|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-615 |
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: 1003.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSDIAKNILVTGLKRMEYRGYDSSGVALEVGEGaaahLDVIRRVGKVAGLESELSNIDSDATCGIGHTRWAT 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGG----LEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 81 HGKPSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAETHDLMASVREACTHVVG 160
Cdd:COG0449 77 HGAPSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 161 AYGLAAVCADEPGVIAVARKDSPIVVGVGETGSYVASDVIALIDATRDVVVLEDGQFAKLTPAGVEYTDEAGNVIEPKVT 240
Cdd:COG0449 157 AYALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 241 HIDWDLDMAEKGGYPDFMLKEIHEQPRVVRDTLVGRMTPAGELDIDELGLSLEELNDIDRVYVIACGTSYHAGLIAKNLI 320
Cdd:COG0449 237 TVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 321 EGWARIPTEVEAASEFRYRNPIITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKANK 400
Cdd:COG0449 317 EELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 401 EIAVASTKSFIGQVVSLTLLALLLAQVKYRLTTKQARMLFRELSDTAEQIQWILDtQTEAVHEAALLCKDAQSALFVGRG 480
Cdd:COG0449 397 EIGVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLD-LEEQIEELAEKYADARNALFLGRG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 481 MGAAISYEGALKLKEVSYLHAEAYAAGEMKHGPIALIDLGFPVIAVATKSATYDKTVSNLMECKARGAKVIVVATEGDEE 560
Cdd:COG0449 476 INYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEE 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1801477804 561 INKIADCIIRVPAVRDVFSPITASVPLQLLAREVAILRGCDVDQPRNLAKSVTVE 615
Cdd:COG0449 556 VEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-615 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 930.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSDIAKNILVTGLKRMEYRGYDSSGVALeVGEGaaaHLDVIRRVGKVAGLESELSNIDSDATCGIGHTRWAT 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAV-LDDG---GLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 81 HGKPSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAETHDLMASVREACTHVVG 160
Cdd:PRK00331 77 HGKPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 161 AYGLAAVCADEPGVIAVARKDSPIVVGVGETGSYVASDVIALIDATRDVVVLEDGQFAKLTPAGVEYTDEAGNVIEPKVT 240
Cdd:PRK00331 157 AYALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 241 HIDWDLDMAEKGGYPDFMLKEIHEQPRVVRDTLVGRMTPAGELDIDElglslEELNDIDRVYVIACGTSYHAGLIAKNLI 320
Cdd:PRK00331 237 TVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELGEGELAD-----EDLKKIDRIYIVACGTSYHAGLVAKYLI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 321 EGWARIPTEVEAASEFRYRNPIITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKANK 400
Cdd:PRK00331 312 ESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 401 EIAVASTKSFIGQVVSLTLLALLLAQVKYRLTTKQARMLFRELSDTAEQIQWILDtQTEAVHEAALLCKDAQSALFVGRG 480
Cdd:PRK00331 392 EIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLD-LKEQIEELAEDFADARNALFLGRG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 481 MGAAISYEGALKLKEVSYLHAEAYAAGEMKHGPIALIDLGFPVIAVATKSATYDKTVSNLMECKARGAKVIVVATEGDEE 560
Cdd:PRK00331 471 VDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEV 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1801477804 561 InKIADCIIRVPAVRDVFSPITASVPLQLLAREVAILRGCDVDQPRNLAKSVTVE 615
Cdd:PRK00331 551 A-EEADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-615 |
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: 807.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 2 CGIVGYTGSDIAKNILVTGLKRMEYRGYDSSGVALeVGEGaaaHLDVIRRVGKVAGLESELSNIDSDATCGIGHTRWATH 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAV-VDEG---KLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 82 GKPSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAETHDLMASVREACTHVVGA 161
Cdd:TIGR01135 77 GKPTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 162 YGLAAVCADEPGVIAVARKDSPIVVGVGETGSYVASDVIALIDATRDVVVLEDGQFAKLTPAGVEYTDEAGNVIEPKVTH 241
Cdd:TIGR01135 157 YALAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 242 IDWDLDMAEKGGYPDFMLKEIHEQPRVVRDTLVGRMTPAGElDIDELGLSlEELNDIDRVYVIACGTSYHAGLIAKNLIE 321
