|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
12-691 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 925.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDgnNNEDKERFIKLV-KKRGKVKALEEELYK---QDGLDS 87
Cdd:PLN02981 3 GIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLVfREEGKIESLVRSVYEevaETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 88 KADFETHFGIAHTRWATHGVPSAINSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYD 167
Cdd:PLN02981 81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 168 --NRESEDTSFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRskyKLSTEQIPVLYRTCNIENMKNmcn 245
Cdd:PLN02981 161 klNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVK---ELPEEKNSSAVFTSEGFLTKN--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 246 srmkrldsstclhavGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLE----RSASDDP-----SRVI 316
Cdd:PLN02981 235 ---------------RDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFEnekgRGGGGLSrpasvERAL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 317 QTLQMELQQIMKGNFSAFMQKEIFEQPESVVNTMRGRV----NFENSTVLLGGLKDHLKEIRRCRRLIIIGCGTSYHAAV 392
Cdd:PLN02981 300 STLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAAL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 393 ATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGV 472
Cdd:PLN02981 380 AARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 473 HINAGPEIGVASTKAYTSQFVSLVMFGLMMSEDRISLQKRRREIISGLKSLPEMIKEVLSLDEKIHDLALELYKQRSLLV 552
Cdd:PLN02981 460 HINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 553 MGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSK 632
Cdd:PLN02981 540 FGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSK 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024354922 633 EDtESSKFAYKT---IELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 691
Cdd:PLN02981 620 GD-ASSVCPSGGcrvIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
12-691 |
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: 771.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLnyrvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVKALEEELykqdgldSKADF 91
Cdd:COG0449 3 GIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGG------LEVRKAVGKLANLEEKL-------AEEPL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 92 ETHFGIAHTRWATHGVPSAINSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYDnres 171
Cdd:COG0449 64 SGTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLK---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 172 EDTSFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyrtcnienmknmcnsrmkrl 251
Cdd:COG0449 139 GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL---------------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 252 dsstclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLERSASDdpsRVIQTLQMELQQIMKGNF 331
Cdd:COG0449 185 ---------GEG--ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE---REVKTVDWDAEAAEKGGY 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 332 SAFMQKEIFEQPESVVNTMRGRVNfENSTVLLGGLKDHLKEIRRCRRLIIIGCGTSYHAAVATRQVLEELTELPVMVELA 411
Cdd:COG0449 251 PHFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 412 SDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQ 491
Cdd:COG0449 330 SEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQ 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 492 FVSLVMFGLMMSEDRISL-QKRRREIISGLKSLPEMIKEVLSLDEKIHDLALELYKQRSLLVMGRGYNYATCLEGALKIK 570
Cdd:COG0449 410 LAALYLLALYLARARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLK 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 571 EITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDTESSKFAYKTIELPHT 650
Cdd:COG0449 490 EISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEV 569
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2024354922 651 VDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 691
Cdd:COG0449 570 DELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
12-691 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 713.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNYRvprtrkEIFETLIKGLQRLEYRGYDSAGVA-IDGNNnedkerfIKLVKKRGKVKALEEELykqdgldSKAD 90
Cdd:PRK00331 3 GIVGYVGQR------NAAEILLEGLKRLEYRGYDSAGIAvLDDGG-------LEVRKAVGKVANLEAKL-------EEEP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 91 FETHFGIAHTRWATHGVPSAINSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYdnRE 170
Cdd:PRK00331 63 LPGTTGIGHTRWATHGKPTERNAHPHTDCSG-RIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEEL--KE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 171 SEDTsFSAlVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyrtcnienmknmcnsrmkr 250
