|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-602 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 946.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAELSAKTA--GVEGTTGIGHTRWATHGKP 78
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEeePLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 79 TEDNAHPHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAEEeGLSVLEAFKKALHIIRGSYA 157
Cdd:PRK00331 81 TERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAkGHVFKSETDTEVIAHLIEEELKE-GGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 158 FALIDSENPDVIYVAKNKSPLLIGLGEGYNMVCSDAMAMIRETNQYMEIHDQELVIVKADSVEVQDYDGNSRERASYTAE 237
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 238 LDLSDIGKGTYPYYMLKEIDEQPTVMRKLIQAYTDDAGQVVIDPAIIKavqDADRIYILAAGTSYHAGFASKKMLEELTD 317
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELGEGELADEDLK---KIDRIYIVACGTSYHAGLVAKYLIESLAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 318 TPVELGISSEWGYGMPLLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIAVA 397
Cdd:PRK00331 317 IPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 398 STKAYTAQIAALAFLAKAVGEANGN-AKAQAFDLVHELSIVAQSIESTLSEKETIEAKVRELLEtTRNAFYIGRGQDYYV 476
Cdd:PRK00331 397 STKAFTAQLAVLYLLALALAKARGTlSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFAD-ARNALFLGRGVDYPV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 477 AMEASLKLKEISYIQCEGFAAGELKHGTIALIEEGTPVLALLSDPVLANHTRGNIQEVAARGAKVLTIAEEN--VAKDTD 554
Cdd:PRK00331 476 ALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGdeVAEEAD 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 446256396 555 D-IVLTTVHPYLSPISMVVPTQLVAYFATLHRGLDVDKPRNLAKSVTVE 602
Cdd:PRK00331 556 DvIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-602 |
0e+00 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 888.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAELSAKTAG--VEGTTGIGHTRWATHGKP 78
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEepLSGTIGIGHTRWATHGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 79 TEDNAHPHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAEEeGLSVLEAFKKALHIIRGSYA 157
Cdd:COG0449 81 SDENAHPHTSCSGRIAVVHNGIIENYAELREELEAkGHTFKSETDTEVIAHLIEEYLKG-GGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 158 FALIDSENPDVIYVAKNKSPLLIGLGEGYNMVCSDAMAMIRETNQYMEIHDQELVIVKADSVEVQDYDGNSRERASYTAE 237
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 238 LDLSDIGKGTYPYYMLKEIDEQPTVMRKLIQAYTDDAGQVVID--PAIIKAVQDADRIYILAAGTSYHAGFASKKMLEEL 315
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDelNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 316 TDTPVELGISSEWGYGMPLLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIA 395
Cdd:COG0449 320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 396 VASTKAYTAQIAALAFLAKAVGEANGN-AKAQAFDLVHELSIVAQSIESTLSEKETIEAKVRELLEtTRNAFYIGRGQDY 474
Cdd:COG0449 400 VASTKAFTTQLAALYLLALYLARARGTlSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYAD-ARNALFLGRGINY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 475 YVAMEASLKLKEISYIQCEGFAAGELKHGTIALIEEGTPVLALLSDPVLANHTRGNIQEVAARGAKVLTIAEEN---VAK 551
Cdd:COG0449 479 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGdeeVEE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 446256396 552 DTDD-IVLTTVHPYLSPISMVVPTQLVAYFATLHRGLDVDKPRNLAKSVTVE 602
Cdd:COG0449 559 LADDvIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-602 |
0e+00 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 738.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 2 CGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAELSAKT--AGVEGTTGIGHTRWATHGKPT 79
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLgeKPLPGGVGIGHTRWATHGKPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 80 EDNAHPHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAEEEGlSVLEAFKKALHIIRGSYAF 158
Cdd:TIGR01135 81 DENAHPHTDEGGRIAVVHNGIIENYAELREELEArGHVFSSDTDTEVIAHLIEEELREGG-DLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 159 ALIDSENPDVIYVAKNKSPLLIGLGEGYNMVCSDAMAMIRETNQYMEIHDQELVIVKADSVEVQDYDGNSRERASYTAEL 238
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 239 DLSDIGKGTYPYYMLKEIDEQPTVMRKLIQAYTDDAGQVVIDPAIIKAVQDADRIYILAAGTSYHAGFASKKMLEELTDT 318
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNIDRIQIVACGTSYHAGLVAKYLIERLAGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 319 PVELGISSEWGYGMPLLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIAVAS 398