Cdd:TIGR01135 237 IDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGG-VFEELGAE-ELLKNIDRIQIVACGTSYHAGLVAKYLIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 322 GWARIPTEVEAASEFRYRNPIITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKANKE 401
Cdd:TIGR01135 315 RLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 402 IAVASTKSFIGQVVSLTLLALLLAQVKYRLTTKQARMLFRELSDTAEQIQWILDtQTEAVHEAALLCKDAQSALFVGRGM 481
Cdd:TIGR01135 395 IGVASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLL-ADESIAELAERYADKRNFLFLGRGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 482 GAAISYEGALKLKEVSYLHAEAYAAGEMKHGPIALIDLGFPVIAVATKSATYDKTVSNLMECKARGAKVIVVATEGDEEI 561
Cdd:TIGR01135 474 GYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETI 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1801477804 562 NKIADCIIRVPAVRDVFSPITASVPLQLLAREVAILRGCDVDQPRNLAKSVTVE 615
Cdd:TIGR01135 554 ASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-614 |
3.12e-152 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 452.94 E-value: 3.12e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSDIAKNILVTGLKRMEYRGYDSSGVA-------LEVGEGAA--AHLDVIRRvgkvagLESELSNIDSDATC 71
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGIStissggeLKTTKYASdgTTSDSIEI------LKEKLLDSHKNSTI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 72 GIGHTRWATHGKPSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAETHDLMASV 151
Cdd:PTZ00295 98 GIAHTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 152 REACTHVVGAYGLAAVCADEPGVIAVARKDSPIVVGVGETGSYVASDVIALIDATRDVVVLEDGQFAKLTPAGVEYTDEA 231
Cdd:PTZ00295 178 KSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 232 GNVI-EPKVTHIdwdldmAEKGGYPDFMLKEIHEQPRVVRDTLV--GRMTPAGEL-DIDELGLSLEELNDIDRVYVIACG 307
Cdd:PTZ00295 258 RRVEkIPEEVIE------KSPEPYPHWTLKEIFEQPIALSRALNngGRLSGYNNRvKLGGLDQYLEELLNIKNLILVGCG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 308 TSYHAGLIAKNLIEGWARIPT-EVEAASEF-RYRNPiiTPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSP 385
Cdd:PTZ00295 332 TSYYAALFAASIMQKLKCFNTvQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 386 VARESDGVIYTKANKEIAVASTKSFIGQVVSLTLLALLLAQVKYRLT-TKQARMLFRELSDTAEQIQWILDTQTEAVHEA 464
Cdd:PTZ00295 410 IARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCsNYKCSSLINSLHRLPTYIGMTLKSCEEQCKRI 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 465 ALLCKDAQSALFVGRGMGAAISYEGALKLKEVSYLHAEAYAAGEMKHGPIALIDL--GFPVIAVATKSATYDKTVSNLME 542
Cdd:PTZ00295 490 AEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKekNTPVILIILDDEHKELMINAAEQ 569
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1801477804 543 CKARGAKVIVVaTEGDEEINKIADCIIRVPAVrDVFSPITASVPLQLLAREVAILRGCDVDQPRNLAKSVTV 614
Cdd:PTZ00295 570 VKARGAYIIVI-TDDEDLVKDFADEIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-615 |
4.16e-150 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 448.82 E-value: 4.16e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSDIAK------NILVTGLKRMEYRGYDSSGVALEVGEGAAAHLD-VIRRVGKVAGLE----SELSNIDSDA 69
Cdd:PLN02981 1 MCGIFAYLNYNVPRerrfilEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSSPlVFREEGKIESLVrsvyEEVAETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 70 T------CGIGHTRWATHGKPSVVNAHPHTSCDG-RIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYA 142
Cdd:PLN02981 81 DlvfenhAGIAHTRWATHGPPAPRNSHPQSSGPGnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 143 ETHDLMASVR------EACTHVVGAYGLAAVCADEPGVIAVARKDSPIVVGVGETGS----------------------- 193
Cdd:PLN02981 161 KLNEEEGDVTfsqvvmEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELPEeknssavftsegfltknrdkpke 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 194 -YVASDVIALIDATRDVVVLEDGQFAKLTPAGVE-YTDEAGNV-----------IEPKVTHIDWDLDMAEKGGYPDFMLK 260
Cdd:PLN02981 241 fFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGiYKFENEKGrgggglsrpasVERALSTLEMEVEQIMKGNYDHYMQK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 261 EIHEQPRVVRDTLVGRMTPAGELDIDE--LGLSLEELNDIDR---VYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASE 335
