|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-682 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 950.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDgNNHEVKERHIQLVKKRGKVKALDEELYK---QDSMD 77
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID-NDPSLESSSPLVFREEGKIESLVRSVYEevaETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 78 LKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVF 157
Cdd:PLN02981 80 LDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 158 D--NRETEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVrskyKLSTEQipilyrtctlenvknic 235
Cdd:PLN02981 160 DklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGV----KELPEE----------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 236 KTRMKRLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVK----RSASDDP-----SRA 306
Cdd:PLN02981 219 KNSSAVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFEnekgRGGGGLSrpasvERA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 307 IQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRV----NFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAA 382
Cdd:PLN02981 299 LSTLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 383 VATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCG 462
Cdd:PLN02981 379 LAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 463 VHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLL 542
Cdd:PLN02981 459 VHINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 543 VMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCS 622
Cdd:PLN02981 539 VFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICS 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826742 623 KDDtESSKFAYKT---IELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:PLN02981 619 KGD-ASSVCPSGGcrvIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-682 |
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: 784.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYMnyrvprTRKEIFETLIKGLQRLEYRGYDSAGVAIdgnnheVKERHIQLVKKRGKVKALDEELYKQDsmdlkv 80
Cdd:COG0449 1 MCGIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAV------LDDGGLEVRKAVGKLANLEEKLAEEP------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 81 eFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDnr 160
Cdd:COG0449 63 -LSGTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLK-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 161 etEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVrskyklsteqipilyrtctlenvknicktrmk 240
Cdd:COG0449 139 --GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL-------------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 241 rldssaclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSASDdpsRAIQTLQMELQQIMKG 320
Cdd:COG0449 185 -----------GEG--ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE---REVKTVDWDAEAAEKG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 321 NFSAFMQKEIFEQPESVFNTMRGRVNfETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVE 400
Cdd:COG0449 249 GYPHFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 401 LASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYT 480
Cdd:COG0449 328 IASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFT 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 481 SQFISLVMFGLMMSEDRISL-QNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLLVMGRGYNYATCLEGALK 559
Cdd:COG0449 408 TQLAALYLLALYLARARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALK 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 560 IKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELP 639
Cdd:COG0449 488 LKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVP 567
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 4826742 640 HTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:COG0449 568 EVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-682 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 731.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYMNYRvprtrkEIFETLIKGLQRLEYRGYDSAGVAIdgnnheVKERHIQLVKKRGKVKALDEELyKQDSMdlkv 80
Cdd:PRK00331 1 MCGIVGYVGQR------NAAEILLEGLKRLEYRGYDSAGIAV------LDDGGLEVRKAVGKVANLEAKL-EEEPL---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 81 efETHFGIAHTRWATHGVPSAVNSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNr 160
Cdd:PRK00331 64 --PGTTGIGHTRWATHGKPTERNAHPHTDCSG-RIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 161 etediTFSTL--VERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVrskyklsteqipilyrtctlenvknicktr 238
Cdd:PRK00331 140 -----GGDLLeaVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL------------------------------ 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 239 mkrldssaclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHrvkrSASDDP-SRAIQTLQMELQQI 317
Cdd:PRK00331 185 -------------GEG--ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIF----DFDGNPvEREVYTVDWDASAA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 318 MKGNFSAFMQKEIFEQPESVFNTMRGRVNFetntvlLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPV 397
Cdd:PRK00331 246 EKGGYRHFMLKEIYEQPEAIRDTLEGRLDE------LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 398 MVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTK 477
Cdd:PRK00331 320 EVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTK 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 478 AYTSQFISLVMFGLMMSEDRISLQNRR-QEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLLVMGRGYNYATCLEG 556
Cdd:PRK00331 400 AFTAQLAVLYLLALALAKARGTLSAEEeADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEG 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 557 ALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYkTI 636
Cdd:PRK00331 480 ALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEADD-VI 558