Cdd:TIGR01135 320 PVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 399 TKAYTAQIAALAFLAKAVGEANGNAKAQ-AFDLVHELSIVAQSIESTLSEKETIEAkVRELLETTRNAFYIGRGQDYYVA 477
Cdd:TIGR01135 400 TKAFTTQLTVLYLLALALAKARGTLSAEeEAELVDALRRLPDLVEQVLLADESIAE-LAERYADKRNFLFLGRGLGYPIA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 478 MEASLKLKEISYIQCEGFAAGELKHGTIALIEEGTPVLALLSDPVLANHTRGNIQEVAARGAKVLTIAE---ENVAKDTD 554
Cdd:TIGR01135 479 LEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPeddETIASVAD 558
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 446256396 555 D-IVLTTVHPYLSPISMVVPTQLVAYFATLHRGLDVDKPRNLAKSVTVE 602
Cdd:TIGR01135 559 DvIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-601 |
5.15e-145 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 434.06 E-value: 5.15e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVLDgADNHLVkaVGRIAELSAKTAGVE------------GTTGIG 68
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTIS-SGGELK--TTKYASDGTTSDSIEilkeklldshknSTIGIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 69 HTRWATHGKPTEDNAHPHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAeEEGLSVLEAFKK 147
Cdd:PTZ00295 101 HTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAkGIKFRSETDSEVIANLIGLEL-DQGEDFQEAVKS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 148 ALHIIRGSYAFALIDSENPDVIYVAKNKSPLLIGLGEGYNMVCSDAMAMIRETNQYMEIHDQELVIVKADSVEvQDYDGN 227
Cdd:PTZ00295 180 AISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVN-DLYTQR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 228 SRER-ASYTAELDlsdigKGTYPYYMLKEIDEQP-TVMRKLIQA--YTDDAGQVVI--DPAIIKAVQDADRIYILAAGTS 301
Cdd:PTZ00295 259 RVEKiPEEVIEKS-----PEPYPHWTLKEIFEQPiALSRALNNGgrLSGYNNRVKLggLDQYLEELLNIKNLILVGCGTS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 302 YHAGFASKKMLEEL-------TDTPVELGIssewgYGMPllSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVP 374
Cdd:PTZ00295 334 YYAALFAASIMQKLkcfntvqVIDASELTL-----YRLP--DEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 375 GSTLSREANYTMLLHAGPEIAVASTKAYTAQIAAL----AFLAKAVGEANGNAKAQAfdLVHELSIVAQSIESTLSEKET 450
Cdd:PTZ00295 407 GSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLsliaLWFAQNKEYSCSNYKCSS--LINSLHRLPTYIGMTLKSCEE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 451 IEAKVRELLETTRNAFYIGRGQDYYVAMEASLKLKEISYIQCEGFAAGELKHGTIALI--EEGTPVLALLSDPVLANHTR 528
Cdd:PTZ00295 485 QCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIdkEKNTPVILIILDDEHKELMI 564
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446256396 529 GNIQEVAARGAKVLTIA-EENVAKD-TDDIVLTTVHPYLSPISMVVPTQLVAYFATLHRGLDVDKPRNLAKSVTV 601
Cdd:PTZ00295 565 NAAEQVKARGAYIIVITdDEDLVKDfADEIILIPSNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-602 |
4.12e-124 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 381.41 E-value: 4.12e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVgNTNAT-------DILIQGLEKLEYRGYDSAGIFVLDGADNH-----LVKAVGRIAELsAKTAGVEGTT--- 65
Cdd:PLN02981 1 MCGIFAYL-NYNVPrerrfilEVLFNGLRRLEYRGYDSAGIAIDNDPSLEsssplVFREEGKIESL-VRSVYEEVAEtdl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 66 ----------GIGHTRWATHGKPTEDNAHPHRSETE-RFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEI----AVHL 129
Cdd:PLN02981 79 nldlvfenhaGIAHTRWATHGPPAPRNSHPQSSGPGnEFLVVHNGIITNYEVLKETLLRhGFTFESDTDTEVipklAKFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 130 IGKFAEEEGLS-----VLEAFKKalhiIRGSYAFALIDSENPDVIYVAKNKSPLLIG---LGEGYN-------------- 187
Cdd:PLN02981 159 FDKLNEEEGDVtfsqvVMEVMRQ----LEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltkn 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 188 -------MVCSDAMAMIRETNQYMEIHDQELV--------IVKADSVEVQDYDGNSR----ERASYTAELDLSDIGKGTY 248
Cdd:PLN02981 235 rdkpkefFLASDASAVVEHTKRVLVIEDNEVVhlkdggvgIYKFENEKGRGGGGLSRpasvERALSTLEMEVEQIMKGNY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 249 PYYMLKEIDEQP----TVMR-KLIQAYTDDAGQVVIDPAI--IKAVQDADRIYILAAGTSYHAGFASKKMLEELTDTPVE 321
Cdd:PLN02981 315 DHYMQKEIHEQPesltTTMRgRLIRGGSGKAKRVLLGGLKdhLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 322 LGISSEwgygmpLLSKK-PLF-----IFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIA 395
Cdd:PLN02981 395 MELASD------LLDRQgPIYredtaVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIG 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 396 VASTKAYTAQIAALAFLAKAVGEANGNAKAQAFDLVHELSIVAQSIESTLSeketIEAKVRELLETTRNA---FYIGRGQ 472
