|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-621 |
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: 1068.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGlpektsTHSALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGKLANLVAEIEAAPLrEASLGIGHTR 80
Cdd:COG0449 1 MCGIVGYIG------KRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPL-SGTIGIGHTR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 81 WATHGGPTDQNAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNAGDLTEAMRLASNE 160
Cdd:COG0449 74 WATHGAPSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 161 LEGAFTLLAVHVDQPDRVVASRRNSPLVVGLGEGENFLGSDVSGFIDFTREAVELEQDQIVTITTDDVAIINFDGTPAEG 240
Cdd:COG0449 154 LEGAYALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 241 KRFHIDWDASAAEKGGYDSFMEKEINEQPKAVEDTLLGRTDASGQLTLDELRIDPEELKNTSKIIVLACGTAAYAGHVAK 320
Cdd:COG0449 234 EVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 321 YAIEHWCRIPVEVELAHEFRYRDPIIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLH 400
Cdd:COG0449 314 YLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 401 AGPEIAVASTKAFLAMIAASYLLGLYLAQLRGQLFREEIKDILADLHKIPAKIQKILDSSEDIKALARAMKDTPSVLFLG 480
Cdd:COG0449 394 AGPEIGVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 481 RHVGFPVALEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQPVFVVVPsprgRDSLHSKVVSNIQEVRARGAKTITVA 560
Cdd:COG0449 474 RGINYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAP----QDELYEKTLSNIQEVKARGGKVIAIA 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2578770988 561 EAGDDAVREFSETVFFVPETSPLLMPLLTTVPLQIFACALAAEKGYDVDQPRNLAKSVTVE 621
Cdd:COG0449 550 DEGDEEVEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-621 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 1037.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGlpektsTHSALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGKLANLVAEIEAAPLrEASLGIGHTR 80
Cdd:PRK00331 1 MCGIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPL-PGTTGIGHTR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 81 WATHGGPTDQNAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNAGDLTEAMRLASNE 160
Cdd:PRK00331 74 WATHGKPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 161 LEGAFTLLAVHVDQPDRVVASRRNSPLVVGLGEGENFLGSDVSGFIDFTREAVELEQDQIVTITTDDVAIINFDGTPAEG 240
Cdd:PRK00331 154 LEGAYALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 241 KRFHIDWDASAAEKGGYDSFMEKEINEQPKAVEDTLLGRTDASGqltldELRIDPEELKNTSKIIVLACGTAAYAGHVAK 320
Cdd:PRK00331 234 EVYTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELG-----EGELADEDLKKIDRIYIVACGTSYHAGLVAK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 321 YAIEHWCRIPVEVELAHEFRYRDPIIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLH 400
Cdd:PRK00331 309 YLIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 401 AGPEIAVASTKAFLAMIAASYLLGLYLAQLRGQLFREEIKDILADLHKIPAKIQKILDSSEDIKALARAMKDTPSVLFLG 480
Cdd:PRK00331 389 AGPEIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLG 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 481 RHVGFPVALEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQPVFVVVPsprgRDSLHSKVVSNIQEVRARGAKTITVA 560
Cdd:PRK00331 469 RGVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAP----NDELYEKTKSNIQEVKARGARVIVIA 544
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2578770988 561 EAGDDaVREFSETVFFVPETSPLLMPLLTTVPLQIFACALAAEKGYDVDQPRNLAKSVTVE 621
Cdd:PRK00331 545 DEGDE-VAEEADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-621 |
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: 838.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGYIGlpektsTHSALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGKLANLVAEIEAAPLReASLGIGHTRW 81
Cdd:TIGR01135 1 CGIVGYIG------QRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKPLP-GGVGIGHTRW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 82 ATHGGPTDQNAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNAGDLTEAMRLASNEL 161
Cdd:TIGR01135 74 ATHGKPTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 162 EGAFTLLAVHVDQPDRVVASRRNSPLVVGLGEGENFLGSDVSGFIDFTREAVELEQDQIVTITTDDVAIINFDGTPAEGK 241
Cdd:TIGR01135 154 RGAYALAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 242 RFHIDWDASAAEKGGYDSFMEKEINEQPKAVEDTLLGRTDASGQLtLDELRIDpEELKNTSKIIVLACGTAAYAGHVAKY 321
