|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-677 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 1443.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFAYLNFHANKERRYILDVLFNGLRRLEYRGYDSAGIAIDN--SSPSSSPLVFRQAGNIESLVNSVNEEITNTDLNL 78
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNdpSLESSSPLVFREEGKIESLVRSVYEEVAETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 79 DEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFD 158
Cdd:PLN02981 81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 159 KANEEGGqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKELDQGESNSHVFQDAHFLSKN-DHPK 237
Cdd:PLN02981 161 KLNEEEG-DVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELPEEKNSSAVFTSEGFLTKNrDKPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 238 EFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERGRCNG-LSRPASVERALSVLEMEVEQISKGKYDHYMQ 316
Cdd:PLN02981 240 EFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGgLSRPASVERALSTLEMEVEQIMKGNYDHYMQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 317 KEIHEQPESLTTTMRGRLIRGGSRKTKTVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIAS 396
Cdd:PLN02981 320 KEIHEQPESLTTTMRGRLIRGGSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 397 DLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQI 476
Cdd:PLN02981 400 DLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 477 VVMVMLALAIGSDTISSQKRREAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEV 556
Cdd:PLN02981 480 VAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 557 ALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSSSGSCRAIEVPQV 636
Cdd:PLN02981 560 ALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCPSGGCRVIEVPQV 639
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 334185586 637 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 677
Cdd:PLN02981 640 EDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-675 |
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: 735.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFAYLnfhANKErryILDVLFNGLRRLEYRGYDSAGIAIDNSSpssSPLVFRQAGNIESLVNSVNEEITNTdlnlde 80
Cdd:COG0449 1 MCGIVGYI---GKRD---AAPILLEGLKRLEYRGYDSAGIAVLDDG---GLEVRKAVGKLANLEEKLAEEPLSG------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 81 vfyfHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLakfvFDKA 160
Cdd:COG0449 66 ----TIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHL----IEEY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 161 NEEGGqtvTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVkeldqGEsnshvfqdahflskndhpKEFF 240
Cdd:COG0449 137 LKGGG---DLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL-----GE------------------GENF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 241 LSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERgrcnglsrpasVERALSVLEMEVEQISKGKYDHYMQKEIH 320
Cdd:COG0449 191 LASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEP-----------VEREVKTVDWDAEAAEKGGYPHFMLKEIH 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 321 EQPESLTTTMRGRLIRGGsrktkTVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWD 400
Cdd:COG0449 260 EQPEAIRDTLRGRLDEDG-----RVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRY 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 401 RQgPIYREDT-AVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVM 479
Cdd:COG0449 335 RD-PVVDPGTlVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAAL 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 480 VMLALAIGSD--TISSQKRREaIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVA 557
Cdd:COG0449 414 YLLALYLARArgTLSAEEEAE-LLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEIS 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 558 LMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAAsvSSSGSCRAIEVPQVE 637
Cdd:COG0449 493 YIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEE--VEELADDVIEVPEVD 570
|
650 660 670
....*....|....*....|....*....|....*...
