|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-682 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 933.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDgnNNEDKERFIKLV-KKRGKVKALEEELYK---QDGL 76
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLVfREEGKIESLVRSVYEevaETDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 77 DSKADFETHFGIAHTRWATHGVPSAINSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYM 156
Cdd:PLN02981 79 NLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 157 YD--NRESEDTSFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRskyKLSTEQIPVLYRTCNIENMKNm 234
Cdd:PLN02981 159 FDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVK---ELPEEKNSSAVFTSEGFLTKN- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 235 cnsrmkrldsstclhavGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLE----RSASDDP-----SR 305
Cdd:PLN02981 235 -----------------RDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFEnekgRGGGGLSrpasvER 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 306 VIQTLQMELQQIMKGNFSAFMQKEIFEQPESVVNTMRGRV----NFENSTVLLGGLKDHLKEIRRCRRLIIIGCGTSYHA 381
Cdd:PLN02981 298 ALSTLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 382 AVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDC 461
Cdd:PLN02981 378 ALAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHC 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 462 GVHINAGPEIGVASTKAYTSQFVSLVMFGLMMSEDRISLQKRRREIISGLKSLPEMIKEVLSLDEKIHDLALELYKQRSL 541
Cdd:PLN02981 458 GVHINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSL 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 542 LVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILC 621
Cdd:PLN02981 538 LVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVIC 617
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024456341 622 SKEDtESSKFAYKT---IELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:PLN02981 618 SKGD-ASSVCPSGGcrvIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-682 |
0e+00 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 780.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLnyrvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVKALEEELykqdgldSKA 80
Cdd:COG0449 1 MCGIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGG------LEVRKAVGKLANLEEKL-------AEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 81 DFETHFGIAHTRWATHGVPSAINSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYDnr 160
Cdd:COG0449 62 PLSGTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLK-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 161 esEDTSFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyrtcnienmknmcnsrmk 240
Cdd:COG0449 139 --GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL-------------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 241 rldsstclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLERSASDdpsRVIQTLQMELQQIMKG 320
Cdd:COG0449 185 -----------GEG--ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE---REVKTVDWDAEAAEKG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 321 NFSAFMQKEIFEQPESVVNTMRGRVNfENSTVLLGGLKDHLKEIRRCRRLIIIGCGTSYHAAVATRQVLEELTELPVMVE 400
Cdd:COG0449 249 GYPHFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 401 LASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYT 480
Cdd:COG0449 328 IASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFT 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 481 SQFVSLVMFGLMMSEDRISL-QKRRREIISGLKSLPEMIKEVLSLDEKIHDLALELYKQRSLLVMGRGYNYATCLEGALK 559
Cdd:COG0449 408 TQLAALYLLALYLARARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALK 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 560 IKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDTESSKFAYKTIELP 639
Cdd:COG0449 488 LKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVP 567
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2024456341 640 HTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:COG0449 568 EVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-682 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 722.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLNYRvprtrkEIFETLIKGLQRLEYRGYDSAGVA-IDGNNnedkerfIKLVKKRGKVKALEEELykqdgldSK 79
Cdd:PRK00331 1 MCGIVGYVGQR------NAAEILLEGLKRLEYRGYDSAGIAvLDDGG-------LEVRKAVGKVANLEAKL-------EE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 80 ADFETHFGIAHTRWATHGVPSAINSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYdn 159
Cdd:PRK00331 61 EPLPGTTGIGHTRWATHGKPTERNAHPHTDCSG-RIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEEL-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 160 RESEDTsFSAlVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyrtcnienmknmcnsrm 239
Cdd:PRK00331 138 KEGGDL-LEA-VRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL------------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 240 krldsstclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLErsasDDP-SRVIQTLQMELQQIM 318
Cdd:PRK00331 185 ------------GEG--ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFD----GNPvEREVYTVDWDASAAE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 319 KGNFSAFMQKEIFEQPESVVNTMRGRVNFenstvlLGGLKDHLKEIRRCRRLIIIGCGTSYHAAVATRQVLEELTELPVM 398
Cdd:PRK00331 247 KGGYRHFMLKEIYEQPEAIRDTLEGRLDE------LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 399 VELASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKA 478
Cdd:PRK00331 321 VEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKA 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 479 YTSQFVSLVMFGLMMSEDRISLQKRR-REIISGLKSLPEMIKEVLSLDEKIHDLALELYKQRSLLVMGRGYNYATCLEGA 557
Cdd:PRK00331 401 FTAQLAVLYLLALALAKARGTLSAEEeADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGA 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 558 LKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDTESSKFAYkTIE 637
Cdd:PRK00331 481 LKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEADD-VIE 559
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2024456341 638 LPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:PRK00331 560 VPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-682 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 693.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNEDKERFIK---------LVKKRGKVKALEEELY 71
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAasaptprpcVVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 72 KQDG----LDSKADFETHFGIAHTRWATHGVPSAINSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTE 147
Cdd:PTZ00394 81 SEAVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNG-EFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 148 TIPKLIKYMYDNRESedTSFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRskyklsteqipvlyrtcn 227
Cdd:PTZ00394 160 VISVLSEYLYTRKGI--HNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 228 iENMKNMCNSRMKRLDSSTClhavgDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLERSASDDPSRVI 307
Cdd:PTZ00394 220 -RTDDRGCVMKLQTYDLTDL-----SGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 308 QTLQMELQQIMKGNFSAFMQKEIFEQPESVVNTMRGRVNFENSTVLLGGLKDH-LKEIRRCRRLIIIGCGTSYHAAVATR 386
Cdd:PTZ00394 294 QHLDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 387 QVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHIN 466
Cdd:PTZ00394 374 PLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLN 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 467 AGPEIGVASTKAYTSQFVSLVMFGLMMSEDRISLQKRRREIISGLKSLPEMIKEVLSL-DEKIHDLALELYKQRSLLVMG 545
Cdd:PTZ00394 454 AGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 546 RGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKED 625
Cdd:PTZ00394 534 RGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVD 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024456341 626 TESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:PTZ00394 614 AELKAAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-682 |
0e+00 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 644.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 2 CGIFAYLNyrvPRTRKEIfetLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVKALEEELykqdgldSKAD 81
Cdd:TIGR01135 1 CGIVGYIG---QRDAVPI---LLEGLKRLEYRGYDSAGIAVVDEGK------LFVRKAVGKVAELANKL-------GEKP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 82 FETHFGIAHTRWATHGVPSAINSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYdnRE 161
Cdd:TIGR01135 62 LPGGVGIGHTRWATHGKPTDENAHPHTDEGG-RIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEEL--RE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 162 SEDTSFSalVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyrtcnienmknmcnsrmkr 241
Cdd:TIGR01135 139 GGDLLEA--VQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGL--------------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 242 ldsstclhavGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKLSIHRLERSASDDPSRVIQtlqMELQQIMKGN 321
Cdd:TIGR01135 184 ----------GDG--ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVID---WDLDAAEKGG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 322 FSAFMQKEIFEQPESVVNTMRGRVNFENSTVLLGGLKDHLKEIRRCRRLiiiGCGTSYHAAVATRQVLEELTELPVMVEL 401