Cdd:TIGR01135 234 VRVIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGV-FEELGAE-ELLKNIDRIQIVACGTSYHAGLVAKY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 322 AIEHWCRIPVEVELAHEFRYRDPIIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHA 401
Cdd:TIGR01135 312 LIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 402 GPEIAVASTKAFLAMIAASYLLGLYLAQLRGQLFREEIKDILADLHKIPAKIQKILDSSEDIKALARAMKDTPSVLFLGR 481
Cdd:TIGR01135 392 GPEIGVASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 482 HVGFPVALEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQPVFVVVPSprgrDSLHSKVVSNIQEVRARGAKTITVAE 561
Cdd:TIGR01135 472 GLGYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPK----DSLLEKTKSNVEEVKARGARVIVFAP 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 562 AGDDAVREFSETVFFVPETSPLLMPLLTTVPLQIFACALAAEKGYDVDQPRNLAKSVTVE 621
Cdd:TIGR01135 548 EDDETIASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-621 |
6.58e-160 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 474.24 E-value: 6.58e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGLPEKTSTHSALDVLLEGLRRLEYRGYDSAGVATVADGVIEGR-----KKSGKLANLVAEIEAApLREASL- 74
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSsplvfREEGKIESLVRSVYEE-VAETDLn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 75 ---------GIGHTRWATHGGPTDQNAHPHFGDQG-RLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYY 144
Cdd:PLN02981 80 ldlvfenhaGIAHTRWATHGPPAPRNSHPQSSGPGnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 145 RNAGD----------LTEAMRlasnELEGAFTLLAVHVDQPDRVVASRRNSPLVVG---LGEGEN--------------- 196
Cdd:PLN02981 160 DKLNEeegdvtfsqvVMEVMR----QLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 197 ------FLGSDVSGFIDFTREAVELEQDQIVTITTDDVAIINFDGtpaeGKRFHIDWDASAAE----------------K 254
Cdd:PLN02981 236 dkpkefFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFEN----EKGRGGGGLSRPASveralstlemeveqimK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 255 GGYDSFMEKEINEQPKAVEDTLLGR--TDASGQLT---LDELRIDPEELKNTSKIIVLACGTAAYAGHVAKYAIEHWCRI 329
Cdd:PLN02981 312 GNYDHYMQKEIHEQPESLTTTMRGRliRGGSGKAKrvlLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 330 PVEVELAHEFRYRD-PIIDENTLVVsISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHAGPEIAVA 408
Cdd:PLN02981 392 PVTMELASDLLDRQgPIYREDTAVF-VSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 409 STKAFLAMIAASYLLGLYLA--QLRGQLFREEIKDILADLhkiPAKIQKILDSSEDIKALARAMKDTPSVLFLGRHVGFP 486
Cdd:PLN02981 471 STKAYTSQIVAMTMLALALGedSISSRSRREAIIDGLFDL---PNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 487 VALEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQPVFVVVPsprgRDSLHSKVVSNIQEVRARGAKTITVAEAGDDA 566
Cdd:PLN02981 548 TALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIAT----RDACFSKQQSVIQQLRARKGRLIVICSKGDAS 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2578770988 567 VR--EFSETVFFVPETSPLLMPLLTTVPLQIFACALAAEKGYDVDQPRNLAKSVTVE 621
Cdd:PLN02981 624 SVcpSGGCRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-620 |
7.46e-160 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 472.58 E-value: 7.46e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGlpektsTHSALDVLLEGLRRLEYRGYDSAGVATVADGvieGRKKSGKLANLVAEIEAAP-LREASL----- 74
Cdd:PTZ00295 24 CCGIVGYLG------NEDASKILLEGIEILQNRGYDSCGISTISSG---GELKTTKYASDGTTSDSIEiLKEKLLdshkn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 75 ---GIGHTRWATHGGPTDQNAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNAGDLT 151
Cdd:PTZ00295 95 stiGIAHTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 152 EAMRLASNELEGAFTLLAVHVDQPDRVVASRRNSPLVVGLGEGENFLGSDVSGFIDFTREAVELEQDQIVTITTDDvaiI 231
Cdd:PTZ00295 175 EAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLEN---V 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 232 NFDGTPAEGKRfhIDWDASAAEKGGYDSFMEKEINEQPKAVEDTLL--GR-TDASGQLTLDELRIDPEELKNTSKIIVLA 308
Cdd:PTZ00295 252 NDLYTQRRVEK--IPEEVIEKSPEPYPHWTLKEIFEQPIALSRALNngGRlSGYNNRVKLGGLDQYLEELLNIKNLILVG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 309 CGTAAYAGHVAKYAIEHW-CRIPVEVELAHEF-RYRDPiiDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNG 386
Cdd:PTZ00295 330 CGTSYYAALFAASIMQKLkCFNTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 387 STIPRESDAVLYLHAGPEIAVASTKAFLAMIAASYLLGLYLAQLR-GQLFREEIKDILADLHKIPAKIQKILDSSEDI-K 464