Cdd:PLN02981 469 VASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLK----LDQEMKELAELLIDEqslLVFGRGY 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 473 DYYVAMEASLKLKEISYIQCEGFAAGELKHGTIALIEEGTPVLALLSDPVLANHTRGNIQEVAARGAKVLTIAEENVA-- 550
Cdd:PLN02981 545 NYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDAss 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 446256396 551 ----KDTDDIVLTTVHPYLSPISMVVPTQLVAYFATLHRGLDVDKPRNLAKSVTVE 602
Cdd:PLN02981 625 vcpsGGCRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-602 |
7.69e-113 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 351.87 E-value: 7.69e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVG-NTNAT-----DILIQGLEKLEYRGYDSAGIFV--------LDGADNH-------LVKAVGRIAELSAKT- 58
Cdd:PTZ00394 1 MCGIFGYANhNVPRTveqilNVLLDGIQKVEYRGYDSAGLAIdanigsekEDGTAASaptprpcVVRSVGNISQLREKVf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 59 ------------AGVEGTTGIGHTRWATHGKPTEDNAHPHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTE- 124
Cdd:PTZ00394 81 seavaatlppmdATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEeGYHFSSDTDTEv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 125 IAVHLIGKFAEEEGLSVLEAFKKALHIIRGSYAFALIDSENPDVIYVAKNKSPLLIGLGEGYNMVC-------------- 190
Cdd:PTZ00394 161 ISVLSEYLYTRKGIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRRTDDRGCvmklqtydltdlsg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 191 -------SDAMAMIRETNQYMEIHDQELVIVKADSVEVQDYDGNSR---ERASYTAELDLSDIGKGTYPYYMLKEIDEQP 260
Cdd:PTZ00394 241 plevffsSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRsivKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 261 ----TVMRKLIQAYTDDAGQVVIDPAIIKAVQDADRIYILAAGTSYHAGFASKKMLEELTDTPVELGISSEWGYGMPLLS 336
Cdd:PTZ00394 321 esviSSMHGRIDFSSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 337 KKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIAVASTKAYTAQIAALAFLAKAV 416
Cdd:PTZ00394 401 RDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 417 GEANGNAKAQAFDLVHELSIVAQSIESTLSEKETIEAKVRELLETTRNAFYIGRGQDYYVAMEASLKLKEISYIQCEGFA 496
Cdd:PTZ00394 481 SSDSVRLQERRNEIIRGLAELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIH 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 497 AGELKHGTIALIEEGTPVLALLSDPVLANHTRGNIQEVAARGAKVLTIAEEN----VAKDTDDIVLTTVHPYLSPISMVV 572
Cdd:PTZ00394 561 SGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVdaelKAAASEIVLVPKTVDCLQCVVNVI 640
|
650 660 670
....*....|....*....|....*....|
gi 446256396 573 PTQLVAYFATLHRGLDVDKPRNLAKSVTVE 602
Cdd:PTZ00394 641 PFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-214 |
8.91e-101 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 304.75 E-value: 8.91e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 2 CGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAELSAKTAG--VEGTTGIGHTRWATHGKPT 79
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEkpLSGHVGIGHTRWATHGEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 80 EDNAHPHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAeEEGLSVLEAFKKALHIIRGSYAF 158
Cdd:cd00714 81 DVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAkGYKFESETDTEVIAHLIEYYY-DGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446256396 159 ALIDSENPDVIYVAKNKSPLLIGLGEGYNMVCSDAMAMIRETNQYMEIHDQELVIV 214
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
253-602 |
5.51e-74 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 239.80 E-value: 5.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 253 LKEIDEQPTVMRKLIQAYTDDAGQVVidpAIIKAvQDADRIYILAAGTSYHAGFASKKMLEELTDTPVELGISSEW-GYG 331
Cdd:COG2222 1 AREIAQQPEAWRRALAALAAAIAALL---ARLRA-KPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVYP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 332 MPLLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIAVASTKAYTAQIAALAF 411
Cdd:COG2222 77 AYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 412 LAKAVGEANgnakaqafDLVHELSIVAQSIESTLSEKETIEAKVRelLETTRNAFYIGRGQDYYVAMEASLKLKEISYIQ 491
Cdd:COG2222 157 LLAAWGGDD--------ALLAALDALPAALEAALAADWPAAALAA--LADAERVVFLGRGPLYGLAREAALKLKELSAGH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 492 CEGFAAGELKHGTIALIEEGTPVLALLSDPVLANHTRGNIQEVAARGAKVLTIAEENVAKDTDDiVLTTVHPYLSPISMV 571
Cdd:COG2222 227 AEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLP-AIPDLHDALDPLLLL 305
|
330 340 350
....*....|....*....|....*....|.
