI-TYVD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 lpaqqrmkgENWYRGTADAVTQNLDIIrryKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACmpVPIEEASAFGVM 181
Cdd:COG1208 78 ---------EGEPLGTGGALKRALPLL---GDEPFLVLNGDILTDLDLAALLAFHREKGADATLAL--VPVPDPSRYGVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 182 AVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVFDADyLYELLEEDDRdenssHDFGkDLIPKITEAGLAYAHPFpl 261
Cdd:COG1208 144 ELDGDGRVTRFVEKPEEPPS-------NLINAGIYVLEPE-IFDYIPEGEP-----FDLE-DLLPRLIAEGRVYGYVH-- 207
|
250 260 270
....*....|....*....|....*....|.
6SHJ_A 262 scvqsdpdaEPYWRDVGTLEAYWKANLDLAS 292
Cdd:COG1208 208 ---------DGYWLDIGTPEDLLEANALLLS 229
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
321-422 |
4.92e-41 |
|
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.
Pssm-ID: 100056 [Multi-domain] Cd Length: 104 Bit Score: 141.06 E-value: 4.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 321 DRSGSHGMTLNSLVSGGCVISGSVVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENA 400
Cdd:cd04651 2 PYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGDP 81
|
90 100
....*....|....*....|..
6SHJ_A 401 EEDARRFYRSEEGIVLVTREML 422
Cdd:cd04651 82 EEDRARFYVTEDGIVVVGKGMV 103
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
33-401 |
6.35e-38 |
|
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273966 [Multi-domain] Cd Length: 369 Bit Score: 140.98 E-value: 6.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 33 LKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQS-HTLVQHIQRG--WSffneeMNEFVDLLPAQQRMK 109
Cdd:TIGR02092 16 LSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHLGSGreWD-----LHRKRDGLFVFPYND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 110 GENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPV-PIEEASAFGVMAVDENDK 188
Cdd:TIGR02092 91 RDDLSEGGKRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVkPADASEYDTILRFDESGK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 189 IIEFVEkpanppsMPNDPSKSLASMGIYVFDADYLYELLEEDDR--DENSSHDFGKDLIPKITEAglAYAHPFPLSCVQS 266
Cdd:TIGR02092 171 VKSIGQ-------NLNPEEEENISLDIYIVSTDLLIELLYECIQrgKLTSLEELIRENLKELNIN--AYEYTGYLANINS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 267 dpdaepywrdvgtLEAYWKANLDL--ASVVPELdMYDRNWPIRTYNESLPPAKFVQdrsgsHGMTLNSLVSGGCVISGSv 344
Cdd:TIGR02092 242 -------------VKSYYKANMDLldPQNFQSL-FYSSQGPIYTKVKDEPPTYYAE-----NSKVENSLVANGCIIEGK- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
6SHJ_A 345 VVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAE 401
Cdd:TIGR02092 302 VENSILSRGVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPNVKIAGTSE 358
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
22-218 |
1.37e-24 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 101.11 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHtLVQHIQRGWSFFNeeMNefVDL 101
Cdd:cd04189 3 GLILAGGKGTRLRPLTYTRPKQLIPVAGK-PIIQYAIEDLREAGIEDIGIVVGPTGE-EIKEALGDGSRFG--VR--ITY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRmkgenwyRGTADAVTQNLDIIRRykAEYVVILaGDHIYKQDYSRMLIDHVEKGARCTVACMPVPieEASAFGVm 181
Cdd:cd04189 77 ILQEEP-------LGLAHAVLAARDFLGD--EPFVVYL-GDNLIQEGISPLVRDFLEEDADASILLAEVE--DPRRFGV- 143
|
170 180 190
....*....|....*....|....*....|....*..