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 4826742 637 ELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:PRK00331 559 EVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-682 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 704.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKE----------RHIqLVKKRGKVKALDEEL 70
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEdgtaasaptpRPC-VVRSVGNISQLREKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 71 YKQDS----MDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDT 146
Cdd:PTZ00394 80 FSEAVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNG-EFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 147 ETIAKLIKYVFDNRETedITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRskyklsteqipilyrtc 226
Cdd:PTZ00394 159 EVISVLSEYLYTRKGI--HNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR----------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 227 tlenvknicktrmkRLDSSACL-----HAVGD--KAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSA 299
Cdd:PTZ00394 220 --------------RTDDRGCVmklqtYDLTDlsGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 300 SDDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDH-LKEIRRCRRLIVIGCGTS 378
Cdd:PTZ00394 286 RSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 379 YHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRE 458
Cdd:PTZ00394 366 LNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 459 TDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSL-EEKIHDLALELYT 537
Cdd:PTZ00394 446 THYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKE 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 538 QRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRP 617
Cdd:PTZ00394 526 SSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAV 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4826742 618 IILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:PTZ00394 606 VVFATEVDAELKAAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-682 |
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: 648.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 2 CGIFAYMNyrvPRTRKEIfetLIKGLQRLEYRGYDSAGVAIdgnnheVKERHIQLVKKRGKVKALDEELYKQdsmdlkvE 81
Cdd:TIGR01135 1 CGIVGYIG---QRDAVPI---LLEGLKRLEYRGYDSAGIAV------VDEGKLFVRKAVGKVAELANKLGEK-------P 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 82 FETHFGIAHTRWATHGVPSAVNSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFdnRE 161
Cdd:TIGR01135 62 LPGGVGIGHTRWATHGKPTDENAHPHTDEGG-RIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEEL--RE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 162 TEDITFStlVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVrskyklsteqipilyrtctlenvknicktrmkr 241
Cdd:TIGR01135 139 GGDLLEA--VQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGL--------------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 242 ldssaclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKrsaSDDPSRAIQTLQMELQQIMKGN 321
Cdd:TIGR01135 184 ----------GDG--ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFE---GAPVQREVRVIDWDLDAAEKGG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 322 FSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDHLKEIRRcrrLIVIGCGTSYHAAVATRQVLEELTELPVMVEL 401
Cdd:TIGR01135 249 YRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNIDR---IQIVACGTSYHAGLVAKYLIERLAGIPVEVEI 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 402 ASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYTS 481
Cdd:TIGR01135 326 ASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTT 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 482 QFISLVMFGLMMSEDR-ISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKI 560
Cdd:TIGR01135 406 QLTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKL 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 561 KEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPH 640
Cdd:TIGR01135 486 KEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPE 565
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 4826742 641 TVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:TIGR01135 566 VEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-681 |
1.15e-158 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 471.81 E-value: 1.15e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYMnyrvprTRKEIFETLIKGLQRLEYRGYDSAGVA-IDGNNHEVKERHIQLVKKRGKVKALDEELykqdsmdLK 79
Cdd:PTZ00295 24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGELKTTKYASDGTTSDSIEILKEKL-------LD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 80 VEFETHFGIAHTRWATHGVPSAVNSHPQrSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDN 159
Cdd:PTZ00295 91 SHKNSTIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 160 RETeditFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRSKyklsteqipilyrtctlenvknicktrm 239
Cdd:PTZ00295 170 GED----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDD---------------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 240 krldssaclhavgdkavEFFFASDASAIIEHTNRVIFLEDDDIAavadgklSIHRVKRSASDDPSRAIQtLQMELQQIMK 319
Cdd:PTZ00295 218 -----------------SIYVASEPSAFAKYTNEYISLKDGEIA-------ELSLENVNDLYTQRRVEK-IPEEVIEKSP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 320 GNFSAFMQKEIFEQPESVFNTM--RGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTEL-P 396
Cdd:PTZ00295 273 EPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 397 VMVELASDF-LDRNTpvfRDDVCF-FISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVA 474
Cdd:PTZ00295 353 VQVIDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 475 STKAYTSQFISLVMFGLMMSE--DRISLQNRRQEIIRGLRSLPELIKEVL-SLEEKIHDLALELYTQRSLLVMGRGYNYA 551
Cdd:PTZ00295 430 STKAFTSQVTVLSLIALWFAQnkEYSCSNYKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKNAKSMFILGKGLGYP 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 552 TCLEGALKIKEITYMHSEGILAGELKHGPLALID--KQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSkDDTESS 629