gi 446256396 572 VPTQLVAYFATLHRGLDVDKPRNLAKSVTVE 602
Cdd:COG2222 306 VVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-203 |
3.05e-56 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 189.20 E-value: 3.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 2 CGIVGVVGNTNATDILI----QGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAELSA--KTAGVEGTTGIGHTRWATH 75
Cdd:cd00352 1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALdlLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 76 GKPTEDNAHPHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAEEEGLsvLEAFKKALHIIRG 154
Cdd:cd00352 81 GLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEArGYRFEGESDSEVILHLLERLGREGGL--FEAVEDALKRLDG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446256396 155 SYAFALIDsENPDVIYVAKN---KSPLLIGLG-EGYNMVCSDAMAMIRETNQY 203
Cdd:cd00352 159 PFAFALWD-GKPDRLFAARDrfgIRPLYYGITkDGGLVFASEPKALLALPFKG 210
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
454-600 |
4.17e-52 |
|
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240142 [Multi-domain] Cd Length: 153 Bit Score: 175.53 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 454 KVRELLETTRNAFYIGRGQDYYVAMEASLKLKEISYIQCEGFAAGELKHGTIALIEEGTPVLALLSDPVLANHTRGNIQE 533
Cdd:cd05009 5 ELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLIKE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446256396 534 VAARGAKVLTIAEENVAKDTDDIVLT--TVHPYLSPISMVVPTQLVAYFATLHRGLDVDKPRNLAKSVT 600
Cdd:cd05009 85 VKARGAKVIVITDDGDAKDLADVVIRvpATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
292-413 |
3.12e-48 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 164.21 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 292 RIYILAAGTSYHAGFASKKMLEELTDTPVELGISSEWGYGMPLLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVT 371
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446256396 372 NVPGSTLSREANYTMLLHAGPEIAVASTKAYTAQIAALAFLA 413
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLA 122
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-191 |
3.36e-37 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 144.01 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAEL--SAKTAGVEGTTGIGHTRWATHGKP 78
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVfdEEDLERLKGNIAIGHVRYSTTGSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 79 TEDNAHPH--RSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKfaEEEGLSVLEAFKKALHIIRGS 155
Cdd:COG0034 87 SLENAQPFyvNSPFGSIALAHNGNLTNAEELREELEEeGAIFQTTSDTEVILHLIAR--ELTKEDLEEAIKEALRRVKGA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446256396 156 YAFALIDsenPDVIYVAKNKS---PLLIG-LGEGYnMVCS 191
Cdd:COG0034 165 YSLVILT---GDGLIAARDPNgirPLVLGkLEDGY-VVAS 200
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-191 |
7.98e-31 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 121.03 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 2 CGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAEL--SAKTAGVEGTTGIGHTRWATHGKPT 79
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVfdEEKLRRLPGNIAIGHVRYSTAGSSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 80 EDNAHPHRSETER--FVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAEEEGLsvLEAFKKALHIIRGSY 156
Cdd:cd00715 81 LENAQPFVVNSPLggIALAHNGNLVNAKELREELEEeGRIFQTTSDSEVILHLIARSLAKDDL--FEAIIDALERVKGAY 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 446256396 157 AFALIdseNPDVIYVAKNKS---PLLIG-LGEGYNMVCS 191
Cdd:cd00715 159 SLVIM---TADGLIAVRDPHgirPLVLGkLEGDGYVVAS 194
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
289-415 |