Cdd:PRK00331 140 GGDL-LEA-VRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL--------------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 251 ldsstclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLErsasDDP-SRVIQTLQMELQQIMKG 329
Cdd:PRK00331 185 ----------GEG--ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFD----GNPvEREVYTVDWDASAAEKG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 330 NFSAFMQKEIFEQPESVVNTMRGRVNFenstvlLGGLKDHLKEIRRCRRLIIIGCGTSYHAAVATRQVLEELTELPVMVE 409
Cdd:PRK00331 249 GYRHFMLKEIYEQPEAIRDTLEGRLDE------LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 410 LASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYT 489
Cdd:PRK00331 323 IASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFT 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 490 SQFVSLVMFGLMMSEDRISLQKRR-REIISGLKSLPEMIKEVLSLDEKIHDLALELYKQRSLLVMGRGYNYATCLEGALK 568
Cdd:PRK00331 403 AQLAVLYLLALALAKARGTLSAEEeADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALK 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 569 IKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDTESSKFAYkTIELP 648
Cdd:PRK00331 483 LKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEADD-VIEVP 561
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2024354922 649 HTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 691
Cdd:PRK00331 562 EVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-691 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 686.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNEDKERFIK---------LVKKRGKVKALEEELYKQ 82
Cdd:PTZ00394 3 GIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAasaptprpcVVRSVGNISQLREKVFSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 83 DG----LDSKADFETHFGIAHTRWATHGVPSAINSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETI 158
Cdd:PTZ00394 83 AVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNG-EFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 159 PKLIKYMYDNRESedTSFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRskyklsteqipvlyrtcniE 238
Cdd:PTZ00394 162 SVLSEYLYTRKGI--HNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR-------------------R 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 239 NMKNMCNSRMKRLDSSTClhavgDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLERSASDDPSRVIQT 318
Cdd:PTZ00394 221 TDDRGCVMKLQTYDLTDL-----SGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 319 LQMELQQIMKGNFSAFMQKEIFEQPESVVNTMRGRVNFENSTVLLGGLKDH-LKEIRRCRRLIIIGCGTSYHAAVATRQV 397
Cdd:PTZ00394 296 LDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 398 LEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAG 477
Cdd:PTZ00394 376 FEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 478 PEIGVASTKAYTSQFVSLVMFGLMMSEDRISLQKRRREIISGLKSLPEMIKEVLSL-DEKIHDLALELYKQRSLLVMGRG 556
Cdd:PTZ00394 456 VEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 557 YNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDTE 636
Cdd:PTZ00394 536 YDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAE 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2024354922 637 SSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 691
Cdd:PTZ00394 616 LKAAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
12-691 |
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: 640.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNyrvPRTRKEIfetLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVKALEEELykqdgldSKADF 91
Cdd:TIGR01135 2 GIVGYIG---QRDAVPI---LLEGLKRLEYRGYDSAGIAVVDEGK------LFVRKAVGKVAELANKL-------GEKPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 92 ETHFGIAHTRWATHGVPSAINSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYdnRES 171
Cdd:TIGR01135 63 PGGVGIGHTRWATHGKPTDENAHPHTDEGG-RIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEEL--REG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 172 EDTSFSalVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyrtcnienmknmcnsrmkrl 251
Cdd:TIGR01135 140 GDLLEA--VQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGL---------------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 252 dsstclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLERSASDDPSRVIQtlqMELQQIMKGNF 331
Cdd:TIGR01135 184 ---------GDG--ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVID---WDLDAAEKGGY 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 332 SAFMQKEIFEQPESVVNTMRGRVNFENSTVLLGGLKDHLKEIRRCRRLiiiGCGTSYHAAVATRQVLEELTELPVMVELA 411
Cdd:TIGR01135 250 RHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNIDRIQIV---ACGTSYHAGLVAKYLIERLAGIPVEVEIA 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 412 SDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQ 491