Cdd:TIGR01135 249 YRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNIDRIQIV---ACGTSYHAGLVAKYLIERLAGIPVEVEI 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 402 ASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTS 481
Cdd:TIGR01135 326 ASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTT 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 482 QFVSLVMFGLMMSEDR-ISLQKRRREIISGLKSLPEMIKEVLSLDEKIHDLALELYKQRSLLVMGRGYNYATCLEGALKI 560
Cdd:TIGR01135 406 QLTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKL 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 561 KEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDTESSKFAYKTIELPH 640
Cdd:TIGR01135 486 KEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPE 565
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2024456341 641 TVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:TIGR01135 566 VEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-681 |
2.82e-155 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 462.95 E-value: 2.82e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLnyrvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNEDKerFIKLVKKRGKVKALEeeLYKQDGLDSKA 80
Cdd:PTZ00295 24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGISTISSGGELK--TTKYASDGTTSDSIE--ILKEKLLDSHK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 81 DfeTHFGIAHTRWATHGVPSAINSHPQrSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYDNR 160
Cdd:PTZ00295 94 N--STIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 161 ESedtsFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRSKyklsteqipvlyrtcnienmknmcnsrmk 240
Cdd:PTZ00295 171 ED----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDD----------------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 241 rldsstclhavgdkavEFFFASDASAIIEHTNRVIFLEDDDIAAVTDGKlsIHRLERsasddPSRVIQtLQMELQQIMKG 320
Cdd:PTZ00295 218 ----------------SIYVASEPSAFAKYTNEYISLKDGEIAELSLEN--VNDLYT-----QRRVEK-IPEEVIEKSPE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 321 NFSAFMQKEIFEQPESVVNTM--RGRVNFENSTVLLGGLKDHLKEIRRCRRLIIIGCGTSYHAAVATRQVLEELTEL-PV 397
Cdd:PTZ00295 274 PYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 398 MVELASDF-LDRNTpvfRDDVCF-FISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVAS 475
Cdd:PTZ00295 354 QVIDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVAS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 476 TKAYTSQFVSLVMFGLMMSE--DRISLQKRRREIISGLKSLPEMIKEVL-SLDEKIHDLALELYKQRSLLVMGRGYNYAT 552
Cdd:PTZ00295 431 TKAFTSQVTVLSLIALWFAQnkEYSCSNYKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKNAKSMFILGKGLGYPI 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 553 CLEGALKIKEITYMHSEGILAGELKHGPLALID--KQMPVIMVIMKDPCFTKCQNALQQVTARQGRPIILCSKEDtESSK 630
Cdd:PTZ00295 511 ALEGALKIKEITYIHAEGFSGGALKHGPFALIDkeKNTPVILIILDDEHKELMINAAEQVKARGAYIIVITDDED-LVKD 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2024456341 631 FAYKTIELPhTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTV 681
Cdd:PTZ00295 590 FADEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-285 |
3.88e-114 |
|
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: 341.73 E-value: 3.88e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 2 CGIFAYLNYRvprtrkEIFETLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVKALEEELYKQDGldskad 81
Cdd:cd00714 1 CGIVGYIGKR------EAVDILLEGLKRLEYRGYDSAGIAVIGDGS------LEVVKAVGKVANLEEKLAEKPL------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 82 fETHFGIAHTRWATHGVPSAINSHPQRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYDnre 161
Cdd:cd00714 63 -SGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 162 sEDTSFSALVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyrtcnienmknmcnsrmkr 241
Cdd:cd00714 138 -GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGI--------------------------------- 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2024456341 242 ldsstclhavgdKAVEFFFASDASAIIEHTNRVIFLEDDDIAAV 285
Cdd:cd00714 184 ------------GDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
526-680 |
2.24e-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: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 526 EKIHDLALELYKQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQN 605
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024456341 606 ALQQVTARQGRPIILCSKEDTEssKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVT 680
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAK--DLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
328-682 |
1.44e-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: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 328 KEIFEQPESVVNTmrgrvnFENSTVLLGGLKDHLKEIRRCRRLIIiGCGTSYHAAVATRQVLEELTELPVMVELASDFLD 407