6SHJ_A 182 AVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVF 218
Cdd:cd04189 144 AVVDDGRIVRLVEKPKEPPS-------NLALVGVYAF 173
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
22-400 |
4.29e-24 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 103.06 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFneemnefVDL 101
Cdd:TIGR03992 3 AVILAAGKGTRMRPLTETRPKPMLPVAGK-PLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGG-------VPI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRMKgenwyRGTADAVTQnldiIRRYKAEYVVILAGDHIYKQDYSRMLIDhVEKGARCTVacmpvPIEEASAFGVM 181
Cdd:TIGR03992 75 EYVVQEEQ-----LGTADALGS----AKEYVDDEFLVLNGDVLLDSDLLERLIR-AEAPAIAVV-----EVDDPSDYGVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 182 AVDeNDKIIEFVEKPANPPSmpndpskSLASMGIYVFDADyLYELLEEDDRDENSSHDFgKDLIPKITEAGLAYAhpfpl 261
Cdd:TIGR03992 140 ETD-GGRVTGIVEKPENPPS-------NLINAGIYLFSPE-IFELLEKTKLSPRGEYEL-TDALQLLIDEGKVKA----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 262 scVQSDpdaePYWRDVGtleaywkanldlasvvpeldmydRNWPIRTYNEslppakfvqdrsgshgMTLNSLVSGgcvIS 341
Cdd:TIGR03992 205 --VELD----GFWLDVG-----------------------RPWDLLDANE----------------ALLDNLEPR---IE 236
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 342 GSVVvqsvlfsrvrvnsfcniDSAVLLPEVWVGRSCRLRR-CVIDRACVIPEGMVIGENA 400
Cdd:TIGR03992 237 GTVE-----------------ENVTIKGPVVIGEGAVIRSgTYIEGPVYIGKNCDIGPNA 279
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
22-287 |
2.88e-22 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 94.50 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRG--W----SFFNEEm 95
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGK-PILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGskFgvniSYVRED- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 96 nefvdllpaqQRMkgenwyrGTADAvtqnLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVAC----MPVP 171
Cdd:cd06426 79 ----------KPL-------GTAGA----LSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyeVQVP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 172 ieeasaFGVMAVDeNDKIIEFVEKPANppsmpndpsKSLASMGIYVFDADYLyELLEeddrdENSSHDFgKDLIPKITEA 251
Cdd:cd06426 138 ------YGVVETE-GGRITSIEEKPTH---------SFLVNAGIYVLEPEVL-DLIP-----KNEFFDM-PDLIEKLIKE 194
|
250 260 270
....*....|....*....|....*....|....*.
6SHJ_A 252 GLAyahpfplscVQSDPDAEpYWRDVGTLEAYWKAN 287
Cdd:cd06426 195 GKK---------VGVFPIHE-YWLDIGRPEDYEKAN 220
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
22-234 |
1.44e-20 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 91.30 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITqyqshTlvqhiqrgwsffNEEMNEFVDL 101
Cdd:COG1209 3 GIILAGGSGTRLRPLTLTVSKQLLPVYDK-PMIYYPLSTLMLAGIREILIIS-----T------------PEDGPQFERL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LpaqqrMKGENW-----Y------RGTADAVTQNLDIIRryKAEYVVILaGDHI-YKQDYSRMLIDHVEKGARCTVACMP 169
Cdd:COG1209 65 L-----GDGSQLgikisYavqpepLGLAHAFIIAEDFIG--GDPVALVL-GDNIfYGDGLSELLREAAARESGATIFGYK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6SHJ_A 170 VpiEEASAFGVMAVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVFDADYLYEL--LEEDDRDE 234
Cdd:COG1209 137 V--EDPERYGVVEFDEDGRVVSLEEKPKEPKS-------NLAVTGLYFYDNDVVEIAknLKPSARGE 194
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
22-397 |
4.46e-20 |
|
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase
Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 90.92 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDL 101
Cdd:TIGR01208 2 ALILAAGKGTRLRPLTFTRPKQLIPVANK-PILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPaqqrmkgenwyRGTADAVTQNLDIIRryKAEYVVILaGDHIYKQDYSRMLIDHVEKGARCTVACMPVPieEASAFGVM 181
Cdd:TIGR01208 81 EP-----------LGLAHAVYTARDFLG--DDDFVVYL-GDNLIQDGISRFVKSFEEKDYDALILLTKVR--DPTAFGVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 182 AVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVFdADYLYEL---LEEDDRDENSShdfgKDLIPKITEAGlaYAHP 258
Cdd:TIGR01208 145 VLEDGKRILKLVEKPKEPPS-------NLAVVGLYMF-RPLIFEAiknIKPSWRGELEI----TDAIQWLIEKG--YKVG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 259 FPLscvqsdpdAEPYWRDVGTLEAYWKANLDLasvvpeLDMYDRNwpirtyneslppakfVQdrsgshGMTLNSLVSGGC 338
Cdd:TIGR01208 211 GSK--------VTGWWKDTGKPEDLLDANRLI------LDEVERE---------------VQ------GVDDESKIRGRV 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 339 VI-SGSVVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIG 397
Cdd:TIGR01208 256 VVgEGAKIVNSVIRGPAVIGEDCIIENSYIGPYTSIGEGVVIRDAEVEHSIVLDESVIEG 315
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
22-286 |
9.55e-16 |
|
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 76.10 E-value: 9.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQhiqrgwsffneEMNEFVDL 101
Cdd:cd06425 3 ALILVGGYGTRLRPLTLTVPKPLVEFCNK-PMIEHQIEALAKAGVKEIILAVNYRPEDMVP-----------FLKEYEKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRMKGENWYRGTADAVTQNLDIIRRYKAEYVViLAGDHIYKQDYSRMLIDHVEKGARCTVacMPVPIEEASAFGVM 181
Cdd:cd06425 71 LGIKITFSIETEPLGTAGPLALARDLLGDDDEPFFV-LNSDVICDFPLAELLDFHKKHGAEGTI--LVTKVEDPSKYGVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 182 AVDENDKIIE-FVEKPANPPSmpndpskSLASMGIYVFDADYLyelleedDRDENSSHDFGKDLIPKITEAGLAYAHPFP 260
Cdd:cd06425 148 VHDENTGRIErFVEKPKVFVG-------NKINAGIYILNPSVL-------DRIPLRPTSIEKEIFPKMASEGQLYAYELP 213
|
250 260
....*....|....*....|....*.