gi 334185586 638 DCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:COG0449 571 ELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVT 608
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-677 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 698.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFAYLNFHANKERRYILDVLFNGLRRLEYRGYDSAGIAIDN------------SSPSSSPLVFRQAGNIESLVNSV- 67
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDAnigsekedgtaaSAPTPRPCVVRSVGNISQLREKVf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 68 NEEITNTDLNLDEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTE 147
Cdd:PTZ00394 81 SEAVAATLPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGE-FTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 148 VIPKLAKFVFDKANeeggqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKeldQGESNSHVFQ-D 226
Cdd:PTZ00394 160 VISVLSEYLYTRKG-----IHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR---RTDDRGCVMKlQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 227 AHFLSKNDHPKEFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGvsiLKFENERGRCNGLsrpasVERALSVLEMEVEQI 306
Cdd:PTZ00394 232 TYDLTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGA---LRFYNAAERQRSI-----VKREVQHLDAKPEGL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 307 SKGKYDHYMQKEIHEQPESLTTTMRGRLirggSRKTKTVLLGGLKDH-LKTIRRSRRIVFIGCGTSYNAALASRPILEEL 385
Cdd:PTZ00394 304 SKGNYPHFMLKEIYEQPESVISSMHGRI----DFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPLFEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 386 SGIPVSMEIASDLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIG 465
Cdd:PTZ00394 380 VPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 466 VASTKAYTSQIVVMVMLALAIGSDTISSQKRREAIIDGLLDLPYKVKEVLKL-DDEMKDLAQLLIDEQSLLVFGRGYNYA 544
Cdd:PTZ00394 460 VASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYDLA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 545 TALEGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSS 624
Cdd:PTZ00394 540 TAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAA 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 334185586 625 SGSCraIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 677
Cdd:PTZ00394 620 ASEI--VLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-675 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 687.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFAYLnfhANKErryILDVLFNGLRRLEYRGYDSAGIA-IDNSSPSssplVFRQAGNIESLVNSVNEEITNTdlnld 79
Cdd:PRK00331 1 MCGIVGYV---GQRN---AAEILLEGLKRLEYRGYDSAGIAvLDDGGLE----VRKAVGKVANLEAKLEEEPLPG----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 80 evfyfHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLakfvFDK 159
Cdd:PRK00331 66 -----TTGIGHTRWATHGKPTERNAHPHTDCSGR-IAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHL----IEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 160 ANEEGGQTVtfcEVVFEVMRHLEGAYAL--IFKSwhYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpK 237
Cdd:PRK00331 136 ELKEGGDLL---EAVRKALKRLEGAYALavIDKD--EPDTIVAARNGSPLVIGLGE-----------------------G 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 238 EFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERgrcnglsrpasVERALSVLEMEVEQISKGKYDHYMQK 317
Cdd:PRK00331 188 ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNP-----------VEREVYTVDWDASAAEKGGYRHFMLK 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 318 EIHEQPESLTTTMRGRLIrggsrktktvLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASD 397
Cdd:PRK00331 257 EIYEQPEAIRDTLEGRLD----------ELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASE 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 398 LWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIV 477
Cdd:PRK00331 327 FRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLA 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 478 VMVMLALAIGSD--TISSQKRREaIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKE 555
Cdd:PRK00331 407 VLYLLALALAKArgTLSAEEEAD-LVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLKE 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 556 VALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAAsvsSSGSCRAIEVPQ 635
Cdd:PRK00331 486 ISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEV---AEEADDVIEVPE 562
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 334185586 636 VEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:PRK00331 563 VHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVT 602
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-675 |
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: 618.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIFAYLNfhankeRRYILDVLFNGLRRLEYRGYDSAGIA-IDNSSPSssplVFRQAGNIESLVNSVNEEitntdlnldE 80
Cdd:TIGR01135 1 CGIVGYIG------QRDAVPILLEGLKRLEYRGYDSAGIAvVDEGKLF----VRKAVGKVAELANKLGEK---------P 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 81 VFYFhAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvfdka 160
Cdd:TIGR01135 62 LPGG-VGIGHTRWATHGKPTDENAHPHTDEGGR-IAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLI------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 161 NEEGGQTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpKEFF 240
Cdd:TIGR01135 133 EEELREGGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGLGD-----------------------GENF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 241 LSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENERgrcnglsrpasVERALSVLEMEVEQISKGKYDHYMQKEIH 320
Cdd:TIGR01135 190 VASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAP-----------VQREVRVIDWDLDAAEKGGYRHFMLKEIY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 321 EQPESLTTTMRGRLIRGGsrktKTVLLGGLKDHLKTIRRsrrIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWD 400
Cdd:TIGR01135 259 EQPRALRDTLEGRIEENG----GVFEELGAEELLKNIDR---IQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 401 RQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMV 480
Cdd:TIGR01135 332 RKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLY 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 481 MLALAIGSDT-ISSQKRREAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVALM 559
Cdd:TIGR01135 412 LLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYI 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 560 HSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAASVSSSGScrAIEVPQVEDC 639
Cdd:TIGR01135 492 HAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADD--VIKLPEVEEL 569
|
650 660 670
....*....|....*....|....*....|....*.