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPPRRVVLV-GAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 408 RNTPVFRD-DVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSL 486
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 487 VM-FGLMMSEDrislqkrrrEIISGLKSLPEMIKEVLSLDEKIHDLAlELYKQRSLLVMGRGYNYATCLEGALKIKEITY 565
Cdd:COG2222 155 LAlLAAWGGDD---------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 566 MHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQNALQQVtARQGRPIILCSKEDTEsskfaykTIELPHTVDC- 644
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAEL-RALGARVVAIGAEDDA-------AITLPAIPDLh 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2024456341 645 --LQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 682
Cdd:COG2222 297 daLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
374-494 |
9.10e-60 |
|
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: 9.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 374 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGS 453
Cdd:cd05008 6 GCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGS 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2024456341 454 SISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFGLMMS 494
Cdd:cd05008 86 TLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-283 |
5.93e-54 |
|
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: 184.57 E-value: 5.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 2 CGIFAYLNYRVPRTRKEIfeTLIKGLQRLEYRGYDSAGVAIDGNNNEDKERFIKLVKKRGKVKALEEelykqdgldskad 81
Cdd:cd00352 1 CGIFGIVGADGAASLLLL--LLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEP------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 82 FETHFGIAHTRWATHGVPSAINSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYDNRE 161
Cdd:cd00352 66 LKSGVALGHVRLATNGLPSEANAQPFRSEDGR-IALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 162 SEDTsfsalVERVIQQLEGAFALVFKSIHyPGEAVATRRG---SPLLIGVRskyklsteqipvlyrtcnienmknmcnsr 238
Cdd:cd00352 145 LFEA-----VEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGIT----------------------------- 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2024456341 239 mkrldsstclhavgdKAVEFFFASDASAIIEHT-NRVIFLEDDDIA 283
Cdd:cd00352 190 ---------------KDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
374-492 |
8.26e-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: 8.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 374 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVG 452
Cdd:pfam01380 12 GRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPG 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2024456341 453 SSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFGLM 492
Cdd:pfam01380 92 SPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
534-665 |
3.98e-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: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 534 ELYKQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKCQnALQQVTAR 613
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2024456341 614 QGRPIILCSKEDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLR 665
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-186 |
5.02e-23 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 98.69 E-value: 5.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 2 CGIFAYLNyrvprtRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVkaleEELYKQDGLDSkad 81
Cdd:cd00715 1 CGVFGIYG------AEDAARLTYLGLYALQHRGQESAGIATSDGKR------FHTHKGMGLV----SDVFDEEKLRR--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 82 FETHFGIAHTRWATHGVPSAINSHP--QRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKymydn 159
Cdd:cd00715 62 LPGNIAIGHVRYSTAGSSSLENAQPfvVNSPLG-GIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA----- 135
|
170 180
....*....|....*....|....*..
gi 2024456341 160 RESEDTSFSALVERVIQQLEGAFALVF 186
Cdd:cd00715 136 RSLAKDDLFEAIIDALERVKGAYSLVI 162
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-186 |
3.66e-22 |
|
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: 100.10 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLNyrvprtRKEIFETLIKGLQRLEYRGYDSAG-VAIDGNNnedkerfIKLVKKRGKVKaleeELYKQDGLDSk 79
Cdd:COG0034 7 ECGVFGIYG------HEDVAQLTYYGLYALQHRGQESAGiATSDGGR-------FHLHKGMGLVS----DVFDEEDLER- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 80 adFETHFGIAHTRWATHGVPSAINSHP--QRSDKGnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKymy 157
Cdd:COG0034 69 --LKGNIAIGHVRYSTTGSSSLENAQPfyVNSPFG-SIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA--- 142
|
170 180
....*....|....*....|....*....