1.57e-27 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 107.77 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 289 DADRIYILAAGTSYHAGFASKKMLEELTDTPVELGISSEWGYG-MPLLSKKPLFIFISQSGETADSRQVLVKANEMGIPS 367
Cdd:pfam01380 4 KAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKI 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446256396 368 LTVTNVPGSTLSREANYTMLLHAGPEIAVASTKAYTAQIAALAFLAKA 415
Cdd:pfam01380 84 IAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-196 |
3.38e-23 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 102.80 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 2 CGIVGVVGNTN--ATDILIQGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAEL--SAKTAGVEGTTGIGHTRWATHGK 77
Cdd:PRK05793 15 CGVFGVFSKNNidVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVfsKEKLKGLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 78 PTEDNAHP--HRSETERFVLVHNGVIENYLEIKEEY-LAGHHFKGQTDTEIAVHLIGKFAEEeglSVLEAFKKALHIIRG 154
Cdd:PRK05793 95 SDLDNAQPlvANYKLGSIAIAHNGNLVNADVIRELLeDGGRIFQTSIDSEVILNLIARSAKK---GLEKALVDAIQAIKG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446256396 155 SYAFA------LIDSENPDVIyvaknkSPLLIG-LGEGYnMVCSDAMAM 196
Cdd:PRK05793 172 SYALViltedkLIGVRDPHGI------RPLCLGkLGDDY-ILSSESCAL 213
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
61-164 |
1.08e-21 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 90.83 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 61 VEGTTGIGHTRWATHGkPTEDNAHPHRSETERFVLVHNGVIENYLEIKEEY-LAGHHFKGQTDTEIAVHLigkfAEEEGL 139
Cdd:pfam13522 8 VEGGVALGHVRLAIVD-LPDAGNQPMLSRDGRLVLVHNGEIYNYGELREELaDLGHAFRSRSDTEVLLAL----YEEWGE 82
|
90 100
....*....|....*....|....*
gi 446256396 140 SVLEAFkkalhiiRGSYAFALIDSE 164
Cdd:pfam13522 83 DCLERL-------RGMFAFAIWDRR 100
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-157 |
1.19e-20 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 95.13 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVLDGADNHLVKAVGRIAEL--SAKTAGVEGTTGIGHTRWATHGKP 78
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVfdESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 79 TEDNAHPhrseterFV---------LVHNGVIENYLEIKEEY-LAGHHFKGQTDTEIAVHLIgkfAEEEGLSVLEAFKKA 148
Cdd:PLN02440 81 SLKNVQP-------FVanyrfgsigVAHNGNLVNYEELRAKLeENGSIFNTSSDTEVLLHLI---AISKARPFFSRIVDA 150
|
....*....
gi 446256396 149 LHIIRGSYA 157
Cdd:PLN02440 151 CEKLKGAYS 159
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-165 |
2.67e-20 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 94.52 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTNATD--ILIQGLEKLEYRGYDSAGIFVLDGAdnhlvkavgriaelsaktagvegttGIGHTRWAThgKP 78
Cdd:COG0367 1 MCGIAGIIDFDGGADreVLERMLDALAHRGPDGSGIWVDGGV-------------------------ALGHRRLSI--ID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 79 TEDNAH-PHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIgkfaEEEGLSVLEAFkkalhiiRGSY 156
Cdd:COG0367 54 LSEGGHqPMVSEDGRYVLVFNGEIYNYRELRAELEAlGHRFRTHSDTEVILHAY----EEWGEDCLERL-------NGMF 122
|
....*....
gi 446256396 157 AFALIDSEN 165
Cdd:COG0367 123 AFAIWDRRE 131
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-165 |
3.08e-20 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 89.54 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 2 CGIVGVV---GNTNATDILIQGLEKLEYRGYDSAGIFVLDGAdnhlvkavgriaelsaktagvegttGIGHTRWATHGkp 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWIDEGV-------------------------ALGHRRLSIID-- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 79 tEDNAH-PHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAEEeglsvleafkkALHIIRGSY 156
Cdd:cd00712 54 -LSGGAqPMVSEDGRLVLVFNGEIYNYRELRAELEAlGHRFRTHSDTEVILHLYEEWGED-----------CLERLNGMF 121
|
....*....