gi 334185586 640 LQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:TIGR01135 570 LAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVT 605
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-676 |
3.01e-157 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 467.96 E-value: 3.01e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFAYLnfhANKERRyilDVLFNGLRRLEYRGYDSAGIAIDNSSPSsspLVFRQAGNIESLVNSVN---EEITNTDLN 77
Cdd:PTZ00295 24 CCGIVGYL---GNEDAS---KILLEGIEILQNRGYDSCGISTISSGGE---LKTTKYASDGTTSDSIEilkEKLLDSHKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 78 ldevfyFHAGIAHTRWATHGEPAPRNSHPQSSgPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVF 157
Cdd:PTZ00295 95 ------STIGIAHTRWATHGGKTDENAHPHCD-YKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 158 DkaneeggQTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpK 237
Cdd:PTZ00295 168 D-------QGEDFQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGD-----------------------D 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 238 EFFLSSDPHALVEHTKKVLVIEDGEVVNLKDGGVSILKFENErgrcnglsrpasVERalsvLEMEVEQISKGKYDHYMQK 317
Cdd:PTZ00295 218 SIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRR------------VEK----IPEEVIEKSPEPYPHWTLK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 318 EIHEQPESLTTTM--RGRLIRGGSRktktVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALASRPILEELSGI-PVSMEI 394
Cdd:PTZ00295 282 EIFEQPIALSRALnnGGRLSGYNNR----VKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVID 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 395 ASDLwDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTS 474
Cdd:PTZ00295 358 ASEL-TLYRLPDEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTS 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 475 QIVVMVMLALAIGS--DTISSQKRREAIIDGLLDLPYKVKEVLKL-DDEMKDLAQLLIDEQSLLVFGRGYNYATALEGAL 551
Cdd:PTZ00295 437 QVTVLSLIALWFAQnkEYSCSNYKCSSLINSLHRLPTYIGMTLKScEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGAL 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 552 KVKEVALMHSEGILAGEMKHGPLALVDE--NLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCskgDAASVSSSGSCR 629
Cdd:PTZ00295 517 KIKEITYIHAEGFSGGALKHGPFALIDKekNTPVILIILDDEHKELMINAAEQVKARGAYIIVIT---DDEDLVKDFADE 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 334185586 630 AIEVPQVeDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTT 676
Cdd:PTZ00295 594 IILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-264 |
5.04e-101 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 307.84 E-value: 5.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIFAYLNFhankerRYILDVLFNGLRRLEYRGYDSAGIAIDNSSpssSPLVFRQAGNIESLVNSVNEEITNtdlnldev 81
Cdd:cd00714 1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---SLEVVKAVGKVANLEEKLAEKPLS-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 82 fyFHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFDKan 161
Cdd:cd00714 64 --GHVGIGHTRWATHGEPTDVNAHPHRSCDGE-IAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDG-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 162 eeggqTVTFCEVVFEVMRHLEGAYALIFKSWHYPNELIACKLGSPLLLGVKEldqgesnshvfqdahflskndhpKEFFL 241
Cdd:cd00714 139 -----GLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGD-----------------------GENFV 190
|
250 260
....*....|....*....|...