6SHJ_A 261 lscvqsdpdaePYWRDVGTLEAYWKA 286
Cdd:cd06425 214 -----------GFWMDIGQPKDFLKG 228
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
22-259 |
2.39e-15 |
|
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.
Pssm-ID: 133065 [Multi-domain] Cd Length: 223 Bit Score: 74.90 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGK-FriIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSF-----FNEEM 95
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRpF--LEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGgiriyYVIEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 96 nefvDLLpaqqrmkgenwyrGTADAVTQNLdiiRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPieEA 175
Cdd:cd06915 79 ----EPL-------------GTGGAIKNAL---PKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVP--DA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 176 SAFGVMAVDENDKIIEFVEKPAnppsmpnDPSKSLASMGIYVFDAdylyELLEEDDRDENSS-HDFGKDLIPKITEAGLA 254
Cdd:cd06915 137 SRYGNVTVDGDGRVIAFVEKGP-------GAAPGLINGGVYLLRK----EILAEIPADAFSLeADVLPALVKRGRLYGFE 205
|
....*
6SHJ_A 255 YAHPF 259
Cdd:cd06915 206 VDGYF 210
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
22-291 |
6.62e-15 |
|
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.
Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 74.49 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTnkRA----------KPavhfggkfrIIDFALSNCINSGIRRMGVITQYQSHTLVQH-------- 83
Cdd:cd02541 3 AVIPAAGLGTRFLPAT--KAipkemlpivdKP---------VIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHfdrsyele 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 84 ---IQRGWSFFNEEMNEFVDLLPAQQRMKGENwyRGTADAVTQNLDIIrryKAEYVVILAGDHIYKQDYSRM--LIDHVE 158
Cdd:cd02541 72 etlEKKGKTDLLEEVRIISDLANIHYVRQKEP--LGLGHAVLCAKPFI---GDEPFAVLLGDDLIDSKEPCLkqLIEAYE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 159 KGARCTVACMPVPIEEASAFGVMAVDEND----KIIEFVEKPA--NPPSmpndpskSLASMGIYVFDADyLYELLEEDDR 232
Cdd:cd02541 147 KTGASVIAVEEVPPEDVSKYGIVKGEKIDgdvfKVKGLVEKPKpeEAPS-------NLAIVGRYVLTPD-IFDILENTKP 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
6SHJ_A 233 DENsshdfGK----DLIPKITEAGLAYAHPFplscvqsdpdaEPYWRDVGTLEAYWKANLDLA 291
Cdd:cd02541 219 GKG-----GEiqltDAIAKLLEEEPVYAYVF-----------EGKRYDCGNKLGYLKATVEFA 265
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
22-283 |
1.77e-12 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 66.44 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFN----EEMNE 97
Cdd:cd06422 2 AMILAAGLGTRMRPLTDTRPKPLVPVAGK-PLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRFGLRitisDEPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 98 fvdLLpaqqrmkgenwyrGTADAVTQNLDIIRrykAEYVVILAGDHIYKQDYSRMLIDHVEKgARCTVACMP-VPIEEAS 176
Cdd:cd06422 81 ---LL-------------ETGGGIKKALPLLG---DEPFLVVNGDILWDGDLAPLLLLHAWR-MDALLLLLPlVRNPGHN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 177 AFGVMAVDENDKIIEFVEKPANPpsmpndpsksLASMGIYVFDAdylyELLEEDDRDENSSHDFGKDLIPKITEAGLAYA 256
Cdd:cd06422 141 GVGDFSLDADGRLRRGGGGAVAP----------FTFTGIQILSP----ELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYD 206
|
250 260
....*....|....*....|....*..