Cdd:TIGR01135 327 SEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQ 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 492 FVSLVMFGLMMSEDR-ISLQKRRREIISGLKSLPEMIKEVLSLDEKIHDLALELYKQRSLLVMGRGYNYATCLEGALKIK 570
Cdd:TIGR01135 407 LTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLK 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 571 EITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDTESSKFAYKTIELPHT 650
Cdd:TIGR01135 487 EISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEV 566
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2024354922 651 VDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 691
Cdd:TIGR01135 567 EELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-690 |
2.69e-153 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 458.33 E-value: 2.69e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLnyrvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNEDKerFIKLVKKRGKVKALEeeLYKQDGLDSKADf 91
Cdd:PTZ00295 26 GIVGYL------GNEDASKILLEGIEILQNRGYDSCGISTISSGGELK--TTKYASDGTTSDSIE--ILKEKLLDSHKN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 92 eTHFGIAHTRWATHGVPSAINSHPQrSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYDNRES 171
Cdd:PTZ00295 95 -STIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGED 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 172 edtsFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRSKyklsteqipvlyrtcnienmknmcnsrmkrl 251
Cdd:PTZ00295 173 ----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDD------------------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 252 dsstclhavgdkavEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKlsIHRLERsasddPSRVIQtLQMELQQIMKGNF 331
Cdd:PTZ00295 218 --------------SIYVASEPSAFAKYTNEYISLKDGEIAELSLEN--VNDLYT-----QRRVEK-IPEEVIEKSPEPY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 332 SAFMQKEIFEQPESVVNTM--RGRVNFENSTVLLGGLKDHLKEIRRCRRLIIIGCGTSYHAAVATRQVLEELTEL-PVMV 408
Cdd:PTZ00295 276 PHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTVQV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 409 ELASDF-LDRNTpvfRDDVCF-FISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTK 486
Cdd:PTZ00295 356 IDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 487 AYTSQFVSLVMFGLMMSE--DRISLQKRRREIISGLKSLPEMIKEVL-SLDEKIHDLALELYKQRSLLVMGRGYNYATCL 563
Cdd:PTZ00295 433 AFTSQVTVLSLIALWFAQnkEYSCSNYKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKNAKSMFILGKGLGYPIAL 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 564 EGALKIKEITYMHSEGILAGELKHGPLALID--KQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDtESSKFA 641
Cdd:PTZ00295 513 EGALKIKEITYIHAEGFSGGALKHGPFALIDkeKNTPVILIILDDEHKELMINAAEQVKARGAYIIVITDDED-LVKDFA 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2024354922 642 YKTIELPhTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTV 690
Cdd:PTZ00295 592 DEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
12-294 |
3.27e-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: 337.11 E-value: 3.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNYRvprtrkEIFETLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVKALEEELYKQDGldskadf 91
Cdd:cd00714 2 GIVGYIGKR------EAVDILLEGLKRLEYRGYDSAGIAVIGDGS------LEVVKAVGKVANLEEKLAEKPL------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 92 ETHFGIAHTRWATHGVPSAINSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYDnres 171
Cdd:cd00714 63 SGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 172 EDTSFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyrtcnienmknmcnsrmkrl 251
Cdd:cd00714 138 GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGI---------------------------------- 183
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024354922 252 dsstclhavgdKAVEFFFASDASAIIEHTNRVIFLEDDDIAAV 294
Cdd:cd00714 184 -----------GDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
535-689 |
2.78e-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: 215.20 E-value: 2.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 535 EKIHDLALELYKQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQN 614
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024354922 615 ALQQVTARQGRPIILCSKEDTEssKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVT 689
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAK--DLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
337-691 |
1.70e-65 |
|
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: 219.38 E-value: 1.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 337 KEIFEQPESVVNTmrgrvnFENSTVLLGGLKDHLKEIRRCRRLIIiGCGTSYHAAVATRQVLEELTELPVMVELASDFLD 416