gi 334185586 242 SSDPHALVEHTKKVLVIEDGEVV 264
Cdd:cd00714 191 ASDAPALLEHTRRVIYLEDGDIA 213
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
317-676 |
3.70e-74 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 242.11 E-value: 3.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 317 KEIHEQPESLtttmrgrlirggsRKTKTVLLGGLKDHLKTIRRS--RRIVFIGCGTSYNAALASRPILEELSGIPVSMEI 394
Cdd:COG2222 2 REIAQQPEAW-------------RRALAALAAAIAALLARLRAKppRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 395 ASDLWDRQGPIYREDTAVF-VSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYT 473
Cdd:COG2222 69 PSELVVYPAYLKLEGTLVVaISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 474 SQIVVMVMLALAIGSDtissqkrrEAIIDGLLDLPYKVKEVLKLDDEMKDLAQLLiDEQSLLVFGRGYNYATALEGALKV 553
Cdd:COG2222 149 TMLLALLALLAAWGGD--------DALLAALDALPAALEAALAADWPAAALAALA-DAERVVFLGRGPLYGLAREAALKL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 554 KEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQSVIQQLHARKGRLIVMCSKGDAasvsssgscrAIEV 633
Cdd:COG2222 220 KELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDA----------AITL 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 334185586 634 PQVEDC---LQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTT 676
Cdd:COG2222 290 PAIPDLhdaLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKT 335
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
519-675 |
4.70e-64 |
|
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: 208.66 E-value: 4.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 519 DEMKDLAQLLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQS 598
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185586 599 VIQQLHARKGRLIVMCSKGDAasvsSSGSCRAIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVT 675
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDA----KDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
362-487 |
1.45e-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: 195.79 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 362 RIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGPIYREDTAVFVSQSGETADTLLALDYARENGALCVGIT 441
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 334185586 442 NTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMVMLALAIG 487
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-264 |
6.93e-50 |
|
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: 173.40 E-value: 6.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIFAYLNFHANKERRYILDvlFNGLRRLEYRGYDSAGIAIDNSSPSSSPLVFRQAGNIEslvnsvneeitntDLNLDEV 81
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLL--LRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVA-------------LDLLDEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 82 FYFHAGIAHTRWATHGEPAPRNSHPQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvfdkan 161
Cdd:cd00352 66 LKSGVALGHVRLATNGLPSEANAQPFRSEDGR-IALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLL-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 162 EEGGQTVTFCEVVFEVMRHLEGAYALIFKSwHYPNELIAC--KLG-SPLLLGVkeldqgesnshvfqdahflsknDHPKE 238
Cdd:cd00352 137 ERLGREGGLFEAVEDALKRLDGPFAFALWD-GKPDRLFAArdRFGiRPLYYGI----------------------TKDGG 193
|
250 260
....*....|....*....|....*..
gi 334185586 239 FFLSSDPHALVEHT-KKVLVIEDGEVV 264
Cdd:cd00352 194 LVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
357-485 |
1.06e-37 |
|
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: 136.66 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 357 IRRSRRIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQ-GPIYREDTAVFVSQSGETADTLLALDYARENGA 435
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 334185586 436 LCVGITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTSQIVVMVMLALA 485
Cdd:pfam01380 82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-215 |
5.79e-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: 92.91 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIFA-YLNFHANKerryildVLFNGLRRLEYRGYDSAGIAIDNSSpsssplVFRQ-AGNieSLVNSV-NEEITNtdlNL 78