Cdd:PTZ00295 510 IALEGALKIKEITYIHAEGFSGGALKHGPFALIDkeKNTPVILIILDDEHKELMINAAEQVKARGAYIIVITD-DEDLVK 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 4826742 630 KFAYKTIELPhTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTV 681
Cdd:PTZ00295 589 DFADEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-285 |
1.40e-112 |
|
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: 337.50 E-value: 1.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 2 CGIFAYMNYRvprtrkEIFETLIKGLQRLEYRGYDSAGVAIDGNNHevkerhIQLVKKRGKVKALDEELYKQDSmdlkve 81
Cdd:cd00714 1 CGIVGYIGKR------EAVDILLEGLKRLEYRGYDSAGIAVIGDGS------LEVVKAVGKVANLEEKLAEKPL------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 82 fETHFGIAHTRWATHGVPSAVNSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDnre 161
Cdd:cd00714 63 -SGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 162 tEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVrskyklsteqipilyrtctlenvknicktrmkr 241
Cdd:cd00714 138 -GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGI--------------------------------- 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 4826742 242 ldssaclhavgdKAVEFFFASDASAIIEHTNRVIFLEDDDIAAV 285
Cdd:cd00714 184 ------------GDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
328-682 |
2.74e-70 |
|
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: 232.10 E-value: 2.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 328 KEIFEQPESVfntmrgRVNFETNTVLLGGLKDHLKEIRRcRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLD 407
Cdd:COG2222 2 REIAQQPEAW------RRALAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 408 RNTPVFRD-DVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISL 486
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 487 VMFGLMMSEDrislqnrrQEIIRGLRSLPELIKEVLSLEEKIHDLAlELYTQRSLLVMGRGYNYATCLEGALKIKEITYM 566
Cdd:COG2222 155 LALLAAWGGD--------DALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 567 HSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTEsskfayktIELPHTVDC-- 644
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAA--------ITLPAIPDLhd 297
|
330 340 350
....*....|....*....|....*....|....*....
gi 4826742 645 -LQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:COG2222 298 aLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
526-680 |
7.23e-66 |
|
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: 213.66 E-value: 7.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 526 EKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQN 605
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4826742 606 ALQQVTARQGRPIILCSKDDTEssKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVT 680
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAK--DLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
369-494 |
3.33e-61 |
|
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: 200.42 E-value: 3.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 369 RLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVT 448
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4826742 449 NTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMS 494
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-283 |
2.37e-53 |
|
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: 182.65 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 2 CGIFAYMNYRVPRTRKEIfeTLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKRGKVkaldeelykqdsmDLKVE 81
Cdd:cd00352 1 CGIFGIVGADGAASLLLL--LLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALD-------------LLDEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 82 FETHFGIAHTRWATHGVPSAVNSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRE 161
Cdd:cd00352 66 LKSGVALGHVRLATNGLPSEANAQPFRSEDGR-IALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 162 TEDitfstLVERVIQQLEGAFALVFKSVHyPGEAVATRRG---SPLLIGVRskyklsteqipilyrtctlenvknicktr 238
Cdd:cd00352 145 LFE-----AVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGIT----------------------------- 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 4826742 239 mkrldssaclhavgdKAVEFFFASDASAIIEHT-NRVIFLEDDDIA 283
Cdd:cd00352 190 ---------------KDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
363-492 |
9.30e-40 |
|
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: 142.44 E-value: 9.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 363 EIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSGETADTLLALRYCKDRG 441
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 4826742 442 ALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLM 492
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
534-665 |
9.59e-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: 105.46 E-value: 9.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 534 ELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQnALQQVTAR 613
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 4826742 614 QGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLR 665
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-186 |
4.65e-23 |
|
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: 98.69 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 2 CGIFAYMNyrvprtRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHevkerhIQLVKKRGKVkaldEELYKQDSMDlkvE 81
Cdd:cd00715 1 CGVFGIYG------AEDAARLTYLGLYALQHRGQESAGIATSDGKR------FHTHKGMGLV----SDVFDEEKLR---R 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 82 FETHFGIAHTRWATHGVPSAVNSHP--QRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvfdn 159
Cdd:cd00715 62 LPGNIAIGHVRYSTAGSSSLENAQPfvVNSPLG-GIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA----- 135
|
170 180
....*....|....*....|....*..