gi 446256396 157 AFALIDSEN 165
Cdd:cd00712 122 AFALWDKRK 130
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
86-169 |
3.99e-17 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 77.56 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 86 HRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLigkFAEEEGLSVLEAFkkalhiiRGSYAFALIDSE 164
Cdd:pfam13537 17 VSSEDGRYVIVFNGEIYNYRELRAELEAkGYRFRTHSDTEVILHL---YEAEWGEDCVDRL-------NGMFAFAIWDRR 86
|
....*
gi 446256396 165 NPDVI 169
Cdd:pfam13537 87 RQRLF 91
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
463-585 |
6.36e-17 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 77.34 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 463 RNAFYIGRGQDYYVAMEASLKLKEISYIQCEGFAAGELKHGTIALIEEGTPVLALLSDPVLANHTRgNIQEVAARGAKVL 542
Cdd:pfam01380 6 KRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARGAKII 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446256396 543 TI---AEENVAKDTDDIVLTTVHP-YLSPISMVVPTQLVAYFATLHR 585
Cdd:pfam01380 85 AItdsPGSPLAREADHVLYINAGPeTGVASTKSITAQLAALDALAVA 131
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-205 |
2.01e-14 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 76.10 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTNATDILIQ----GLEKLEYRGYDSAGIFVLDGAdnhlvkavgriaelsaktagvegttGIGHTRWATHG 76
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKkaleMSRLMRHRGPDWSGIYASDNA-------------------------ILGHERLSIVD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 77 kpTEDNAHPHRSETERFVLVHNGVIENYLEIKEEYLAGHHFKGQTDTEIAVHLIgkfaEEEGLSVLEAfkkalhiIRGSY 156
Cdd:PRK09431 56 --VNGGAQPLYNEDGTHVLAVNGEIYNHQELRAELGDKYAFQTGSDCEVILALY----QEKGPDFLDD-------LDGMF 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446256396 157 AFALIDSENPDVIyVAKNK---SPLLIGL-GEGYNMVCSDAMAMIRETNQYME 205
Cdd:PRK09431 123 AFALYDSEKDAYL-IARDPigiIPLYYGYdEHGNLYFASEMKALVPVCKTIKE 174
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-200 |
2.29e-14 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 73.07 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 2 CGIVGVV---GNTNATDILIQGLEKLEYRG-YDSAG--IFVLDGA-------DNHLVKAVGRIAELSA--KTAGVEGTTG 66
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGfaLYGDPDAfvyssgkDMEVFKGVGYPEDIARryDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 67 IGHTRWATHGKPTEDNAHPHRSETErfVLVHNGVIENYLEIKEE-YLAGHHFKGQTDTEIAVHLI------GKFAEEEGL 139
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPFSIGDI--AVVHNGEISNYGSNREYlERFGYKFETETDTEVIAYYLdlllrkGGLPLEYYK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446256396 140 SVL---EAFKKALHIIRGSYAFALIDSEN------PDVIYVAKNKS---PLLIGLGEGYNMVCSDAMAmIRET 200
Cdd:cd01907 159 HIIrmpEEERELLLALRLTYRLADLDGPFtiivgtPDGFIVIRDRIklrPAVVAETDDYVAIASEECA-IREI 230
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
241-434 |
4.25e-14 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 73.04 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 241 SDIGKGTYPYYMLKEI---DEQPTVMRKLIQAYTDDAGQV--VIDPA----IIKAVQDADRIYILAAGTSYH-AGFASKK 310
Cdd:COG1737 76 QELAEGLSSYERLRRLspdDSLEDILAKVLEAEIANLEETleLLDEEalerAVDLLAKARRIYIFGVGASAPvAEDLAYK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 311 MLeeLTDTPVEL--GISSEWGYGMPLLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLL 388
Cdd:COG1737 156 LL--RLGKNVVLldGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYV 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446256396 389 HA-GPEIAVASTKAYTAQIAALAFLAKAVGEANGNAKAQAFDLVHEL 434
Cdd:COG1737 234 PSeEPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEAL 280
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
61-164 |
1.36e-11 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 64.99 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 61 VEGTTGIGHTRWATHGKPTEDNAHPHRSetERFVLVHNGVIENYLEIKEEYLAG------HHFKGQTDTEIAVHLIGKFA 134
Cdd:COG0121 74 IKSRLVIAHVRKATVGPVSLENTHPFRG--GRWLFAHNGQLDGFDRLRRRLAEElpdelyFQPVGTTDSELAFALLLSRL 151
|
90 100 110
....*....|....*....|....*....|....*.