Cdd:cd00715 1 CGVFGiYGAEDAAR-------LTYLGLYALQHRGQESAGIATSDGK------RFHThKGM--GLVSDVfDEEKLR---RL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 79 DEvfyfHAGIAHTRWATHGEPAPRNSHPQSSG-PGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvf 157
Cdd:cd00715 63 PG----NIAIGHVRYSTAGSSSLENAQPFVVNsPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLI---- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185586 158 dkANEEGGQTVTfcEVVFEVMRHLEGAYALIFKSwhyPNELIACK--LG-SPLLLGVKELD 215
Cdd:cd00715 135 --ARSLAKDDLF--EAIIDALERVKGAYSLVIMT---ADGLIAVRdpHGiRPLVLGKLEGD 188
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
527-660 |
9.54e-21 |
|
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: 88.51 E-value: 9.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 527 LLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQQsVIQQLHAR 606
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 334185586 607 KGRLIVMCSKGDaaSVSSSGSCRAIEVPQVEDCLQPVINIVPLQLLAYHLTVLR 660
Cdd:pfam01380 80 GAKIIAITDSPG--SPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-213 |
1.34e-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: 92.39 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFA-YLNFHANKerryildVLFNGLRRLEYRGYDSAGIAidnSSPSSSPLVFRQAGniesLVNSV-NEEITNtdlNL 78
Cdd:COG0034 7 ECGVFGiYGHEDVAQ-------LTYYGLYALQHRGQESAGIA---TSDGGRFHLHKGMG----LVSDVfDEEDLE---RL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 79 DEvfyfHAGIAHTRWATHGEPAPRNSHP-QSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKL-AKFV 156
Cdd:COG0034 70 KG----NIAIGHVRYSTTGSSSLENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLiAREL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 157 FDKaneeggqtvTFCEVVFEVMRHLEGAYALIFKSwhyPNELIACK--LG-SPLLLGVKE 213
Cdd:COG0034 146 TKE---------DLEEAIKEALRRVKGAYSLVILT---GDGLIAARdpNGiRPLVLGKLE 193
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-292 |
1.16e-16 |
|
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: 83.14 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIFAYLNfHANKERRYILDvlfnGLRRLEYRGYDSAGIAIDNSSpssSPLVFRQAGniesLVNSVNEEITNTDLNLdev 81
Cdd:TIGR01134 1 CGVVGIYG-QEEVAASLTYY----GLYALQHRGQESAGISVFDGN---RFRLHKGNG----LVSDVFNEEHLQRLKG--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 82 fyfHAGIAHTRWATHGEPAPRNSHP--QSSGPGDDfLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKFVFDk 159
Cdd:TIGR01134 66 ---NVGIGHVRYSTAGSSGLENAQPfvVNSPYGGL-ALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 160 aneeggQTVTFCEVVFEVMRHLEGAYALIFKSWHypnELIACK--LG-SPLLLGVKEldqgesnshvfqdahflskndhp 236
Cdd:TIGR01134 141 ------SKDDLFDAVARVLERVRGAYALVLMTED---GLVAVRdpHGiRPLVLGRRG----------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185586 237 KEFFLSSDPHAL----VEHTKKVlviEDGEVVNLKDGGVSILKFENE-RGRCN----GLSRPASV 292
Cdd:TIGR01134 189 DGYVVASESCALdilgAEFVRDV---EPGEVVVIFDGGLESRQCARRpRAPCVfeyvYFARPDSV 250
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
85-189 |
1.02e-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: 433279 [Multi-domain] Cd Length: 130 Bit Score: 68.49 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 85 HAGIAHTRWATHGEPAPRNsHPQSSgPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAkfvfdkanEEG 164
Cdd:pfam13522 11 GVALGHVRLAIVDLPDAGN-QPMLS-RDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALY--------EEW 80
|
90 100
....*....|....*....|....*
gi 334185586 165 GQtvtfcevvfEVMRHLEGAYALIF 189
Cdd:pfam13522 81 GE---------DCLERLRGMFAFAI 96
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-189 |
1.83e-13 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 73.17 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFA-YLNFHANKErryildvLFNGLRRLEYRGYDSAGIAidnsspSSSPLVFRQ-AGNieSLVNSVNEEITNTDLNl 78
Cdd:PLN02440 1 ECGVVGiFGDPEASRL-------CYLGLHALQHRGQEGAGIV------TVDGNRLQSiTGN--GLVSDVFDESKLDQLP- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 79 devfyFHAGIAHTRWATHGEPAPRNSHPQSSG-PGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIpkLAKFVF 157
Cdd:PLN02440 65 -----GDIAIGHVRYSTAGASSLKNVQPFVANyRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVL--LHLIAI 137
|
170 180 190
....*....|....*....|....*....|..