gi 4826742 160 RETEDITFSTLVERVIQQLEGAFALVF 186
Cdd:cd00715 136 RSLAKDDLFEAIIDALERVKGAYSLVI 162
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-186 |
9.42e-23 |
|
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: 102.02 E-value: 9.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYMNyrvprtRKEIFETLIKGLQRLEYRGYDSAG-VAIDGNnhevkerHIQLVKKRGKVKaldeELYKQDSMDlk 79
Cdd:COG0034 7 ECGVFGIYG------HEDVAQLTYYGLYALQHRGQESAGiATSDGG-------RFHLHKGMGLVS----DVFDEEDLE-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 80 vEFETHFGIAHTRWATHGVPSAVNSHP--QRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvf 157
Cdd:COG0034 68 -RLKGNIAIGHVRYSTTGSSSLENAQPfyVNSPFG-SIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA--- 142
|
170 180
....*....|....*....|....*....
gi 4826742 158 dnRETEDITFSTLVERVIQQLEGAFALVF 186
Cdd:COG0034 143 --RELTKEDLEEAIKEALRRVKGAYSLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-217 |
1.35e-18 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 88.92 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 2 CGIFAYMNyrvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKkrgkvkaldeELYKQDSMDlkvE 81
Cdd:TIGR01134 1 CGVVGIYG-----QEEVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVS----------DVFNEEHLQ---R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 82 FETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVI-HNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvfdNR 160
Cdd:TIGR01134 63 LKGNVGIGHVRYSTAGSSGLENAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLA----HN 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826742 161 ETEDITFSTLVERVIQQLEGAFALVFKSVHypgEAVATR--RG-SPLLIGVR-SKYKLSTE 217
Cdd:TIGR01134 139 DESKDDLFDAVARVLERVRGAYALVLMTED---GLVAVRdpHGiRPLVLGRRgDGYVVASE 196
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-210 |
8.56e-18 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 86.66 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYmnYRVPRTRKEIFEtlikGLQRLEYRGYDSAG-VAIDGNNhevkerhIQLVKKRGKVKaldeELYKQDSMDlk 79
Cdd:PLN02440 1 ECGVVGI--FGDPEASRLCYL----GLHALQHRGQEGAGiVTVDGNR-------LQSITGNGLVS----DVFDESKLD-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 80 vEFETHFGIAHTRWATHGVPSAVNSHPqrsdkgneFV---------VIHNGIITNYKDLRKFLESKGYEFESETDTETIA 150
Cdd:PLN02440 62 -QLPGDIAIGHVRYSTAGASSLKNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4826742 151 KLIkyvfdnreTEDI--TFSTLVERVIQQLEGAFALVFKSvhyPGEAVATR-----RgsPLLIGVRS 210
Cdd:PLN02440 133 HLI--------AISKarPFFSRIVDACEKLKGAYSMVFLT---EDKLVAVRdphgfR--PLVMGRRS 186
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
82-186 |
6.41e-16 |
|
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: 74.65 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 82 FETHFGIAHTRWATHGVPSAVNsHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYvfdnre 161
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLPDAGN-QPMLSRDGR-LVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEE------ 79
|
90 100
....*....|....*....|....*
gi 4826742 162 teditfstLVERVIQQLEGAFALVF 186
Cdd:pfam13522 80 --------WGEDCLERLRGMFAFAI 96
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-155 |
5.19e-15 |
|
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: 75.38 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 2 CGIFAYMnyrvpRTRKEIF--ETLIKGLQRLEYRG-YDSAGVAIDGNNHevkerhiQLVKKRGKvkalDEELYKQ----- 73
Cdd:cd01907 1 CGIFGIM-----SKDGEPFvgALLVEMLDAMQERGpGDGAGFALYGDPD-------AFVYSSGK----DMEVFKGvgype 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 74 ---DSMDLKvEFETHFGIAHTRWATHgvpSAVN---SHPQRSdkGNEFVViHNGIITNYKDLRKFLESKGYEFESETDTE 147
Cdd:cd01907 65 diaRRYDLE-EYKGYHWIAHTRQPTN---SAVWwygAHPFSI--GDIAVV-HNGEISNYGSNREYLERFGYKFETETDTE 137
|
....*...