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPPRRVVLV-GAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 417 RNTPVFRD-DVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSL 495
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 496 VM-FGLMMSEDrislqkrrrEIISGLKSLPEMIKEVLSLDEKIHDLAlELYKQRSLLVMGRGYNYATCLEGALKIKEITY 574
Cdd:COG2222 155 LAlLAAWGGDD---------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 575 MHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVtARQGRPIILCSKEDTEsskfaykTIELPHTVDC- 653
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAEL-RALGARVVAIGAEDDA-------AITLPAIPDLh 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2024354922 654 --LQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 691
Cdd:COG2222 297 daLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
383-503 |
1.04e-59 |
|
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: 196.56 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 383 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGS 462
Cdd:cd05008 6 GCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGS 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2024354922 463 SISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFGLMMS 503
Cdd:cd05008 86 TLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
12-292 |
3.43e-52 |
|
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: 179.95 E-value: 3.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNYRVPRTRKEIfeTLIKGLQRLEYRGYDSAGVAIDGNNNEDKERFIKLVKKRGKVKALEEelykqdgldskadF 91
Cdd:cd00352 2 GIFGIVGADGAASLLLL--LLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEP-------------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 92 ETHFGIAHTRWATHGVPSAINSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYDNRES 171
Cdd:cd00352 67 KSGVALGHVRLATNGLPSEANAQPFRSEDGR-IALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 172 EDTsfsalVERVIQQLEGAFALVFKSIHyPGEAVATRRG---SPLLIGVRskyklsteqipvlyrtcnienmknmcnsrm 248
Cdd:cd00352 146 FEA-----VEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGIT------------------------------ 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2024354922 249 krldsstclhavgdKAVEFFFASDASAIIEHT-NRVIFLEDDDIA 292
Cdd:cd00352 190 --------------KDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
383-501 |
8.75e-36 |
|
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: 131.27 E-value: 8.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 383 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVG 461
Cdd:pfam01380 12 GRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPG 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2024354922 462 SSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFGLM 501
Cdd:pfam01380 92 SPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
543-674 |
4.06e-28 |
|
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: 109.70 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 543 ELYKQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQnALQQVTAR 622
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2024354922 623 QGRPIILCSKEDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLR 674
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
12-195 |
1.92e-21 |
|
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: 94.06 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNyrvprtRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVkaleEELYKQDGLDSkadF 91
Cdd:cd00715 2 GVFGIYG------AEDAARLTYLGLYALQHRGQESAGIATSDGKR------FHTHKGMGLV----SDVFDEEKLRR---L 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 92 ETHFGIAHTRWATHGVPSAINSHP--QRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKymydnR 169
Cdd:cd00715 63 PGNIAIGHVRYSTAGSSSLENAQPfvVNSPLG-GIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA-----R 136
|
170 180
....*....|....*....|....*.
gi 2024354922 170 ESEDTSFSALVERVIQQLEGAFALVF 195
Cdd:cd00715 137 SLAKDDLFEAIIDALERVKGAYSLVI 162
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
35-195 |
1.00e-19 |
|
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: 92.78 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 35 GLQRLEYRGYDSAG-VAIDGNNnedkerfIKLVKKRGKVKaleeELYKQDGLDSkadFETHFGIAHTRWATHGVPSAINS 113
Cdd:COG0034 26 GLYALQHRGQESAGiATSDGGR-------FHLHKGMGLVS----DVFDEEDLER---LKGNIAIGHVRYSTTGSSSLENA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 114 HP--QRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKymydnRESEDTSFSALVERVIQQLEGAF 191
Cdd:COG0034 92 QPfyVNSPFG-SIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA-----RELTKEDLEEAIKEALRRVKGAY 165
|
....