gi 334185586 158 DKANeeggqtvTFCEVVFEVMRHLEGAYALIF 189
Cdd:PLN02440 138 SKAR-------PFFSRIVDACEKLKGAYSMVF 162
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-305 |
1.85e-13 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 73.14 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIF-AYLNfhankERRYILDVLFNGLRRLEYRGYDSAGIAIDNSSPSSsplVFRQAGniesLVNSV-NEEITNTdlnld 79
Cdd:PRK05793 15 CGVFgVFSK-----NNIDVASLTYYGLYALQHRGQESAGIAVSDGEKIK---VHKGMG----LVSEVfSKEKLKG----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 80 evFYFHAGIAHTRWATHGEPAPRNSHP-QSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLakfvFD 158
Cdd:PRK05793 78 --LKGNSAIGHVRYSTTGASDLDNAQPlVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNL----IA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 159 KANEEGgqtvtFCEVVFEVMRHLEGAYALIFKSwhyPNELIACKLGS---PLLLGVKELDqgesnshvfqdahflskndh 235
Cdd:PRK05793 152 RSAKKG-----LEKALVDAIQAIKGSYALVILT---EDKLIGVRDPHgirPLCLGKLGDD-------------------- 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185586 236 pkeFFLSSDPHAL-VEHTKKVLVIEDGEVVNLKDGGVSILKFEnERGRCNG-------LSRPASVERALSVLEMEVEQ 305
Cdd:PRK05793 204 ---YILSSESCALdTIGAEFIRDVEPGEIVIIDEDGIKSIKFA-EKTKCQTcafeyiyFARPDSVIDGISVYESRVRA 277
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
355-487 |
2.57e-13 |
|
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: 67.64 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 355 KTIRRSRRIVFIGCGTSYNAAlasrpilEELS------GIPVSMEIASDLW-DRQGPIYREDTAVFVSQSGETADTLLAL 427
Cdd:cd05013 8 DLLAKARRIYIFGVGSSGLVA-------EYLAykllrlGKPVVLLSDPHLQlMSAANLTPGDVVIAISFSGETKETVEAA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185586 428 DYARENGALCVGITNTVGSSIARKTHcgVHINAGAEIGVASTKAYTSQIVVMVML-ALAIG 487
Cdd:cd05013 81 EIAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLALIdALFLA 139
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-149 |
3.72e-13 |
|
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: 69.60 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIFAylnFHANKERRYILDVLFNGLRRLEYRG-YDSAGIAI----DNSSPSSSPL--VFRQAGNIESLVNSvneeitnt 74
Cdd:cd01907 1 CGIFG---IMSKDGEPFVGALLVEMLDAMQERGpGDGAGFALygdpDAFVYSSGKDmeVFKGVGYPEDIARR-------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185586 75 dLNLDEVFYFHaGIAHTRWATHGEPAPRNSHPQSSGpgdDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVI 149
Cdd:cd01907 70 -YDLEEYKGYH-WIAHTRQPTNSAVWWYGAHPFSIG---DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVI 139
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
357-504 |
7.51e-13 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 69.57 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 357 IRRSRRIVFIGCGTSYNAAlasrpilEELS------GIPVSM-EIASDLWDRQ-GPIYREDTAVFVSQSGETADTLLALD 428
Cdd:COG1737 131 LAKARRIYIFGVGASAPVA-------EDLAykllrlGKNVVLlDGDGHLQAESaALLGPGDVVIAISFSGYTRETLEAAR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 429 YARENGALCVGITNTVGSSIARktHCGVHINAGAEIGVASTKAYTSQIVVMVM-------LALAIGSDTISSQKRREAII 501
Cdd:COG1737 204 LAKERGAKVIAITDSPLSPLAK--LADVVLYVPSEEPTLRSSAFSSRVAQLALidalaaaVAQRDGDKARERLERTEALL 281
|
...