gi 2024456341 158 dnRESEDTSFSALVERVIQQLEGAFALVF 186
Cdd:COG0034 143 --RELTKEDLEEAIKEALRRVKGAYSLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-217 |
3.26e-18 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 87.76 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 2 CGIFAYLNyrvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNNedkerfIKLVKKRGKVKaleeELYKQDGLDskaD 81
Cdd:TIGR01134 1 CGVVGIYG-----QEEVAASLTYYGLYALQHRGQESAGISVFDGNR------FRLHKGNGLVS----DVFNEEHLQ---R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 82 FETHFGIAHTRWATHGVPSAINSHPQRSDKGNEFVVI-HNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYmydNR 160
Cdd:TIGR01134 63 LKGNVGIGHVRYSTAGSSGLENAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAH---ND 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024456341 161 ESEDTSFSAlVERVIQQLEGAFALVFKSIHypgEAVATR--RG-SPLLIGVR-SKYKLSTE 217
Cdd:TIGR01134 140 ESKDDLFDA-VARVLERVRGAYALVLMTED---GLVAVRdpHGiRPLVLGRRgDGYVVASE 196
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-210 |
6.10e-18 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 87.04 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYlnYRVPRTRKEIFEtlikGLQRLEYRGYDSAG-VAIDGNnnedkeRFiKLVKKRGKVKaleeELYKQDGLDSk 79
Cdd:PLN02440 1 ECGVVGI--FGDPEASRLCYL----GLHALQHRGQEGAGiVTVDGN------RL-QSITGNGLVS----DVFDESKLDQ- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 80 adFETHFGIAHTRWATHGVPSAINSHPqrsdkgneFV---------VIHNGIITNYKDLRKFLESKGYEFESETDTETIP 150
Cdd:PLN02440 63 --LPGDIAIGHVRYSTAGASSLKNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456341 151 KLIkymydnreSEDTS---FSALVErVIQQLEGAFALVFKSihyPGEAVATR-----RgsPLLIGVRS 210
Cdd:PLN02440 133 HLI--------AISKArpfFSRIVD-ACEKLKGAYSMVFLT---EDKLVAVRdphgfR--PLVMGRRS 186
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
26-185 |
3.38e-15 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 78.54 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 26 GLQRLEYRGYDSAGVAI-DGnnnedkeRFIKLVKKRGKVkaleEELYKQDGLDSkadFETHFGIAHTRWATHGVPSAINS 104
Cdd:PRK05793 35 GLYALQHRGQESAGIAVsDG-------EKIKVHKGMGLV----SEVFSKEKLKG---LKGNSAIGHVRYSTTGASDLDNA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 105 HPQRSD-KGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKyMYDNRESEDtsfsALVErVIQQLEGAFA 183
Cdd:PRK05793 101 QPLVANyKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIA-RSAKKGLEK----ALVD-AIQAIKGSYA 174
|
..
gi 2024456341 184 LV 185
Cdd:PRK05793 175 LV 176
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
82-186 |
8.27e-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: 8.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 82 FETHFGIAHTRWATHGVPSAINsHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLikymydnre 161
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLPDAGN-QPMLSRDGR-LVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL--------- 76
|
90 100
....*....|....*....|....*
gi 2024456341 162 sedtsFSALVERVIQQLEGAFALVF 186
Cdd:pfam13522 77 -----YEEWGEDCLERLRGMFAFAI 96
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
90-185 |
1.92e-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: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 90 HTRWATHGVPSAInsHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYMYdnresedtsfsa 169
Cdd:pfam13537 1 HRRLSIIDLEGGA--QPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW------------ 66
|
90
....*....|....*.
gi 2024456341 170 lVERVIQQLEGAFALV 185
Cdd:pfam13537 67 -GEDCVDRLNGMFAFA 81
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-157 |
3.63e-14 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 72.69 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 2 CGIFAYLnyrvpRTRKEIF--ETLIKGLQRLEYRG-YDSAGVAIDGnnneDKERFIKLVKKR-GKVKAL--EEELYKQDG 75
Cdd:cd01907 1 CGIFGIM-----SKDGEPFvgALLVEMLDAMQERGpGDGAGFALYG----DPDAFVYSSGKDmEVFKGVgyPEDIARRYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 76 LDSkadFETHFGIAHTRWATHgvpSAIN---SHPQRSdkGNEFVViHNGIITNYKDLRKFLESKGYEFESETDTETIPKL 152
Cdd:cd01907 72 LEE---YKGYHWIAHTRQPTN---SAVWwygAHPFSI--GDIAVV-HNGEISNYGSNREYLERFGYKFETETDTEVIAYY 142
|
....*
gi 2024456341 153 IKYMY 157
Cdd:cd01907 143 LDLLL 147
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-185 |
4.73e-13 |
|
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: 68.74 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 2 CGIFAYLNYRvprTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNnnedkerfiklvkkrgkvkaleeelykqdgldskad 81
Cdd:cd00712 1 CGIAGIIGLD---GASVDRATLERMLDALAHRGPDGSGIWIDEG------------------------------------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 82 fethFGIAHTRWATHGVpsainSH---PQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLikYM-Y 157
Cdd:cd00712 42 ----VALGHRRLSIIDL-----SGgaqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL--YEeW 109
|
170 180
....*....|....*....|....*...