6SHJ_A 257 HpfplscvqsdpdaepYWRDVGTLEAY 283
Cdd:cd06422 207 G---------------LWFDVGTPERL 218
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
22-287 |
3.46e-12 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 65.65 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWS----FFN---EE 94
Cdd:COG1213 2 AVILAAGRGSRLGPLTDDIPKCLVEIGGK-TLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPdvtfVYNpdyDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 95 MNEFVDLLPAQQRMKGEnwyrgtadavtqnldiirrykaeyVVILAGDHIYKQDYSRMLIDHvekGARCTVAC---MPVP 171
Cdd:COG1213 81 TNNIYSLWLAREALDED------------------------FLLLNGDVVFDPAILKRLLAS---DGDIVLLVdrkWEKP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 172 IEEASAFgvmAVDENDKIIEFVEKPanppsmpnDPSKSLA-SMGIYVF---DADYLYELLEEDDRDENSSHDFGkDLIPK 247
Cdd:COG1213 134 LDEEVKV---RVDEDGRIVEIGKKL--------PPEEADGeYIGIFKFsaeGAAALREALEALIDEGGPNLYYE-DALQE 201
|
250 260 270 280
....*....|....*....|....*....|....*....|
6SHJ_A 248 ITEAGLAyAHPFPLSCVqsdpdaepYWRDVGTLEAYWKAN 287
Cdd:COG1213 202 LIDEGGP-VKAVDIGGL--------PWVEIDTPEDLERAE 232
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
24-287 |
6.50e-12 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 64.90 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 24 ILAGGRGTRLKDLT---NKRAKPAvhfgGKFRIIDFALSNCINSGIRRMGVITQyqshtlvqhiqrgwsffNEEMNEFVD 100
Cdd:cd02538 5 ILAGGSGTRLYPLTkvvSKQLLPV----YDKPMIYYPLSTLMLAGIREILIIST-----------------PEDLPLFKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 101 LLPaqqrmKGENW-----YR------GTADAVTQNLDIIRrykAEYVVILAGDHI-YKQDYSRMLIDHVEKGARCTVACM 168
Cdd:cd02538 64 LLG-----DGSDLgiritYAvqpkpgGLAQAFIIGEEFIG---DDPVCLILGDNIfYGQGLSPILQRAAAQKEGATVFGY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 169 PVPieEASAFGVMAVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVFDADYLyelleeddrdensshDFGKDLIP-- 246
Cdd:cd02538 136 EVN--DPERYGVVEFDENGRVLSIEEKPKKPKS-------NYAVTGLYFYDNDVF---------------EIAKQLKPsa 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
6SHJ_A 247 ----KITEAGLAYAHPFPLSCVQSDPDAepYWRDVGTLEAYWKAN 287
Cdd:cd02538 192 rgelEITDVNNEYLEKGKLSVELLGRGF--AWLDTGTHESLLEAS 234
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
22-248 |
2.84e-11 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 63.02 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWS---FFNE---EM 95
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGK-PLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNikfVYNPdyaET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 96 NEFVDLLPAQQRMKGEnwyrgtadavtqnldiirrykaeyVVILAGDHIYkqdYSRMLIDHVEKGARCTVACMPVPIEEA 175
Cdd:cd02523 80 NNIYSLYLARDFLDED------------------------FLLLEGDVVF---DPSILERLLSSPADNAILVDKKTKEWE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6SHJ_A 176 SAFGVmAVDENDKIIEFVEKPANppsmPNDPskSLASMGIYVF---DADYLYELLEEDDRDENSS---HDFGKDLIPKI 248
Cdd:cd02523 133 DEYVK-DLDDAGVLLGIISKAKN----LEEI--QGEYVGISKFspeDADRLAEALEELIEAGRVNlyyEDALQRLISEE 204
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
22-229 |
5.49e-10 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 59.07 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDltnKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQrgwsffnEEMNEFVdl 101
Cdd:cd02540 1 AVILAAGKGTRMKS---DLPKVLHPLAGK-PMLEHVLDAARALGPDRIVVVVGHGAEQVKKALA-------NPNVEFV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRmkgenwyrGTADAVTQNLDIIRRYkAEYVVILAGDH--IYKQDYSRMLIDHVEKGARCTV--ACMPVPieeaSA 177
Cdd:cd02540 68 LQEEQL--------GTGHAVKQALPALKDF-EGDVLVLYGDVplITPETLQRLLEAHREAGADVTVltAELEDP----TG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
6SHJ_A 178 FGVMAVDENDKIIEFVE-KPANPpsmpNDPSKSLASMGIYVFDADYLYELLEE 229
Cdd:cd02540 135 YGRIIRDGNGKVLRIVEeKDATE----EEKAIREVNAGIYAFDAEFLFEALPK 183
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
134-229 |
3.73e-09 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 57.35 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 134 EYVVILAGDHIYKQDYSRM--LIDHVEKGARCTVACMPVPIEEASAFGVMAVDEND----KIIEFVEKPAnppsmPND-P 206
Cdd:COG1210 123 EPFAVLLGDDLIDSEKPCLkqMIEVYEETGGSVIAVQEVPPEEVSKYGIVDGEEIEggvyRVTGLVEKPA-----PEEaP 197
|
90 100
....*....|....*....|...