Cdd:PLN02981 321 EIHEQPESLTTTMRGRLIRGGSGKAKRvlLGGLKDHLKTIRRsrrIVFIGCGTSYNAALAARPILEELSGVPVTMELASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 336 FRYRN-PIITPTTLVVaVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKANKEIAVASTKSFIGQV 414
Cdd:PLN02981 401 LLDRQgPIYREDTAVF-VSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 415 VSLTLLALllaQVKYRLTTKQAR--MLFRELSDTAEQIQWILDTQTEaVHEAALLCKDAQSALFVGRGMGAAISYEGALK 492
Cdd:PLN02981 480 VAMTMLAL---ALGEDSISSRSRreAIIDGLFDLPNKVREVLKLDQE-MKELAELLIDEQSLLVFGRGYNYATALEGALK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 493 LKEVSYLHAEAYAAGEMKHGPIALIDLGFPVIAVATKSATYDKTVSNLMECKARGAKVIVVATEGDEEINKIAD-C-IIR 570
Cdd:PLN02981 556 VKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCPSGgCrVIE 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1801477804 571 VPAVRDVFSPITASVPLQLLAREVAILRGCDVDQPRNLAKSVTVE 615
Cdd:PLN02981 636 VPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-615 |
5.20e-142 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 427.76 E-value: 5.20e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSDIAK------NILVTGLKRMEYRGYDSSGVALEVGEGAAAHLD-----------VIRRVGKVAGL----- 58
Cdd:PTZ00394 1 MCGIFGYANHNVPRtveqilNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGtaasaptprpcVVRSVGNISQLrekvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 59 --ESELSNIDSDATC----GIGHTRWATHGKPSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEV 132
Cdd:PTZ00394 81 seAVAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 133 FAHLIEEAYAE--THDLMASVREACTHVVGAYGLAAVCADEPGVIAVARKDSPIVVGVGETGS----------------- 193
Cdd:PTZ00394 161 ISVLSEYLYTRkgIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRRTDDrgcvmklqtydltdlsg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 194 ----YVASDVIALIDATRDVVVLEDGQFAKLTPAGVEYTDEAG---NVIEPKVTHIDWDLDMAEKGGYPDFMLKEIHEQP 266
Cdd:PTZ00394 241 plevFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAErqrSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 267 RVVRDTLVGRMT-PAGELDIDELGLS-LEELNDIDRVYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASEFRYRNPIIT 344
Cdd:PTZ00394 321 ESVISSMHGRIDfSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 345 PTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKANKEIAVASTKSFIGQVVSLTLLALLL 424
Cdd:PTZ00394 401 RDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 425 AQVKYRLTTKQARMLfRELSDTAEQIQWILDTQTEAVHEAALLCKDAQSALFVGRGMGAAISYEGALKLKEVSYLHAEAY 504
Cdd:PTZ00394 481 SSDSVRLQERRNEII-RGLAELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 505 AAGEMKHGPIALIDLGFPVIAVATKSATYDKTVSNLMECKARGAKVIVVATEGDEEINKIADCIIRVPAVRDVFSPITAS 584
Cdd:PTZ00394 560 HSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQCVVNV 639
|
650 660 670
....*....|....*....|....*....|.
gi 1801477804 585 VPLQLLAREVAILRGCDVDQPRNLAKSVTVE 615
Cdd:PTZ00394 640 IPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-218 |
1.97e-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: 340.19 E-value: 1.97e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 2 CGIVGYTGSDIAKNILVTGLKRMEYRGYDSSGVALeVGEGaaaHLDVIRRVGKVAGLESELSNIDSDATCGIGHTRWATH 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAV-IGDG---SLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 82 GKPSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAETHDLMASVREACTHVVGA 161
Cdd:cd00714 77 GEPTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801477804 162 YGLAAVCADEPGVIAVARKDSPIVVGVGETGSYVASDVIALIDATRDVVVLEDGQFA 218
Cdd:cd00714 157 YALAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIA 213
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
259-615 |
4.19e-79 |
|
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: 253.67 E-value: 4.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 259 LKEIHEQPRVVRDTLvgrmtPAGELDIDELGLSLEELNDiDRVYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASEF-R 337
Cdd:COG2222 1 AREIAQQPEAWRRAL-----AALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 338 YRNPIITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKANKEIAVASTKSFIGQVVSL 417
Cdd:COG2222 75 YPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 418 TLLALLLaqvkyrlttKQARMLFRELSDTAEQIQWILDTQTEAVHEAALlcKDAQSALFVGRGMGAAISYEGALKLKEVS 497