gi 4826742 148 TIAKLIKY 155
Cdd:cd01907 138 VIAYYLDL 145
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
26-185 |
2.30e-14 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 75.84 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 26 GLQRLEYRGYDSAGVAI-DGnnhevkeRHIQLVKKRGKV-KALDEELYKqdsmdlkvEFETHFGIAHTRWATHGVPSAVN 103
Cdd:PRK05793 35 GLYALQHRGQESAGIAVsDG-------EKIKVHKGMGLVsEVFSKEKLK--------GLKGNSAIGHVRYSTTGASDLDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 104 SHPQRSD-KGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLI----KYVFDNreteditfsTLVErVIQQL 178
Cdd:PRK05793 100 AQPLVANyKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIarsaKKGLEK---------ALVD-AIQAI 169
|
....*..
gi 4826742 179 EGAFALV 185
Cdd:PRK05793 170 KGSYALV 176
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
369-492 |
5.78e-14 |
|
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: 68.76 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 369 RLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFISQSGETADTLLALRYCKDRGALTVGV 447
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 4826742 448 TNTVGSSISRETDcgVHINAGPEIGVASTKAYtsqFISLVMFGLM 492
Cdd:cd05710 81 TDDEDSPLAKLAD--YVIVYGFEIDAVEEKYL---LLYMLALRLL 120
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
90-185 |
2.16e-13 |
|
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: 67.16 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 90 HTRWATHGVPSAvnSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFdnreteditfst 169
Cdd:pfam13537 1 HRRLSIIDLEGG--AQPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW------------ 66
|
90
....*....|....*.
gi 4826742 170 lVERVIQQLEGAFALV 185
Cdd:pfam13537 67 -GEDCVDRLNGMFAFA 81
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-152 |
4.40e-12 |
|
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: 66.04 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 2 CGIFAYMNYRvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNnhevkerhiqlvkkrgkvkaldeelykqdsmdlkve 81
Cdd:cd00712 1 CGIAGIIGLD---GASVDRATLERMLDALAHRGPDGSGIWIDEG------------------------------------ 41
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826742 82 fethFGIAHTRWATHGVpsavnSH---PQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKL 152
Cdd:cd00712 42 ----VALGHRRLSIIDL-----SGgaqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL 105
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-152 |
4.73e-12 |
|
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: 69.10 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYMNYRVPRTRkeifETLIKGLQRLEYRGYDSAGVAIDGnnhevkerhiqlvkkrgkvkaldeelykqdsmdlkv 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------ 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826742 81 efetHFGIAHTRWAThgVPSAVNSH-PQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKL 152
Cdd:COG0367 41 ----GVALGHRRLSI--IDLSEGGHqPMVSEDGR-YVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
370-448 |
1.91e-10 |
|
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: 57.77 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 370 LIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFISQSGETADTLLALRYCKDRGALTVGV 447
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 4826742 448 T 448
Cdd:cd04795 81 T 81
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
421-492 |
3.35e-10 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 61.72 E-value: 3.35e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826742 421 ISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFISLVMF--GLM 492
Cdd:PRK05441 138 IAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstGVM 213
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
402-509 |
3.81e-10 |
|
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: 61.00 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 402 ASDFLDRNTPvfRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVAST--KAY 479