6SHJ_A 207 SKsLASMGIYVFDADyLYELLEE 229
Cdd:COG1210 198 SN-LAIVGRYILTPE-IFDILEK 218
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
22-229 |
3.94e-08 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 55.03 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDltnkrAKPAV-H-FGGKFrIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQrgwsffneEMN-EF 98
Cdd:COG1207 5 VVILAAGKGTRMKS-----KLPKVlHpLAGKP-MLEHVLDAARALGPDRIVVVVGHGAEQVRAALA--------DLDvEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 99 VdlLPAQQrmkgenwyRGTADAVTQNLDIIRRYKaEYVVILAGDH--IYKQDYSRMLIDHVEKGARCTV--ACMPVPiee 174
Cdd:COG1207 71 V--LQEEQ--------LGTGHAVQQALPALPGDD-GTVLVLYGDVplIRAETLKALLAAHRAAGAAATVltAELDDP--- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 175 aSAFGVMAVDENDKIIEFVE-KPANPpsmpndpsKSLA----SMGIYVFDADYLYELLEE 229
Cdd:COG1207 137 -TGYGRIVRDEDGRVLRIVEeKDATE--------EQRAireiNTGIYAFDAAALREALPK 187
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
22-287 |
1.08e-07 |
|
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.
Pssm-ID: 133015 [Multi-domain] Cd Length: 253 Bit Score: 52.57 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGK---FRIID-FAlsnciNSGIRRMGVITQYQSHtlvqHIQRGWSFFNEEMNE 97
Cdd:cd02524 1 VVILAGGLGTRLSEETELKPKPMVEIGGRpilWHIMKiYS-----HYGHNDFILCLGYKGH----VIKEYFLNYFLHNSD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 98 F-VDLLPAQQRM---KGENW-----YRGTADAVTQNLDIIRRY--KAEYVVILAGDHIYKQDYsRMLID-HVEKGARCTV 165
Cdd:cd02524 72 VtIDLGTNRIELhnsDIEDWkvtlvDTGLNTMTGGRLKRVRRYlgDDETFMLTYGDGVSDVNI-NALIEfHRSHGKLATV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 166 ACMPVPieeaSAFGVMAVDENDKIIEFVEKPANPPSMPNDpskslasmGIYVFDADYLyELLEEDDRdensshDFGKDLI 245
Cdd:cd02524 151 TAVHPP----GRFGELDLDDDGQVTSFTEKPQGDGGWING--------GFFVLEPEVF-DYIDGDDT------VFEREPL 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
6SHJ_A 246 PKITEAG--LAYAHpfplscvqsdpdaEPYW------RDVGTLEAYWKAN 287
Cdd:cd02524 212 ERLAKDGelMAYKH-------------TGFWqcmdtlRDKQTLEELWNSG 248
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
22-197 |
9.19e-07 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 49.58 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGwSFFNEEMNEFVDL 101
Cdd:cd04198 3 AVILAGGGGSRLYPLTDNIPKALLPVANK-PMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRS-FPLNLKQKLDEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LPAQQRMkgenwyrGTADAvtqnLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEASAFG-- 179
Cdd:cd04198 81 IVLDEDM-------GTADS----LRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGkg 149
|
170 180
....*....|....*....|....*..