Cdd:COG2222 155 LALLAAW---------GGDDALLAALDALPAALEAALAADWPAAALAAL--ADAERVVFLGRGPLYGLAREAALKLKELS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 498 YLHAEAYAAGEMKHGPIALIDLGFPVIAVATKSATYDKTVSNLMECKARGAKVIVVATEGDEEInkiadCIIRVPAVRDV 577
Cdd:COG2222 224 AGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAI-----TLPAIPDLHDA 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 1801477804 578 FSPITASVPLQLLAREVAILRGCDVDQPRNLAKSVTVE 615
Cdd:COG2222 299 LDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
459-613 |
1.33e-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: 209.04 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 459 EAVHEAALLCKDAQSALFVGRGMGAAISYEGALKLKEVSYLHAEAYAAGEMKHGPIALIDLGFPVIAVATKSATYDKTVS 538
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801477804 539 NLMECKARGAKVIVVATEGDEEinKIADCIIRVPAVRDVFSPITASVPLQLLAREVAILRGCDVDQPRNLAKSVT 613
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAK--DLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-218 |
7.72e-59 |
|
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: 196.13 E-value: 7.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 2 CGIVGYTGSDIAKNILVT----GLKRMEYRGYDSSGVALEVGEGaaahLDVIRRVGKVAGLESELSNIDSDATCGIGHTR 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDG----LFVEKRAGPVSDVALDLLDEPLKSGVALGHVR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 78 WATHGKPSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAEtHDLMASVREACTH 157
Cdd:cd00352 77 LATNGLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRE-GGLFEAVEDALKR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801477804 158 VVGAYGLAAVCADEPGVIAVARKD--SPIVVGVGETGSYV-ASDVIALIDAT-RDVVVLEDGQFA 218
Cdd:cd00352 156 LDGPFAFALWDGKPDRLFAARDRFgiRPLYYGITKDGGLVfASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
300-416 |
3.86e-56 |
|
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: 185.78 E-value: 3.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 300 RVYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASEFRYRNPIITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGIT 379
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1801477804 380 NVVGSPVARESDGVIYTKANKEIAVASTKSFIGQVVS 416
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLA 117
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-233 |
6.69e-35 |
|
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: 132.58 E-value: 6.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 2 CGIVGYTGSDIAKNILVTGLKRMEYRGYDSSGVAleVGEGAaaHLDVIRRVGKVAGL--ESELSNIDSDatCGIGHTRWA 79
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIA--TSDGK--RFHTHKGMGLVSDVfdEEKLRRLPGN--IAIGHVRYS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 80 THGKPSVVNAHPH--TSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAEThDLMASVREACTH 157
Cdd:cd00715 75 TAGSSSLENAQPFvvNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKD-DLFEAIIDALER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 158 VVGAYGLAAVCADepGVIAVarKDS----PIVVGVGETGSYV-ASDVIAL--IDAT--RDVvvlEDGQFAKLTPAGVEYT 228
Cdd:cd00715 154 VKGAYSLVIMTAD--GLIAV--RDPhgirPLVLGKLEGDGYVvASESCALdiIGAEfvRDV---EPGEIVVIDDDGLESS 226
|
....*
gi 1801477804 229 DEAGN 233
Cdd:cd00715 227 QRAPK 231
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-227 |
8.72e-34 |
|
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: 133.98 E-value: 8.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 2 CGIVGYTGSDI-AKNILVTGLKRMEYRGYDSSGVALEVGEGAAAHldvirrvgKVAGLESELSNIDSDAT----CGIGHT 76
Cdd:TIGR01134 1 CGVVGIYGQEEvAASLTYYGLYALQHRGQESAGISVFDGNRFRLH--------KGNGLVSDVFNEEHLQRlkgnVGIGHV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 77 RWATHGKPSVVNAHPHT--SCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAETHDLMASVREA 154
Cdd:TIGR01134 73 RYSTAGSSGLENAQPFVvnSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 155 CTHVVGAYGLAAvcADEPGVIAVarKDS----PIVVGVGETGSYVASDVIAL--IDAT--RDV-----VVLEDG-----Q 216
Cdd:TIGR01134 153 LERVRGAYALVL--MTEDGLVAV--RDPhgirPLVLGRRGDGYVVASESCALdiLGAEfvRDVepgevVVIFDGglesrQ 228
|
250
....*....|...