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 4826742 480 TSQFISLVMF-------------GLM--MSEDRISLQNRRQEIIR 509
Cdd:cd05007 186 TAQKLALNMLstavmirlgkvygNLMvdVRATNEKLRERAIRIVM 230
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
365-670 |
7.98e-10 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 61.17 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 365 RRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFI--SQSGETADTLLALRYCKDRGA 442
Cdd:PRK11382 42 RDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 443 LTVGVTNTVGSSISRETDCGVHINAGP--EIGVASTKAYTSQFISlvmfglmmsedRISLQNRRQEIIRGLRSLPELIKE 520
Cdd:PRK11382 121 LTAAFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMIT-----------RLAPNAEIGKIKNDLKQLPNALGH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 521 -VLSLEEKIHDLALE------LYTQRSLLVMGRGYNyatclEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMV 593
Cdd:PRK11382 190 lVRTWEEKGRQLGELasqwpmIYTVAAGPLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFL 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4826742 594 IMKDPCFAKCQNALQQVTARQGRPIILcskDDTESSKFAYKtielphtvdCLQGILSVIPLQLLSFHLAVLRGYDVD 670
Cdd:PRK11382 265 LGNDESRHTTERAINFVKQRTDNVIVI---DYAEISQGLHP---------WLAPFLMFVPMEWLCYYLSIYKDHNPD 329
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
364-488 |
1.77e-09 |
|
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: 56.47 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 364 IRRCRRLIVIGCGTSYHAA--VATRqvleeLTELPVMVELASD---FLDRNTPVFRDDVCFFISQSGETADTLLALRYCK 438
Cdd:cd05013 10 LAKARRIYIFGVGSSGLVAeyLAYK-----LLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAEIAK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 4826742 439 DRGALTVGVTNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFISLVM 488
Cdd:cd05013 85 ERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
368-489 |
1.94e-09 |
|
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: 56.01 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 368 RRLIVIGCGTSYHAA---VATRQVleelTELPvmvelaSDFLDrntP----------VFRDDVCFFISQSGETADTLLAL 434
Cdd:cd05014 1 GKVVVTGVGKSGHIArkiAATLSS----TGTP------AFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 4826742 435 RYCKDRGALTVGVTNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFISLVMF 489
Cdd:cd05014 68 PHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALG 122
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
364-514 |
4.67e-09 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 58.02 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 364 IRRCRRLIVIGCGTSYHAAVATRQVLEEL----TELPVMVELASDFLDRNTPvfrDDVCFFISQSGETADTLLALRYCKD 439
Cdd:COG1737 131 LAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARLAKE 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4826742 440 RGALTVGVTNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFISLVM----FGLMMSEDRISLQNRRQEIIRGLRSL 514
Cdd:COG1737 208 RGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALidalAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
402-492 |
8.00e-09 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 57.41 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 402 ASDFLDRN-TPvfrDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIgVA-ST--K 477
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 4826742 478 AYTSQFISLVMF--GLM 492
Cdd:COG2103 198 AGTAQKLVLNMLstAAM 214
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
83-186 |
3.63e-08 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 56.19 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 83 ETHFGIAHTRWATHGVPSAVnsHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIkyvfdnRET 162
Cdd:TIGR01536 39 DGNAILGHRRLAIIDLSGGA--QPMSNEGK-TYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY------EEW 109
|
90 100
....*....|....*....|....