gi 2024456341 158 DnresedtsfsalvERVIQQLEGAFALV 185
Cdd:cd00712 110 G-------------EDCLERLNGMFAFA 124
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-185 |
1.09e-12 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 71.02 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLNYRVPRTRkeifETLIKGLQRLEYRGYDSAGVAIDGnnnedkerfiklvkkrgkvkaleeelykqdgldska 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 81 dfetHFGIAHTRWAThgVPSAINSH-PQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLikymydn 159
Cdd:COG0367 41 ----GVALGHRRLSI--IDLSEGGHqPMVSEDGR-YVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA------- 106
|
170 180
....*....|....*....|....*.
gi 2024456341 160 resedtsFSALVERVIQQLEGAFALV 185
Cdd:COG0367 107 -------YEEWGEDCLERLNGMFAFA 125
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
374-460 |
1.49e-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: 64.52 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 374 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFISQSGETADTLMALRYCKERRALTVGITNTVG 452
Cdd:cd05710 6 GCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDED 85
|
....*...
gi 2024456341 453 SSISRETD 460
Cdd:cd05710 86 SPLAKLAD 93
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
402-509 |
4.67e-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: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 402 ASDFLDRNTPvfRDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 479
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024456341 480 TSQFVSLVMF-------------GLM--MSEDRISLQKRRREIIS 509
Cdd:cd05007 186 TAQKLALNMLstavmirlgkvygNLMvdVRATNEKLRERAIRIVM 230
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
415-492 |
7.80e-10 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 60.57 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 415 DDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--G 490
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstG 211
|
..
gi 2024456341 491 LM 492
Cdd:PRK05441 212 VM 213
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
374-448 |
4.16e-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: 4.16e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024456341 374 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFISQSGETADTLMALRYCKERRALTVGIT 448
Cdd:cd04795 5 GIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAIT 81
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-185 |
4.17e-08 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 56.26 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLNYRVprTRKEIFETLIKGLQRLEYRGYDSAGVaidgnnnedkerfiklvkkrgKVKALEEELYkqdgldska 80
Cdd:PTZ00077 1 MCGILAIFNSKG--ERHELRRKALELSKRLRHRGPDWSGI---------------------IVLENSPGTY--------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 81 dfetHFgIAHTRWATHGVPSAinSHPQRSDKGNeFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIPKLIKYmYDNR 160
Cdd:PTZ00077 49 ----NI-LAHERLAIVDLSDG--KQPLLDDDET-VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKE-YGPK 119
|
170 180
....*....|....*....|....*
gi 2024456341 161 EsedtsfsalverVIQQLEGAFALV 185
Cdd:PTZ00077 120 D------------FWNHLDGMFATV 132
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
109-186 |
5.38e-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: 5.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456341 109 SDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIpkLIKYMYDNresedtsfsalvERVIQQLEGAFALVF 186
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 ... |
415-488 |
1.42e-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: 1.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024456341 415 DDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM 488
Cdd:cd05013 61 GDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
414-514 |
1.89e-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: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 414 RDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM----F 489
Cdd:COG1737 182 PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALidalA 259
|
90 100
....*....|....*....|....*
gi 2024456341 490 GLMMSEDRISLQKRRREIISGLKSL 514
Cdd:COG1737 260 AAVAQRDGDKARERLERTEALLSEL 284
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
374-673 |
2.96e-07 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 53.08 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 374 GCGTSYHAAVATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFI--SQSGETADTLMALRYCKERRALTVGITNTV 451