gi 446256396 135 EEEGLSVLEAFKKALHIIR------GSYAFALIDSE 164
Cdd:COG0121 152 RDGGPDPAEALAEALRELAelarapGRLNLLLSDGE 187
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
64-164 |
6.21e-11 |
|
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238889 [Multi-domain] Cd Length: 257 Bit Score: 63.18 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 64 TTGIGHTRWATHGKPTEDNAHPHRseTERFVLVHNGVIENYLEIKEEYLAG--HHFKGQTDTEIAVHLIGKFAEEEGLSV 141
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFT--RGRWLFAHNGQLDGFRLLRRRLLRLlpRLPVGTTDSELAFALLLSRLLERDPLD 158
|
90 100 110
....*....|....*....|....*....|..
gi 446256396 142 LEAFKKALH---------IIRGSYAFALIDSE 164
Cdd:cd01908 159 PAELLDAILqtlrelaalAPPGRLNLLLSDGE 190
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
282-412 |
1.00e-10 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 59.94 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 282 AIIKAVQDADRIYILAAGTSYH-AGFASKKML------EELTDTPVELGISSewgygmpLLSKKPLFIFISQSGETADSR 354
Cdd:cd05013 5 KAVDLLAKARRIYIFGVGSSGLvAEYLAYKLLrlgkpvVLLSDPHLQLMSAA-------NLTPGDVVIAISFSGETKETV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446256396 355 QVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIAVAStkAYTAQIAALAFL 412
Cdd:cd05013 78 EAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSS--AFSSRIAQLALI 133
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-165 |
1.57e-08 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 57.42 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTNATDILIQ-GLE---KLEYRGYDSAGIFVLDGADnhlvkavgriaelsaktagvEGTTGIGHTRWATHG 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRkALElskRLRHRGPDWSGIIVLENSP--------------------GTYNILAHERLAIVD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 77 kpTEDNAHPHRSETERFVLVHNGVIENYLEIKEEYLA-GHHFKGQTDTEIAVHLIGKFAEEEGLSVLEafkkalhiirGS 155
Cdd:PTZ00077 61 --LSDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKeGYKFSSNSDCEIIGHLYKEYGPKDFWNHLD----------GM 128
|
170
....*....|
gi 446256396 156 YAFALIDSEN 165
Cdd:PTZ00077 129 FATVIYDMKT 138
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
288-593 |
2.07e-07 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 53.08 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 288 QDADRIYILAAGTSYHAGFASKKMLEELTDTPVELGISSEWGYGMPL-LSKKPLFIFISQSGETADSRQVLVKANEMGIP 366
Cdd:PRK11382 42 RDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYrLDDRCAVIGVSDYGKTEEVIKALELGRACGAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 367 SLTVTNVPGSTLSREANYTMLLHAGPEIAVASTKAYTAQIAALAFLAkavgeangnAKAQAFDLVHELSIVAQSIESTLs 446
Cdd:PRK11382 122 TAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLA---------PNAEIGKIKNDLKQLPNALGHLV- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 447 ekETIEAKVRELLETTRNAFYIgrgqdYYVAM---------EASLKLKEISYIQCEGFAAGELKHGTIALIEEGTPVLAL 517
Cdd:PRK11382 192 --RTWEEKGRQLGELASQWPMI-----YTVAAgplrplgykEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFL 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446256396 518 LSDPVLANHTRGNIQEVAARGAKVLTIAEENVAKDtddivlttVHPYLSPISMVVPTQLVAYFATLHRGLDVDKPR 593
Cdd:PRK11382 265 LGNDESRHTTERAINFVKQRTDNVIVIDYAEISQG--------LHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-185 |
5.73e-07 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 52.46 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 1 MCGIVGVVGNTN---ATDILIQGLEK-LEYRGYDSAGIFVldGADNHLVkavgriaelsaktagvegttgigHTRWATHG 76
Cdd:PLN02549 1 MCGILAVLGCSDdsqAKRSRVLELSRrLRHRGPDWSGLYG--NEDCYLA-----------------------HERLAIMD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 77 KPTEDnaHPHRSETERFVLVHNGVIENYLEIKEEYlAGHHFKGQTDTEIAVHLIGKFAEEeglsvleaFKKALhiiRGSY 156
Cdd:PLN02549 56 PESGD--QPLYNEDKTIVVTANGEIYNHKELREKL-KLHKFRTGSDCEVIAHLYEEHGEE--------FVDML---DGMF 121
|
170 180 190
....*....|....*....|....*....|..