gi 1801477804 217 FAKLTPAGV--EY 227
Cdd:TIGR01134 229 CARRPRAPCvfEY 241
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-209 |
9.30e-34 |
|
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: 134.38 E-value: 9.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSDIAKNILVTGLKRMEYRGYDSSGVAleVGEGAaaHLDVIRRVGKVAGL--ESELSNIDSDAtcGIGHTRW 78
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIA--TSDGG--RFHLHKGMGLVSDVfdEEDLERLKGNI--AIGHVRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 79 ATHGKPSVVNAHPHT--SCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEaYAETHDLMASVREACT 156
Cdd:COG0034 81 STTGSSSLENAQPFYvnSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAR-ELTKEDLEEAIKEALR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1801477804 157 HVVGAYglAAVCADEPGVIAVarKDS----PIVVGVGETGSYVASDVIAL--IDAT--RDV 209
Cdd:COG0034 160 RVKGAY--SLVILTGDGLIAA--RDPngirPLVLGKLEDGYVVASESCALdiLGAEfvRDV 216
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
294-416 |
4.99e-29 |
|
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: 112.01 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 294 ELNDIDRVYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASEFRYR-NPIITPTTLVVAVSQSGETADTLAAIRDARIKG 372
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1801477804 373 AKVFGITNVVGSPVARESDGVIYTKANKEIAVASTKSFIGQVVS 416
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAA 124
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-215 |
6.19e-24 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 105.53 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSDIAKNILVTGLKRMEYRGYDSSGVALEVGEGaaahLDVIRRVGKVAGL--ESELSNIDSDatCGIGHTRW 78
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNR----LQSITGNGLVSDVfdESKLDQLPGD--IAIGHVRY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 79 ATHGKPSVVNAHPH--TSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAEThdLMASVREACT 156
Cdd:PLN02440 75 STAGASSLKNVQPFvaNYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARP--FFSRIVDACE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801477804 157 HVVGAYGLAAVCADepgvIAVARKDS----PIVVGVGETGSYV-ASDVIAL--IDAT--RDV-----VVLEDG 215
Cdd:PLN02440 153 KLKGAYSMVFLTED----KLVAVRDPhgfrPLVMGRRSNGAVVfASETCALdlIGATyeREVnpgevIVVDKD 221
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
68-198 |
1.57e-23 |
|
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: 96.22 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 68 DATCGIGHTRWATHGkPSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAETHDl 147
Cdd:pfam13522 9 EGGVALGHVRLAIVD-LPDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWGEDCLE- 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1801477804 148 masvreactHVVGAYGLAAV-CADEPGVIAVARKDS-PIVVGVGETGSYVASD 198
Cdd:pfam13522 87 ---------RLRGMFAFAIWdRRRRTLFLARDRLGIkPLYYGILGGGFVFASE 130
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-202 |
5.11e-21 |
|
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: 92.72 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 2 CGIVGY---TGSDIAKNILVTGLKRMEYRG-YDSSGVALEVGEGAAAH-----LDVIRRVGKVAGLeSELSNIDS-DATC 71
Cdd:cd01907 1 CGIFGImskDGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDAFVYssgkdMEVFKGVGYPEDI-ARRYDLEEyKGYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 72 GIGHTRWATHgkpSVVN---AHPHTSCDgrIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAE----- 143
Cdd:cd01907 80 WIAHTRQPTN---SAVWwygAHPFSIGD--IAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKgglpl 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801477804 144 ---THDLMASVREACTHVVGAYGLAAVCADEPGVIAVARKDSPIVVG---------VGETGSYV--ASDVIAL 202
Cdd:cd01907 155 eyyKHIIRMPEEERELLLALRLTYRLADLDGPFTIIVGTPDGFIVIRdriklrpavVAETDDYVaiASEECAI 227
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
470-598 |
7.74e-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: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 470 DAQSALFVGRGMGAAISYEGALKLKEVSYLHAEAYAAGEMKHGPIALIDLGFPVIAVATKSATYDkTVSNLMECKARGAK 549
Cdd:pfam01380 4 KAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKD-LLAAAELAKARGAK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1801477804 550 VIVVATEGDEEINKIADCIIRVPAVRDVFSPITASVPLQLLAREVAILR 598
Cdd:pfam01380 83 IIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
300-398 |
1.86e-19 |
|
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: 84.16 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 300 RVYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASEFRYRNPI-ITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGI 378
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100
....*....|....*....|
gi 1801477804 379 TNVVGSPVARESDGVIYTKA 398
Cdd:cd05710 81 TDDEDSPLAKLADYVIVYGF 100
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-139 |
2.34e-19 |
|
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: 91.82 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSD--IAKNILVTGLKRMEYRGYDSSGValEVGEGAA-AHldviRRvgkvagleseLSNIDSDATcgiGHtr 77
Cdd:COG0367 1 MCGIAGIIDFDggADREVLERMLDALAHRGPDGSGI--WVDGGVAlGH----RR----------LSIIDLSEG---GH-- 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1801477804 78 wathgkpsvvnaHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEE 139