Cdd:PRK11382 51 ACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAAFTKRA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 452 GSSISRETDCGVHINAGPEIGVASTKAYTsqfVSLVMFGLMMSEDRISlqkrrrEIISGLKSLPEMIKE-VLSLDEKIHD 530
Cdd:PRK11382 130 DSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMITRLAPNAEIG------KIKNDLKQLPNALGHlVRTWEEKGRQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 531 LAlELYKQRSLL-------VMGRGYNyatclEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFTKC 603
Cdd:PRK11382 201 LG-ELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTT 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 604 QNALQQVTARQGRPIILCSKEDTESSKfayktielphtvDCLQGILSVIPLQLLSFHLAVLRGYDVDFPR 673
Cdd:PRK11382 275 ERAINFVKQRTDNVIVIDYAEISQGLH------------PWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
374-489 |
7.62e-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: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 374 GCGTSYHAA---VATRQVleelTELPvmvelaSDFLDrntP----------VFRDDVCFFISQSGETADTLMALRYCKER 440
Cdd:cd05014 7 GVGKSGHIArkiAATLSS----TGTP------AFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLLPHLKRR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2024456341 441 RALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFVSLVMF 489
Cdd:cd05014 74 GAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALG 122
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-149 |
9.03e-07 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 52.22 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 1 MCGIFAYLNyrVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNnnedkerfiklvkkrgkvkaleeelykqdgldska 80
Cdd:PRK09431 1 MCGIFGILD--IKTDADELRKKALEMSRLMRHRGPDWSGIYASDN----------------------------------- 43
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 81 dfethfGI-AHTRWATHGVPSAinSHPQRSDKGNEfVVIHNGIITNYKDLRKFLESKgYEFESETDTETI 149
Cdd:PRK09431 44 ------AIlGHERLSIVDVNGG--AQPLYNEDGTH-VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVI 103
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
83-149 |
1.39e-05 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 47.27 E-value: 1.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024456341 83 ETHFGIAHTRWATHGVPSAINSHPQRsdkGNEFVVIHNGIITNYKDLRKFLESK-----GYEFESETDTETI 149
Cdd:COG0121 75 KSRLVIAHVRKATVGPVSLENTHPFR---GGRWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELA 143
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
414-489 |
5.54e-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: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 414 RDDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDcgVHINAGPE-----IGVASTkayTSQFVSLVM 488
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
.
gi 2024456341 489 F 489
Cdd:COG0794 166 G 166
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
81-204 |
2.78e-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: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 81 DFETHFGIAHTRWATHGVPSAINSHP-QRSDKGNEFVVIHNGIITNYKDLRkfleSKGYEFESETDTETI-----PKLIK 154
Cdd:pfam13230 68 PIRSRNVIAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNGDLKGYAPKL----SGRFQPVGSTDSELAfcwllDRLAS 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2024456341 155 YMYDNRESEDTSFSALVE--RVIQQLeGAFALVFKSihypGEAVATRRGSPL 204
Cdd:pfam13230 144 RFPYARPSAGELFRALRElaREIAAH-GTFNFLLSD----GRDLFAHCSTRL 190
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
88-203 |
5.62e-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: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456341 88 IAHTRWATHGVPSAINSHPQRSDkgnEFVVIHNGIITNYKDLR-KFLESKGYEFESETDTETIPKLI-KYMYDNRESEDT 165
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRrRLLRLLPRLPVGTTDSELAFALLlSRLLERDPLDPA 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2024456341 166 SFSALVERVIQQLE-----GAFALVFKSihypGEA-VATRRGSP 203
Cdd:cd01908 161 ELLDAILQTLRELAalappGRLNLLLSD----GEYlIATRYASA 200
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
415-489 |
5.64e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 42.37 E-value: 5.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024456341 415 DDVCFFISQSGETADTLMALRYCKERRALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF 489
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
541-594 |
7.78e-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: 7.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2024456341 541 LLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGP-LALIDKQMPVIMVI 594
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALS 55
|
|
| |