gi 334185586 502 DGL 504
Cdd:COG1737 282 SEL 284
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
362-453 |
1.22e-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: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 362 RIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGPIYREDT-AVFVSQSGETADTLLALDYARENGALCVGI 440
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKSvVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 334185586 441 TNTVGSSIARKTH 453
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
362-668 |
3.79e-10 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 61.94 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 362 RIVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGpiYRED---TAVFVSQSGETADTLLALDYARENGALCV 438
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTP--YRLDdrcAVIGVSDYGKTEEVIKALELGRACGALTA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 439 GITNTVGSSIARKTHCGVHINAGAEIGVASTKAYTsqiVVMVMLALAIGSDTISSQKrreaiiDGLLDLPYKVKEVLKL- 517
Cdd:PRK11382 124 AFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMITRLAPNAEIGKIK------NDLKQLPNALGHLVRTw 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 518 DDEMKDLAQLLIDEQSLLVFGRGYNYATAL-EGALKVKEVALMHSEGILAGEMKHGPLALVDENLPIAVIATRDACFSKQ 596
Cdd:PRK11382 195 EEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTT 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185586 597 QSVIQQLHARKGRLIVMcskgDAASVSSSgscraievpqVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPR 668
Cdd:PRK11382 275 ERAINFVKQRTDNVIVI----DYAEISQG----------LHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-152 |
3.87e-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: 62.93 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFAYLNFHANKERryilDVLFNGLRRLEYRGYDSAGIAIDNsspsssplvfrqagnieslvnsvneeitntdlnlde 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------ 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185586 81 vfyfHAGIAHTRWATHGEPAprNSH-PQSSgPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKL 152
Cdd:COG0367 41 ----GVALGHRRLSIIDLSE--GGHqPMVS-EDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
106-188 |
1.64e-09 |
|
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: 55.99 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 106 PQSSGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAKfvfdkanEEGGQtvtfcevvfEVMRHLEGAY 185
Cdd:pfam13537 15 PMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE-------AEWGE---------DCVDRLNGMF 78
|
...
gi 334185586 186 ALI 188
Cdd:pfam13537 79 AFA 81
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-152 |
2.83e-09 |
|
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: 57.57 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIFAYLNFHANKERRyilDVLFNGLRRLEYRGYDSAGIAIDNsspsssplvfrqagnieslvnsvneeitntdlnldev 81
Cdd:cd00712 1 CGIAGIIGLDGASVDR---ATLERMLDALAHRGPDGSGIWIDE------------------------------------- 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185586 82 fyfHAGIAHTRWATHGepaPRNSH-PQSSGPGDdFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKL 152
Cdd:cd00712 41 ---GVALGHRRLSIID---LSGGAqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL 105
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
395-482 |
1.81e-08 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 56.33 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 395 ASDLWDRQgpIYREDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVAST--KAY 472
Cdd:PRK05441 121 AADLKAIN--LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAG 198
|
90
....*....|
gi 334185586 473 TSQIVVMVML 482
Cdd:PRK05441 199 TAQKLVLNMI 208
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
361-486 |
2.44e-08 |
|
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: 52.93 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 361 RRIVFIGCGTSYnaalasrPILEELSGIPVSMEIAS-----------DLwdrqGPIYREDTAVFVSQSGETADTLLALDY 429
Cdd:cd05014 1 GKVVVTGVGKSG-------HIARKIAATLSSTGTPAfflhptealhgDL----GMVTPGDVVIAISNSGETDELLNLLPH 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185586 430 ARENGALCVGITNTVGSSIARktHCGVHINAGAE-----IGVASTkayTSQIVVMVML-ALAI 486
Cdd:cd05014 70 LKRRGAPIIAITGNPNSTLAK--LSDVVLDLPVEeeacpLGLAPT---TSTTAMLALGdALAV 127
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
2-149 |
4.54e-08 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 54.59 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 2 CGIFAYLnfhANKER--RYILDVLFNGLRRleyRGYDSA--------GIAIDNSSPSssPLVFRQAGNIESlvnsvneei 71
Cdd:COG0121 1 CRLLGYS---GNVPTdlEFLLLDPEHSLVR---QSGATRegphadgwGIGWYEGDGE--PRLYRDPLPAWS--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 72 tntDLNLDEV---FYFHAGIAHTRWATHGEPAPRNSHPQSsgpGDDFLVVHNGVITNYEVLKETL-----VRHGFTFESD 143
Cdd:COG0121 64 ---DPNLRLLarpIKSRLVIAHVRKATVGPVSLENTHPFR---GGRWLFAHNGQLDGFDRLRRRLaeelpDELYFQPVGT 137
|
....*.