Cdd:COG0367 60 ------------QPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEE 109
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-139 |
7.22e-19 |
|
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: 85.69 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 2 CGIVGY---TGSDIAKNILVTGLKRMEYRGYDSSGVALevgegaaahldvirrvgkvagleselsnidsDATCGIGHTRW 78
Cdd:cd00712 1 CGIAGIiglDGASVDRATLERMLDALAHRGPDGSGIWI-------------------------------DEGVALGHRRL 49
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801477804 79 A----THGkpsvvnAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEE 139
Cdd:cd00712 50 SiidlSGG------AQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEE 108
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
92-143 |
1.17e-17 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 79.10 E-value: 1.17e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1801477804 92 HTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAE 143
Cdd:pfam13537 17 VSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEWGE 68
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-209 |
1.21e-17 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 85.86 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 2 CGIVG-YTGSDI-AKNILVTGLKRMEYRGYDSSGVALEVGEgaaaHLDVIRRVGKVAGL--ESELSNIDSDatCGIGHTR 77
Cdd:PRK05793 15 CGVFGvFSKNNIdVASLTYYGLYALQHRGQESAGIAVSDGE----KIKVHKGMGLVSEVfsKEKLKGLKGN--SAIGHVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 78 WATHGKPSVVNAHP--HTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIeeAYAETHDLMASVREAC 155
Cdd:PRK05793 89 YSTTGASDLDNAQPlvANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLI--ARSAKKGLEKALVDAI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 156 THVVGAYGLAAVCADEpgVIAVARKDS--PIVVGVGETGSYVASDVIAL--IDA--TRDV 209
Cdd:PRK05793 167 QAIKGSYALVILTEDK--LIGVRDPHGirPLCLGKLGDDYILSSESCALdtIGAefIRDV 224
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
295-415 |
5.78e-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: 66.48 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 295 LNDIDRVYVIACGTSyhaGLIAKNLIEGWARIPTEVEAAS---EFRYRNPIITPTTLVVAVSQSGETADTLAAIRDARIK 371
Cdd:cd05013 10 LAKARRIYIFGVGSS---GLVAEYLAYKLLRLGKPVVLLSdphLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1801477804 372 GAKVFGITNVVGSPVARESDGVIYTKAN-KEIAVASTKSFIGQVV 415
Cdd:cd05013 87 GAKVIAITDSANSPLAKLADIVLLVSSEeGDFRSSAFSSRIAQLA 131
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-139 |
5.86e-11 |
|
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: 65.05 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 4 IVGYTGSDIAKNILVTGLKRM----EYRGYDSSGValevgegaaahldvirrvgkvagleselsnIDSDATCGIGHTRWA 79
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMsdtiAHRGPDASGI------------------------------EYKDGNAILGHRRLA 50
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 80 THGkpSVVNAHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEE 139
Cdd:TIGR01536 51 IID--LSGGAQPMSNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEE 108
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-265 |
1.26e-10 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 64.40 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGI---VGYTGSDIAKNILVTGL-KRMEYRGYDSSGvaLEVGEGaaahldvirrvgkvagleselsnidsdatCGIGHT 76
Cdd:PLN02549 1 MCGIlavLGCSDDSQAKRSRVLELsRRLRHRGPDWSG--LYGNED-----------------------------CYLAHE 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 77 RWA----THGKPSVVNAhphtscDGRIAIVHNGIIENFAELREELEgrGHHFKSETDTEVFAHLIEEAYAETHDLMASVr 152
Cdd:PLN02549 50 RLAimdpESGDQPLYNE------DKTIVVTANGEIYNHKELREKLK--LHKFRTGSDCEVIAHLYEEHGEEFVDMLDGM- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 153 eacthvvgaygLAAVCADEPGVIAVARKD----SPIVVGVGETGS-YVASDVIALIDatrDVVVLEdgQFakltPAGVEY 227
Cdd:PLN02549 121 -----------FSFVLLDTRDNSFIAARDhigiTPLYIGWGLDGSvWFASEMKALCD---DCERFE--EF----PPGHYY 180
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1801477804 228 TDEAGNVI---EPKvthidWDLDMAEKGGYPDFMLKEIHEQ 265
Cdd:PLN02549 181 SSKAGGFRrwyNPP-----WFSESIPSTPYDPLVLREAFEK 216
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
58-154 |
2.32e-10 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 61.13 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 58 LESELSNIDSdaTCGIGHTRWATHGKPSVVNAHPHTscDGRIAIVHNGIIENFAELREELEGR-----GHHFKSETDTEV 132
Cdd:COG0121 67 LRLLARPIKS--RLVIAHVRKATVGPVSLENTHPFR--GGRWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSEL 142
|
90 100
....*....|....*....|...
gi 1801477804 133 -FAHLIEEAYAETHDLMASVREA 154
Cdd:COG0121 143 aFALLLSRLRDGGPDPAEALAEA 165
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
58-168 |
3.21e-10 |
|
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: 60.87 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 58 LESELSNIDSdaTCGIGHTRWATHGKPSVVNAHPHTscDGRIAIVHNGIIENFAELREEL-EGRGHHFKSETDTEVFAHL 136
Cdd:cd01908 71 LESLARPIKS--PLVLAHVRAATVGPVSLENCHPFT--RGRWLFAHNGQLDGFRLLRRRLlRLLPRLPVGTTDSELAFAL 146
|
90 100 110
....*....|....*....|....*....|....*..