Cdd:PTZ00295 408 SLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNYKCSSLINSLHRLPTYIGMTLKSCEEQcK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 465 ALARAMKDTPSVLFLGRHVGFPVALEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQ--PVFVVVPSprgrDSLHSKV 542
Cdd:PTZ00295 488 RIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEKntPVILIILD----DEHKELM 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2578770988 543 VSNIQEVRARGAKTITVAEAgDDAVREFSETVFFVPETSPlLMPLLTTVPLQIFACALAAEKGYDVDQPRNLAKSVTV 620
Cdd:PTZ00295 564 INAAEQVKARGAYIIVITDD-EDLVKDFADEIILIPSNGP-LTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-621 |
2.46e-136 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 413.12 E-value: 2.46e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGLPEKTSTHSALDVLLEGLRRLEYRGYDSAGVATvaDGVIEGRKKSGKLAN-------LVAEI-EAAPLRE- 71
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAI--DANIGSEKEDGTAASaptprpcVVRSVgNISQLREk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 72 -------ASL-----------GIGHTRWATHGGPTDQNAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDT 133
Cdd:PTZ00394 79 vfseavaATLppmdattshhvGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 134 EVAAKLIGRYYRNAG--DLTEAMRLASNELEGAFTLLAVHVDQPDRVVASRRNSPLVVGLGEG----------------- 194
Cdd:PTZ00394 159 EVISVLSEYLYTRKGihNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRRTddrgcvmklqtydltdl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 195 ----ENFLGSDVSGFIDFTREAVELEQDQIVTITTDDVAIINFDGTPAEG-KRF--HIDWDASAAEKGGYDSFMEKEINE 267
Cdd:PTZ00394 239 sgplEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIvKREvqHLDAKPEGLSKGNYPHFMLKEIYE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 268 QPKAVEDTLLGRTD-ASGQLTLDELRIDPEELKNTSK-IIVLACGTAAYAGHVAKYAIEHWCRIPVEVELAHEFRYRDPI 345
Cdd:PTZ00394 319 QPESVISSMHGRIDfSSGTVQLSGFTQQSIRAILTSRrILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 346 IDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHAGPEIAVASTKAFLAMIAASYLLGL 425
Cdd:PTZ00394 399 IQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVAL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 426 YLA--QLRGQLFREEIKDILADLhkiPAKIQKILDSSED-IKALARAMKDTPSVLFLGRHVGFPVALEGALKLKELAYIH 502
Cdd:PTZ00394 479 LLSsdSVRLQERRNEIIRGLAEL---PAAISECLKITHDpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 503 AEGFAAGELKHGPIALIEQDQPVFVVVPSPRGRDslHSKvvSNIQEVRARGAKTITVAEAGDDAVREFSETVFFVPETSP 582
Cdd:PTZ00394 556 TEGIHSGELKHGPLALIDETSPVLAMCTHDKHFG--LSK--SAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVD 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 2578770988 583 LLMPLLTTVPLQIFACALAAEKGYDVDQPRNLAKSVTVE 621
Cdd:PTZ00394 632 CLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-223 |
1.97e-116 |
|
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: 345.59 E-value: 1.97e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGYIGlpektsTHSALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGKLANLVAEIEAAPLrEASLGIGHTRW 81
Cdd:cd00714 1 CGIVGYIG------KREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPL-SGHVGIGHTRW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 82 ATHGGPTDQNAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNAGDLTEAMRLASNEL 161
Cdd:cd00714 74 ATHGEPTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2578770988 162 EGAFTLLAVHVDQPDRVVASRRNSPLVVGLGEGENFLGSDVSGFIDFTREAVELEQDQIVTI 223
Cdd:cd00714 154 EGAYALAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
262-621 |
2.09e-78 |
|
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: 252.13 E-value: 2.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 262 EKEINEQPKAVEDTLLGRTDASGQLtLDELRIDPeelknTSKIIVLACGTAAYAGHVAKYAIEHWCRIPVEVELAHEF-R 340
Cdd:COG2222 1 AREIAQQPEAWRRALAALAAAIAAL-LARLRAKP-----PRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 341 YRDPIIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHAGPEIAVASTKAFLAMIAAs 420
Cdd:COG2222 75 YPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 421 yllglyLAQLRGQLFREEikDILADLHKIPAKIQKILDSSEDIKALArAMKDTPSVLFLGRHVGFPVALEGALKLKELAY 500
Cdd:COG2222 154 ------LLALLAAWGGDD--ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 501 IHAEGFAAGELKHGPIALIEQDQPVFVVVPSPRGRDsLHSKVvsnIQEVRARGAKTITVAEAGDDAVrefseTVFFVPET 580
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRE-LDLDL---AAELRALGARVVAIGAEDDAAI-----TLPAIPDL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2578770988 581 SPLLMPLLTTVPLQIFACALAAEKGYDVDQPRNLAKSVTVE 621