gi 446256396 157 AFALIDSENpDVIYVAKN---KSPLLIGLGEG 185
Cdd:PLN02549 122 SFVLLDTRD-NSFIAARDhigITPLYIGWGLD 152
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
292-384 |
3.59e-06 |
|
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240214 [Multi-domain] Cd Length: 120 Bit Score: 46.42 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 292 RIYILAAGTSYHAGFASKKMLEELTDTPVELGISSEWGY-GMPLLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTV 370
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHtGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|....
gi 446256396 371 TNVPGSTLSREANY 384
Cdd:cd05710 81 TDDEDSPLAKLADY 94
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
334-413 |
9.61e-05 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 42.53 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 334 LLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPE------IAVASTkayTAQIA 407
Cdd:cd05014 44 MVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEacplglAPTTST---TAMLA 120
|
....*.
gi 446256396 408 ALAFLA 413
Cdd:cd05014 121 LGDALA 126
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
283-390 |
1.62e-04 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 42.95 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 283 IIKAVQDADRIYILAAGTSyhaGFASKKMLEELTdtpvELGISSEWGYGM--PLLSKKPLFIFISQSGETADSRQVLVKA 360
Cdd:cd05005 26 LISAILNAKRIFVYGAGRS---GLVAKAFAMRLM----HLGLNVYVVGETttPAIGPGDLLIAISGSGETSSVVNAAEKA 98
|
90 100 110
....*....|....*....|....*....|
gi 446256396 361 NEMGIPSLTVTNVPGSTLSREANYTMLLHA 390
Cdd:cd05005 99 KKAGAKVVLITSNPDSPLAKLADVVVVIPA 128
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
477-592 |
2.60e-04 |
|
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli. It is similar to the glucosamine-6-phosphate synthases (GlmS) which catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source.
Pssm-ID: 240143 [Multi-domain] Cd Length: 151 Bit Score: 41.84 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 477 AMEASLKLKEISYIQCEGFA--AGELKHGTIALIEEGTPVLALLS-DPVLANHTRGNIQEVAARG--AKVLTIAEEN--V 549
Cdd:cd05010 13 AREAALKVLELTAGKVATVYdsPLGFRHGPKSLVDDDTLVVVFVSnDPYTRQYDLDLLKELRRDGiaARVIAISPESdaG 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446256396 550 AKDTDDIVLTTVH----PYLSPIsMVVPTQLVAYFATLHRGLDVDKP 592
Cdd:cd05010 93 IEDNSHYYLPGSRdlddVYLAFP-YILYAQLFALFNSIALGLTPDNP 138
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
331-410 |
2.90e-04 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 43.43 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 331 GMplLSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPE------IAVASTkayTA 404
Cdd:COG0794 87 GM--ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREacplnlAPTTST---TA 161
|
....*....
gi 446256396 405 QIA---ALA 410
Cdd:COG0794 162 TLAlgdALA 170
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
466-546 |
3.86e-04 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 39.66 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 466 FYIGRGQDYYVAMEASLKLKEISYIQCEGFAAGELKHG-TIALIEEGTPVLALLSDPVLANHTRGnIQEVAARGAKVLTI 544
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHAsLLSLLRKGDVVIALSYSGRTEELLAA-LEIAKELGIPVIAI 80
|
..
gi 446256396 545 AE 546
Cdd:cd04795 81 TD 82
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
335-409 |
8.34e-04 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 41.35 E-value: 8.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446256396 335 LSKKPLFIFISQSGETADSRQVLVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIAVAST--KAYTAQIAAL 409
Cdd:cd05007 116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQKLAL 192
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
357-409 |
1.74e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 40.54 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446256396 357 LVKANEMGIPSLTVTNVPGSTLSREANYTMLLHAGPEIAVAST--KAYTAQIAAL 409
Cdd:PRK05441 151 LEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVL 205
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
50-136 |
7.28e-03 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 38.85 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446256396 50 RIAELsAKTAGVEGTTGIGHTRWATHGKPTEDNAHPH-RSETER-FVLVHNGVIENYleikEEYLAG-HHFKGQTDTEIA 126
Cdd:pfam13230 59 PIAEL-VRRYPIRSRNVIAHIRKATQGRVTLENTHPFmRELWGRyWIFAHNGDLKGY----APKLSGrFQPVGSTDSELA 133
|
90
....*....|.
gi 446256396 127 V-HLIGKFAEE 136
Cdd:pfam13230 134 FcWLLDRLASR 144
|
|
| |