6SHJ_A 180 ---------VMAVDENDKIIEFVEKPA 197
Cdd:cd04198 150 kskkaderdVIGLDEKTQRLLFITSEE 176
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
11-404 |
1.04e-04 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 44.58 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 11 MLARQLPLKSValILAGGRGTRLKDLTNKRAKPAvhfGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQR-GWS 89
Cdd:PRK14358 1 MTEQTRPLDVV--ILAAGQGTRMKSALPKVLHPV---AGR-PMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGsGVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 90 FFNEEmnefvdllpaQQRMKGENWYRGTADAVTQNLDIIrrykaeyvvILAGDH-IYKQDYSRMLI-DHVEKGARCTVAC 167
Cdd:PRK14358 75 FARQE----------QQLGTGDAFLSGASALTEGDADIL---------VLYGDTpLLRPDTLRALVaDHRAQGSAMTILT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 168 MPVPieEASAFGVMAVDENDKIIEFVEKPANPPSmpndpSKSLASM--GIYVFDADyLYELLEEDDRDENSSHDFGKDLI 245
Cdd:PRK14358 136 GELP--DATGYGRIVRGADGAVERIVEQKDATDA-----EKAIGEFnsGVYVFDAR-APELARRIGNDNKAGEYYLTDLL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 246 pKITEAGLAYAHPFPLscvqSDPDAEPYWRD---VGTLEAYWKANLDLASVVPELDMYDrnwPIRTYNESlpPAKFVQDR 322
Cdd:PRK14358 208 -GLYRAGGAQVRAFKL----SDPDEVLGANDragLAQLEATLRRRINEAHMKAGVTLQD---PGTILIED--TVTLGRDV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 323 SGSHGMTL--NSLVSGGCVISG-SVVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRrcvidRACVIPEGMVIG-- 397
Cdd:PRK14358 278 TIEPGVLLrgQTRVADGVTIGAySVVTDSVLHEGAVIKPHSVLEGAEVGAGSDVGPFARLR-----PGTVLGEGVHIGnf 352
|
410
....*....|
6SHJ_A 398 ---ENAEEDA 404
Cdd:PRK14358 353 vetKNARLDA 362
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
22-221 |
1.71e-04 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 43.12 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKDLTNKRAKPAVHFGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDL 101
Cdd:PRK15480 6 GIILAGGSGTRLYPVTMAVSKQLLPIYDK-PMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 102 LP---AQQRMKGENWYRGTADAvtqnldiirrykaeyvvILAGDHI-YKQDYSRMLIDHVEKGARCTVacMPVPIEEASA 177
Cdd:PRK15480 85 SPdglAQAFIIGEEFIGGDDCA-----------------LVLGDNIfYGHDLPKLMEAAVNKESGATV--FAYHVNDPER 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
6SHJ_A 178 FGVMAVDENDKIIEFVEKPANPPSmpndpskSLASMGIYVFDAD 221
Cdd:PRK15480 146 YGVVEFDQNGTAISLEEKPLQPKS-------NYAVTGLYFYDND 182
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
331-392 |
3.74e-04 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 39.15 E-value: 3.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
6SHJ_A 331 NSLVSGGCVI-SGSVVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLR-RCVIDRACVIPE 392
Cdd:cd03356 16 NSVIGDNVRIgDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVnLCIIGDDVVVED 79
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
22-229 |
7.29e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 41.74 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 22 ALILAGGRGTRLKdltNKRAKpAVH-FGGKfRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIqrgwsffnEEMNEFVd 100
Cdd:PRK14354 5 AIILAAGKGTRMK---SKLPK-VLHkVCGK-PMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVL--------GDRSEFA- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 101 lLPAQQRmkgenwyrGTADAVTQNLDIIRRyKAEYVVILAGDH--IYKQDYSRMLIDHVEKGARCTV--ACMPVPieeaS 176
Cdd:PRK14354 71 -LQEEQL--------GTGHAVMQAEEFLAD-KEGTTLVICGDTplITAETLKNLIDFHEEHKAAATIltAIAENP----T 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
6SHJ_A 177 AFGVMAVDEND---KIIEfvEKPANPpsmpndpsKSLA----SMGIYVFDADYLYELLEE 229
Cdd:PRK14354 137 GYGRIIRNENGeveKIVE--QKDATE--------EEKQikeiNTGTYCFDNKALFEALKK 186
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
331-393 |
2.08e-03 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 36.79 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
6SHJ_A 331 NSLVSGGCVI-SGSVVVQSVLFSRVRVNSFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEG 393
Cdd:cd04652 16 RSVIGANCKIgKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAG 79
|
|
| |