gi 2024354922 192 ALVF 195
Cdd:COG0034 166 SLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
35-226 |
4.96e-17 |
|
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: 84.29 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 35 GLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVKaleeELYKQDGLDskaDFETHFGIAHTRWATHGVPSAINSH 114
Cdd:TIGR01134 20 GLYALQHRGQESAGISVFDGNR------FRLHKGNGLVS----DVFNEEHLQ---RLKGNVGIGHVRYSTAGSSGLENAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 115 PQRSDKGNEFVVI-HNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYmydNRESEDTSFSAlVERVIQQLEGAFAL 193
Cdd:TIGR01134 87 PFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAH---NDESKDDLFDA-VARVLERVRGAYAL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024354922 194 VFKSIHypgEAVATR--RG-SPLLIGVR-SKYKLSTE 226
Cdd:TIGR01134 163 VLMTED---GLVAVRdpHGiRPLVLGRRgDGYVVASE 196
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
35-219 |
9.47e-17 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 83.57 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 35 GLQRLEYRGYDSAG-VAIDGNnnedkeRFiKLVKKRGKVKaleeELYKQDGLDSkadFETHFGIAHTRWATHGVPSAINS 113
Cdd:PLN02440 20 GLHALQHRGQEGAGiVTVDGN------RL-QSITGNGLVS----DVFDESKLDQ---LPGDIAIGHVRYSTAGASSLKNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 114 HPqrsdkgneFV---------VIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIkymydnreSEDTS---FSALVE 181
Cdd:PLN02440 86 QP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLI--------AISKArpfFSRIVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024354922 182 rVIQQLEGAFALVFKSihyPGEAVATR-----RgsPLLIGVRS 219
Cdd:PLN02440 150 -ACEKLKGAYSMVFLT---EDKLVAVRdphgfR--PLVMGRRS 186
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
35-194 |
3.03e-15 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 78.92 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 35 GLQRLEYRGYDSAGVAI-DGnnnedkeRFIKLVKKRGKVkaleEELYKQDGLDSkadFETHFGIAHTRWATHGVPSAINS 113
Cdd:PRK05793 35 GLYALQHRGQESAGIAVsDG-------EKIKVHKGMGLV----SEVFSKEKLKG---LKGNSAIGHVRYSTTGASDLDNA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 114 HPQRSD-KGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKyMYDNRESEDtsfsALVErVIQQLEGAFA 192
Cdd:PRK05793 101 QPLVANyKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIA-RSAKKGLEK----ALVD-AIQAIKGSYA 174
|
..
gi 2024354922 193 LV 194
Cdd:PRK05793 175 LV 176
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
91-195 |
8.39e-15 |
|
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: 71.57 E-value: 8.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 91 FETHFGIAHTRWATHGVPSAINsHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLikymydnre 170
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLPDAGN-QPMLSRDGR-LVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL--------- 76
|
90 100
....*....|....*....|....*
gi 2024354922 171 sedtsFSALVERVIQQLEGAFALVF 195
Cdd:pfam13522 77 -----YEEWGEDCLERLRGMFAFAI 96
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
99-194 |
2.12e-14 |
|
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: 70.24 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 99 HTRWATHGVPSAInsHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYdnresedtsfsa 178
Cdd:pfam13537 1 HRRLSIIDLEGGA--QPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW------------ 66
|
90
....*....|....*.
gi 2024354922 179 lVERVIQQLEGAFALV 194
Cdd:pfam13537 67 -GEDCVDRLNGMFAFA 81
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
12-166 |
1.15e-12 |
|
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: 68.45 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLnyrvpRTRKEIF--ETLIKGLQRLEYRG-YDSAGVAIDGnnneDKERFIKLVKKR-GKVKAL--EEELYKQDGL 85
Cdd:cd01907 2 GIFGIM-----SKDGEPFvgALLVEMLDAMQERGpGDGAGFALYG----DPDAFVYSSGKDmEVFKGVgyPEDIARRYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 86 DSkadFETHFGIAHTRWATHgvpSAIN---SHPQRSdkGNEFVViHNGIITNYKDLRKFLESKGYEFESETDTETIPKLI 162
Cdd:cd01907 73 EE---YKGYHWIAHTRQPTN---SAVWwygAHPFSI--GDIAVV-HNGEISNYGSNREYLERFGYKFETETDTEVIAYYL 143
|
....
gi 2024354922 163 KYMY 166
Cdd:cd01907 144 DLLL 147
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
383-469 |
1.47e-12 |
|
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: 64.90 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 383 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFISQSGETADTLMALRYCKERRALTVGITNTVG 461
Cdd:cd05710 6 GCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDED 85
|
....*...