gi 1801477804 137 I----EEAYAETHDLM-ASVREACTHVVGAYGLAAVC 168
Cdd:cd01908 147 LlsrlLERDPLDPAELlDAILQTLRELAALAPPGRLN 183
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
283-399 |
4.22e-10 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 61.10 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 283 LDIDELGLSLEELNDIDRVYVIACGTSYHAGLIAKNLIeGWARIPTEV--EAASEFRYRNPIITPTTLVVAVSQSGETAD 360
Cdd:COG1737 119 LDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKL-LRLGKNVVLldGDGHLQAESAALLGPGDVVIAISFSGYTRE 197
|
90 100 110
....*....|....*....|....*....|....*....
gi 1801477804 361 TLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKAN 399
Cdd:COG1737 198 TLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSE 236
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-275 |
5.50e-10 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 62.04 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGYTGSDIAKNIL---VTGL-KRMEYRGYDSSGValevgegaaahldvirrvgKVAGLESELSNIdsdatcgIGHT 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELrrkALELsKRLRHRGPDWSGI-------------------IVLENSPGTYNI-------LAHE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 77 RWA----THGKpsvvnaHPHTSCDGRIAIVHNGIIENFAELREELEGRGHHFKSETDTEVFAHLIEEAYAethdlmasvR 152
Cdd:PTZ00077 55 RLAivdlSDGK------QPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGP---------K 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 153 EACTHVVGAYglAAVCADEPGVIAVARKDS----PIVVGVGETGS-YVASDVIALIDATRDVVVLEDGQfakltpagveY 227
Cdd:PTZ00077 120 DFWNHLDGMF--ATVIYDMKTNTFFAARDHigiiPLYIGYAKDGSiWFSSELKALHDQCVEVKQFPPGH----------Y 187
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1801477804 228 TDEAGNVIEPKVTH--IDWDLDMAEKGGYPDFmlKEIHEQ-PRVVRDTLVG 275
Cdd:PTZ00077 188 YDQTKEKGEFVRYYnpNWHDFDHPIPTGEIDL--EEIREAlEAAVRKRLMG 236
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-139 |
1.06e-09 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 61.08 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 1 MCGIVGY----TGSDIAKNILVTGLKRMEYRGYDSSGvalevgegaaahldvirrvgkvagleselsnIDSDATCGIGHT 76
Cdd:PRK09431 1 MCGIFGIldikTDADELRKKALEMSRLMRHRGPDWSG-------------------------------IYASDNAILGHE 49
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801477804 77 RWA----THGkpsvvnAHPHTSCDGRIAIVHNGIIENFAELREELEGRgHHFKSETDTEVFAHLIEE 139
Cdd:PRK09431 50 RLSivdvNGG------AQPLYNEDGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILALYQE 109
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
268-553 |
3.20e-09 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 58.86 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 268 VVRDTLVGRMTPAGELDIDELGLSLEEL--NDIDRVYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASEFRYRNPI-IT 344
Cdd:PRK11382 12 LVTENMVQEVEKVLSHDVPLVHAIVEEMvkRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYrLD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 345 PTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKAN--KEIAVASTKSFIGQVVSLTLLAL 422
Cdd:PRK11382 92 DRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDYQADciWEIHLLLCYSVVLEMITRLAPNA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 423 LLAQVKYRLTTKQARM--LFRELSDTAEQIqwildtqTEAVHEAALLCKDAQSALfvgRGMGAAisyEGALKLKEVSYLH 500
Cdd:PRK11382 172 EIGKIKNDLKQLPNALghLVRTWEEKGRQL-------GELASQWPMIYTVAAGPL---RPLGYK---EGIVTLMEFTWTH 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1801477804 501 AEAYAAGEMKHGPIALIDLGFPVIAVATKSATYDKTVSNLMECKARGAKVIVV 553
Cdd:PRK11382 239 GCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTTERAINFVKQRTDNVIVI 291
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
342-398 |
1.19e-08 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 56.69 E-value: 1.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801477804 342 IITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKA 398
Cdd:PRK11337 184 LLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTA 240
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
293-379 |
5.14e-07 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 51.91 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 293 EELNDIDRVYVIACGTSYHAGLIAKNLIEGWARIPTeveaaseFRYRN----PIITPTTLVVAVSQSGETADTLAAIRDA 368
Cdd:PRK08674 29 EDLEKIDNIVISGMGGSGIGGDLLRILLFDELKVPV-------FVNRDytlpAFVDEKTLVIAVSYSGNTEETLSAVEQA 101
|
90
....*....|.