gi 4826742 163 EditfstlvERVIQQLEGAFALVF 186
Cdd:TIGR01536 110 G--------EECVDRLDGMFAFAL 125
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-154 |
4.62e-07 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 53.18 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYMNYRVprTRKEIFETLIKGLQRLEYRGYDSAGVAIdgnnhevkerhiqlvkkrgkvkaldeelykqdsmdLKV 80
Cdd:PTZ00077 1 MCGILAIFNSKG--ERHELRRKALELSKRLRHRGPDWSGIIV-----------------------------------LEN 43
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826742 81 EFETHFGIAHTRWATHGVPSAvnSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIK 154
Cdd:PTZ00077 44 SPGTYNILAHERLAIVDLSDG--KQPLLDDDET-VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYK 114
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-185 |
1.43e-06 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 51.45 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 1 MCGIFAYmnYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNnhevkerhiqlvkkrgkvkaldeelykqdsmdlkv 80
Cdd:PRK09431 1 MCGIFGI--LDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDN----------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 81 efethfGI-AHTRWATHGVPSAvnSHPQRSDKGNEfVVIHNGIITNYKDLRKFLESKgYEFESETDTETIAKLikYvfdn 159
Cdd:PRK09431 44 ------AIlGHERLSIVDVNGG--AQPLYNEDGTH-VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL--Y---- 107
|
170 180
....*....|....*....|....*.
gi 4826742 160 rETEDITFstlvervIQQLEGAFALV 185
Cdd:PRK09431 108 -QEKGPDF-------LDDLDGMFAFA 125
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
83-153 |
1.80e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 49.96 E-value: 1.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826742 83 ETHFGIAHTRWATHGVPSAVNSHPQRsdkGNEFVVIHNGIITNYKDLRKFLESK-----GYEFESETDTETIAKLI 153
Cdd:COG0121 75 KSRLVIAHVRKATVGPVSLENTHPFR---GGRWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELAFALL 147
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
364-470 |
1.85e-06 |
|
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: 50.36 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 364 IRRCR-RLIVIGCGTSYHAA---VATrqvleeltelpvmveLASdfldRNTPVF----------------RDDVCFFISQ 423
Cdd:COG0794 40 ILNCKgRVVVTGMGKSGHIArkiAAT---------------LAS----TGTPAFflhpaeashgdlgmitPGDVVIAISN 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 4826742 424 SGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDcgVHINAGPE 470
Cdd:COG0794 101 SGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVE 145
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
88-178 |
8.01e-06 |
|
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: 47.77 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 88 IAHTRWATHGVPSAVNSHPQRSDkgnEFVVIHNGIITNYKDLR-KFLESKGYEFESETDTETIAKLIkyvFDNRETEDIT 166
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRrRLLRLLPRLPVGTTDSELAFALL---LSRLLERDPL 157
|
90
....*....|..
gi 4826742 167 FSTLVERVIQQL 178
Cdd:cd01908 158 DPAELLDAILQT 169
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
415-489 |
3.90e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 46.22 E-value: 3.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4826742 415 DDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFISLVMF 489
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
81-149 |
3.90e-04 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 42.70 E-value: 3.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 81 EFETHFGIAHTRWATHGVPSAVNSHP-QRSDKGNEFVVIHNGIITNYKDLRkfleSKGYEFESETDTETI 149
Cdd:pfam13230 68 PIRSRNVIAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNGDLKGYAPKL----SGRFQPVGSTDSELA 133
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
541-594 |
1.15e-03 |
|
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: 38.51 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 4826742 541 LLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGP-LALIDKQMPVIMVI 594
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALS 55
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
409-499 |
4.16e-03 |
|
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: 38.71 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826742 409 NTPVF-RDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINA----GPEIGVASTKAYTSQF 483
Cdd:cd05005 69 TTPAIgPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAatkdDHGGEHKSIQPLGTLF 148
|
90 100
....*....|....*....|..
gi 4826742 484 -ISLVMFG-----LMMSEDRIS 499
Cdd:cd05005 149 eQSALVFLdaviaKLMEELGVS 170
|
|
| |