Cdd:COG2222 296 HDALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
303-428 |
1.42e-63 |
|
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: 205.42 E-value: 1.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 303 KIIVLACGTAAYAGHVAKYAIEHWCRIPVEVELAHEFRYRDPIIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSIC 382
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2578770988 383 NTNGSTIPRESDAVLYLHAGPEIAVASTKAFLAMIAASYLLGLYLA 428
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
461-619 |
2.81e-59 |
|
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: 195.17 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 461 EDIKALARAMKDTPSVLFLGRHVGFPVALEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQPVFVVVPsprgRDSLHS 540
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAP----EDRLEE 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2578770988 541 KVVSNIQEVRARGAKTITVAEAGDDAvrEFSETVFFVPETSPLLMPLLTTVPLQIFACALAAEKGYDVDQPRNLAKSVT 619
Cdd:cd05009 77 KLESLIKEVKARGAKVIVITDDGDAK--DLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-221 |
5.33e-58 |
|
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: 194.20 E-value: 5.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGYIGLPEKTSthSALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGKLANLVAEIEAAPLrEASLGIGHTRW 81
Cdd:cd00352 1 CGIFGIVGADGAAS--LLLLLLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPL-KSGVALGHVRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 82 ATHGGPTDQNAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNaGDLTEAMRLASNEL 161
Cdd:cd00352 78 ATNGLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRE-GGLFEAVEDALKRL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2578770988 162 EGAFTLLAVHVDqPDRVVASR-RN--SPLVVGLG-EGENFLGSDVSGFIDFTREAV-ELEQDQIV 221
Cdd:cd00352 157 DGPFAFALWDGK-PDRLFAARdRFgiRPLYYGITkDGGLVFASEPKALLALPFKGVrRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-423 |
1.98e-31 |
|
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: 118.56 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 297 ELKNTSKIIVLACGTAAYAGHVAKYAIEHWCRIPVEVELAHEFRYR-DPIIDENTLVVSISQSGETMDTLMAVRYAKEQG 375
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2578770988 376 ARTLSICNTNGSTIPRESDAVLYLHAGPEIAVASTKAFLAMIAASYLL 423
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDAL 128
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-223 |
5.33e-30 |
|
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: 118.72 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGYIGLPEktsthsALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGklanLVAEI-EAAPLRE--ASLGIGH 78
Cdd:cd00715 1 CGVFGIYGAED------AARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMG----LVSDVfDEEKLRRlpGNIAIGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 79 TRWATHGGPTDQNAHPHFGD--QGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNAgDLTEAMRL 156
Cdd:cd00715 71 VRYSTAGSSSLENAQPFVVNspLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKD-DLFEAIID 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 157 ASNELEGAFTLLAVHvdqPDRVVASR-----RnsPLVVG-LGEGENFLGS-----DVSGFiDFTR-----EAVELEQDQI 220
Cdd:cd00715 150 ALERVKGAYSLVIMT---ADGLIAVRdphgiR--PLVLGkLEGDGYVVASescalDIIGA-EFVRdvepgEIVVIDDDGL 223
|
...
gi 2578770988 221 VTI 223
Cdd:cd00715 224 ESS 226
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-233 |
8.76e-30 |
|
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: 122.82 E-value: 8.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGLPEktsthsALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGklanLVAEIeaapLREASL------ 74
Cdd:COG0034 7 ECGVFGIYGHED------VAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMG----LVSDV----FDEEDLerlkgn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 75 -GIGHTRWATHGGPTDQNAHPHFGDQ--GRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRnAGDLT 151
Cdd:COG0034 73 iAIGHVRYSTTGSSSLENAQPFYVNSpfGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELT-KEDLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 152 EAMRLASNELEGAFTLLAVHvdqPDRVVASR-----RnsPLVVGLGEGENFLGS-----DVSGFiDFTReavELEQDQIV 221
Cdd:COG0034 152 EAIKEALRRVKGAYSLVILT---GDGLIAARdpngiR--PLVLGKLEDGYVVASescalDILGA-EFVR---DVEPGEIV 222
|
250
....*....|..