gi 2024354922 462 SSISRETD 469
Cdd:cd05710 86 SPLAKLAD 93
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
12-194 |
1.66e-11 |
|
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: 64.50 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNYRvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNnnedkerfiklvkkrgkvkaleeelykqdgldskadf 91
Cdd:cd00712 2 GIAGIIGLD---GASVDRATLERMLDALAHRGPDGSGIWIDEG------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 92 ethFGIAHTRWATHGVpsainSH---PQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLikYM-YD 167
Cdd:cd00712 42 ---VALGHRRLSIIDL-----SGgaqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL--YEeWG 110
|
170 180
....*....|....*....|....*..
gi 2024354922 168 nresedtsfsalvERVIQQLEGAFALV 194
Cdd:cd00712 111 -------------EDCLERLNGMFAFA 124
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
411-518 |
4.75e-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: 60.61 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 411 ASDFLDRNTPvfRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 488
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024354922 489 TSQFVSLVMF-------------GLM--MSEDRISLQKRRREIIS 518
Cdd:cd05007 186 TAQKLALNMLstavmirlgkvygNLMvdVRATNEKLRERAIRIVM 230
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
424-501 |
7.94e-10 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 60.57 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 424 DDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--G 499
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstG 211
|
..
gi 2024354922 500 LM 501
Cdd:PRK05441 212 VM 213
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
12-194 |
9.26e-10 |
|
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: 61.78 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNYRVPRTRkeifETLIKGLQRLEYRGYDSAGVAIDGnnnedkerfiklvkkrgkvkaleeelykqdgldskadf 91
Cdd:COG0367 3 GIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG-------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 92 etHFGIAHTRWAThgVPSAINSH-PQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLikymydnre 170
Cdd:COG0367 41 --GVALGHRRLSI--IDLSEGGHqPMVSEDGR-YVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA--------- 106
|
170 180
....*....|....*....|....
gi 2024354922 171 sedtsFSALVERVIQQLEGAFALV 194
Cdd:COG0367 107 -----YEEWGEDCLERLNGMFAFA 125
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
383-457 |
4.18e-09 |
|
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: 53.92 E-value: 4.18e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024354922 383 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFISQSGETADTLMALRYCKERRALTVGIT 457
Cdd:cd04795 5 GIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAIT 81
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
118-195 |
6.03e-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: 55.80 E-value: 6.03e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024354922 118 SDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIpkLIKYMYDNresedtsfsalvERVIQQLEGAFALVF 195
Cdd:TIGR01536 62 SNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVI--LHLYEEWG------------EECVDRLDGMFAFAL 125
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
424-497 |
1.47e-07 |
|
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: 51.08 E-value: 1.47e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024354922 424 DDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM 497
Cdd:cd05013 61 GDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
423-523 |
2.11e-07 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 53.01 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 423 RDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM----F 498
Cdd:COG1737 182 PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALidalA 259
|
90 100
....*....|....*....|....*
gi 2024354922 499 GLMMSEDRISLQKRRREIISGLKSL 523
Cdd:COG1737 260 AAVAQRDGDKARERLERTEALLSEL 284
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
383-682 |
3.15e-07 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 53.08 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 383 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFI--SQSGETADTLMALRYCKERRALTVGITNTV 460
Cdd:PRK11382 51 ACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAAFTKRA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 461 GSSISRETDCGVHINAGPEIGVASTKAYTsqfVSLVMFGLMMSEDRISlqkrrrEIISGLKSLPEMIKE-VLSLDEKIHD 539
Cdd:PRK11382 130 DSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMITRLAPNAEIG------KIKNDLKQLPNALGHlVRTWEEKGRQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 540 LAlELYKQRSLL-------VMGRGYNyatclEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKC 612
Cdd:PRK11382 201 LG-ELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTT 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 613 QNALQQVTARQGRPIILCSKEDTESSKfayktielphtvDCLQGILSVIPLQLLSFHLAVLRGYDVDFPR 682
Cdd:PRK11382 275 ERAINFVKQRTDNVIVIDYAEISQGLH------------PWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
383-498 |
7.73e-07 |
|
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: 48.69 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 383 GCGTSYHAA---VATRQVleelTELPvmvelaSDFLDrntP----------VFRDDVCFFISQSGETADTLMALRYCKER 449
Cdd:cd05014 7 GVGKSGHIArkiAATLSS----TGTP------AFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLLPHLKRR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2024354922 450 RALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFVSLVMF 498
Cdd:cd05014 74 GAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALG 122
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
97-194 |
1.33e-06 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 51.64 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 97 IAHTRWATHGVPSAinSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYmYDNREsedtsf 176
Cdd:PTZ00077 51 LAHERLAIVDLSDG--KQPLLDDDET-VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKE-YGPKD------ 120
|
90
....*....|....*...