gi 1801477804 369 RIKGAKVFGIT 379
Cdd:PRK08674 102 LKRGAKIIAIT 112
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
300-379 |
2.07e-06 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 46.87 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 300 RVYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASefrYRNPIITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGIT 379
Cdd:cd05017 1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYVVKDY---TLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
301-379 |
2.83e-06 |
|
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: 45.83 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 301 VYVIACGTSYHAGLIAKNLIEGWARIPTEVEAASEFRYRNP--IITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGI 378
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLlsLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1801477804 379 T 379
Cdd:cd04795 81 T 81
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
280-407 |
4.84e-06 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 47.18 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 280 AGELDIDELGLSLEELNDIDRVYVIACGTSyhaGLIAK---------NLIEGWARIPTEveaasefryrnPIITPTTLVV 350
Cdd:cd05005 15 ADKIDEEELDKLISAILNAKRIFVYGAGRS---GLVAKafamrlmhlGLNVYVVGETTT-----------PAIGPGDLLI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1801477804 351 AVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIY----TKANKEIAVAST 407
Cdd:cd05005 81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVipaaTKDDHGGEHKSI 141
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
343-394 |
6.13e-05 |
|
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: 44.82 E-value: 6.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1801477804 343 ITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVI 394
Cdd:cd05007 116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAI 167
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
342-415 |
1.64e-04 |
|
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: 41.76 E-value: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801477804 342 IITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKANKE---IAVASTKSFIGQVV 415
Cdd:cd05014 44 MVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEacpLGLAPTTSTTAMLA 120
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
343-394 |
1.95e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 43.62 E-value: 1.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1801477804 343 ITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVI 394
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAI 180
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
342-401 |
4.07e-04 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 42.66 E-value: 4.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 342 IITPTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYTKANKE 401
Cdd:COG0794 88 MITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVERE 147
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
441-599 |
9.48e-04 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 41.45 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 441 RELSDTAEQIQwildtqTEAVHEAALLCKDAQSALFVGRGMGAAISYEGALKL----KEVSYLHAEAYAAGEMkhgpIAL 516
Cdd:COG1737 110 ANLEETLELLD------EEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLlrlgKNVVLLDGDGHLQAES----AAL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 517 I---DLgfpVIAVatkSAT-YDKTVSNLME-CKARGAKVIVVATEGDEEINKIADCIIRVPA--VRDVFSPITASVP--- 586
Cdd:COG1737 180 LgpgDV---VIAI---SFSgYTRETLEAARlAKERGAKVIAITDSPLSPLAKLADVVLYVPSeePTLRSSAFSSRVAqla 253
|
170
....*....|....
gi 1801477804 587 -LQLLAREVAILRG 599
Cdd:COG1737 254 lIDALAAAVAQRDG 267
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
476-605 |
2.29e-03 |
|
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli. It is similar to the glucosamine-6-phosphate synthases (GlmS) which catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source.
Pssm-ID: 240143 [Multi-domain] Cd Length: 151 Bit Score: 38.76 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 476 FVGRGMGAAISYEGALKLKEVS--YLHAEAYAAGEMKHGPIALID---LGFPVIAVATKSATYDKTVsnLMECKARG--A 548
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDddtLVVVFVSNDPYTRQYDLDL--LKELRRDGiaA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 549 KVIVVATEGDEEINKIadCIIRVPAVR---DVFSPITASVPLQLLAREVAILRGCDVDQP 605
Cdd:cd05010 81 RVIAISPESDAGIEDN--SHYYLPGSRdldDVYLAFPYILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
475-554 |
2.56e-03 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 37.35 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 475 LFVGRGMGAAISYEGALKLKEVSYLHAEAYAAGEMKHGP-IALIDLGFPVIAVAtKSATYDKTVSNLMECKARGAKVIVV 553
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALS-YSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1801477804 554 A 554
Cdd:cd04795 81 T 81
|
|
| PRK11557 |
PRK11557 |
MurR/RpiR family transcriptional regulator; |
267-407 |
5.91e-03 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 38.98 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801477804 267 RVVRDTLVGRMTPA--GELDI---DELGLSLEELNDIDRVYVIACGTSyhaGLIAKNLieGWARIPTEVEAASEFRYRNP 341
Cdd:PRK11557 92 RLVGEKLIKENTAAmrATLDVnseEKLHECVTMLRSARRIILTGIGAS---GLVAQNF--AWKLMKIGINAVAERDMHAL 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801477804 342 IIT-----PTTLVVAVSQSGETADTLAAIRDARIKGAKVFGITNVVGSPVARESDGVIYT----KANKEIAVAST 407
Cdd:PRK11557 167 LATvqalsPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTiaeeQATRSAAISST 241
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
535-573 |
9.78e-03 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 37.55 E-value: 9.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1801477804 535 KTVSNLME-CKARGAKVIVVATEGDEEINKIADCIIRVPA 573
Cdd:cd05005 89 SSVVNAAEkAKKAGAKVVLITSNPDSPLAKLADVVVVIPA 128
|
|
| |