gi 334185586 144 TDTEVI 149
Cdd:COG0121 138 TDSELA 143
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
49-149 |
9.38e-08 |
|
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: 53.93 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 49 SSPLVFRQAGNIESLVNsvneeitntDLNLDEVFYFHAGIAHTRWATHGEPAPRNSHPQSSGPgddFLVVHNGVITNYEV 128
Cdd:cd01908 54 GRPFRYRSPLPAWSDIN---------LESLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGR---WLFAHNGQLDGFRL 121
|
90 100
....*....|....*....|..
gi 334185586 129 LKETLVRHGFTF-ESDTDTEVI 149
Cdd:cd01908 122 LRRRLLRLLPRLpVGTTDSELA 143
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
363-441 |
2.01e-07 |
|
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: 48.91 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 363 IVFIGCGTSYNAALASRPILEELSGIPVSMEIASDLWDRQGPIY--REDTAVFVSQSGETADTLLALDYARENGALCVGI 440
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 334185586 441 T 441
Cdd:cd04795 81 T 81
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
409-486 |
7.14e-07 |
|
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: 50.98 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 409 DTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVAST--KAYTSQIVVMVML--AL 484
Cdd:cd05007 120 DVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQKLALNMLstAV 199
|
..
gi 334185586 485 AI 486
Cdd:cd05007 200 MI 201
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-155 |
3.23e-06 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 50.48 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 1 MCGIFAYLNfhaNKERRYILDVLFNGL-RRLEYRGYDSAGIAIDNSSPSSSplvfrqagNIeslvnsvneeitntdlnld 79
Cdd:PTZ00077 1 MCGILAIFN---SKGERHELRRKALELsKRLRHRGPDWSGIIVLENSPGTY--------NI------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 80 evfyfhagIAHTRWA-----THGEPAPRNSHPqssgpgddFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVIPKLAK 154
Cdd:PTZ00077 51 --------LAHERLAivdlsDGKQPLLDDDET--------VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYK 114
|
.
gi 334185586 155 F 155
Cdd:PTZ00077 115 E 115
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
109-149 |
6.25e-06 |
|
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: 49.25 E-value: 6.25e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 334185586 109 SGPGDDFLVVHNGVITNYEVLKETLVRHGFTFESDTDTEVI 149
Cdd:TIGR01536 62 SNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVI 102
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
355-486 |
1.47e-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: 47.66 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 355 KTIRRSR-RIVFIGCGTS-----YNAA-LASrpileelSGIPvSMEI----AS--DLwdrqGPIYREDTAVFVSQSGETA 421
Cdd:COG0794 38 ELILNCKgRVVVTGMGKSghiarKIAAtLAS-------TGTP-AFFLhpaeAShgDL----GMITPGDVVIAISNSGETE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185586 422 DTLLALDYARENGALCVGITNTVGSSIARktHCGVHINAGAE-----IGVASTkayTSQIVVMVML-ALAI 486
Cdd:COG0794 106 ELLALLPLLKRLGVPLIAITGNPDSTLAR--AADVVLDLPVEreacpLNLAPT---TSTTATLALGdALAV 171
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
408-453 |
2.51e-04 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 43.60 E-value: 2.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 334185586 408 EDTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTH 453
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLAD 233
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| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
409-486 |
8.47e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 41.99 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185586 409 DTAVFVSQSGETADTLLALDYARENGALCVGITNTVGSSIARKTHCGVHINAGAEIGVAST--KAYTSQIVVMVMLALAI 486
Cdd:PRK12570 129 DVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNMLSTAS 208
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|
| |