gi 2024354922 177 salverVIQQLEGAFALV 194
Cdd:PTZ00077 121 ------FWNHLDGMFATV 132
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
92-158 |
1.41e-05 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 47.27 E-value: 1.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024354922 92 ETHFGIAHTRWATHGVPSAINSHPQRsdkGNEFVVIHNGIITNYKDLRKFLESK-----GYEFESETDTETI 158
Cdd:COG0121 75 KSRLVIAHVRKATVGPVSLENTHPFR---GGRWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELA 143
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
423-498 |
5.29e-05 |
|
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: 45.74 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 423 RDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDcgVHINAGPE-----IGVASTkayTSQFVSLVM 497
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
.
gi 2024354922 498 F 498
Cdd:COG0794 166 G 166
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
90-213 |
2.82e-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: 43.47 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 90 DFETHFGIAHTRWATHGVPSAINSHP-QRSDKGNEFVVIHNGIITNYKDLRkfleSKGYEFESETDTETI-----PKLIK 163
Cdd:pfam13230 68 PIRSRNVIAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNGDLKGYAPKL----SGRFQPVGSTDSELAfcwllDRLAS 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2024354922 164 YMYDNRESEDTSFSALVE--RVIQQLeGAFALVFKSihypGEAVATRRGSPL 213
Cdd:pfam13230 144 RFPYARPSAGELFRALRElaREIAAH-GTFNFLLSD----GRDLFAHCSTRL 190
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
12-158 |
3.56e-04 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 43.74 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 12 GIFAYLNyrVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNnnedkerfiklvkkrgkvkaleeelykqdgldskadf 91
Cdd:PRK09431 3 GIFGILD--IKTDADELRKKALEMSRLMRHRGPDWSGIYASDN------------------------------------- 43
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024354922 92 ethfGI-AHTRWATHGVPSAinSHPQRSDKGNEfVVIHNGIITNYKDLRKFLESKgYEFESETDTETI 158
Cdd:PRK09431 44 ----AIlGHERLSIVDVNGG--AQPLYNEDGTH-VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVI 103
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
97-212 |
5.71e-04 |
|
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: 42.38 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024354922 97 IAHTRWATHGVPSAINSHPQRSDkgnEFVVIHNGIITNYKDLR-KFLESKGYEFESETDTETIPKLI-KYMYDNRESEDT 174
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRrRLLRLLPRLPVGTTDSELAFALLlSRLLERDPLDPA 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2024354922 175 SFSALVERVIQQLE-----GAFALVFKSihypGEA-VATRRGSP 212
Cdd:cd01908 161 ELLDAILQTLRELAalappGRLNLLLSD----GEYlIATRYASA 200
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
424-498 |
5.73e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 42.37 E-value: 5.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024354922 424 DDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF 498
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
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| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
550-603 |
7.73e-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: 38.89 E-value: 7.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2024354922 550 LLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGP-LALIDKQMPVIMVI 603
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALS 55
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