gi 2578770988 222 TITTDDVAIINF 233
Cdd:COG0034 223 VIDEDGLRSRQF 234
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-211 |
2.57e-24 |
|
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: 106.25 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGYIGLPEKtsthsALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGklanLVAEI-EAAPLRE--ASLGIGH 78
Cdd:TIGR01134 1 CGVVGIYGQEEV-----AASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNG----LVSDVfNEEHLQRlkGNVGIGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 79 TRWATHGGPTDQNAHPHFGD--QGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNAGDLTEAMRL 156
Cdd:TIGR01134 72 VRYSTAGSSGLENAQPFVVNspYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2578770988 157 ASNELEGAFTLLAVHvdqPDRVVASRR---NSPLVVGLGEGENFLGS-----DVSGFiDFTRE 211
Cdd:TIGR01134 152 VLERVRGAYALVLMT---EDGLVAVRDphgIRPLVLGRRGDGYVVASescalDILGA-EFVRD 210
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-226 |
4.99e-23 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 102.83 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGLPEktsthsALDVLLEGLRRLEYRGYDSAGVATVADGVIEGRKKSGKLANLVAEIEAAPLReASLGIGHTR 80
Cdd:PLN02440 1 ECGVVGIFGDPE------ASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLP-GDIAIGHVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 81 WATHGGPTDQNAHPHFGDQ--GRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIgryyrnAGDLTEA--MRL 156
Cdd:PLN02440 74 YSTAGASSLKNVQPFVANYrfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLI------AISKARPffSRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 157 --ASNELEGAFTLLAVhvdQPDRVVASR-----RnsPLVVGL-GEGENFLGSDVSGF--IDFTREAvELEQDQIVTITTD 226
Cdd:PLN02440 148 vdACEKLKGAYSMVFL---TEDKLVAVRdphgfR--PLVMGRrSNGAVVFASETCALdlIGATYER-EVNPGEVIVVDKD 221
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-234 |
1.10e-19 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 92.40 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGyIGLPEKTSTHSaldVLLEGLRRLEYRGYDSAGVAtVADG-VIEGRKKSGKLANLVAEIEAAPLrEASLGIGHTR 80
Cdd:PRK05793 15 CGVFG-VFSKNNIDVAS---LTYYGLYALQHRGQESAGIA-VSDGeKIKVHKGMGLVSEVFSKEKLKGL-KGNSAIGHVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 81 WATHGGPTDQNAHP---HFgDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRnaGDLTEAMRLA 157
Cdd:PRK05793 89 YSTTGASDLDNAQPlvaNY-KLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK--KGLEKALVDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 158 SNELEGAFTLLavhVDQPDRVVASRRNS---PLVVGLGEGENFLGS-----DVSGfIDFTReavELEQDQIVTITTDDVA 229
Cdd:PRK05793 166 IQAIKGSYALV---ILTEDKLIGVRDPHgirPLCLGKLGDDYILSSescalDTIG-AEFIR---DVEPGEIVIIDEDGIK 238
|
....*
gi 2578770988 230 IINFD 234
Cdd:PRK05793 239 SIKFA 243
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
475-604 |
9.76e-18 |
|
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: 79.65 E-value: 9.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 475 SVLFLGRHVGFPVALEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQPVFVVVPSPRGRDSLHskvvsNIQEVRARGA 554
Cdd:pfam01380 7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-----AAELAKARGA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2578770988 555 KTITVAEAGDDAVREFSETVFFVPETSPLLMPLLTTVPLQIFACALAAEK 604
Cdd:pfam01380 82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
69-194 |
2.02e-16 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 75.81 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 69 LREASLGIGHTRWATHGGPTDQNaHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLigryYRNAG 148
Cdd:pfam13522 7 WVEGGVALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL----YEEWG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2578770988 149 dlTEAMrlasNELEGAFTlLAVHVDQPDRVVASRR---NSPLVVGLGEG 194
Cdd:pfam13522 82 --EDCL----ERLRGMFA-FAIWDRRRRTLFLARDrlgIKPLYYGILGG 123
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
304-398 |
7.79e-16 |
|
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: 73.76 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 304 IIVLACGTAAYAGHVAKYAIEHWCRIPVEVELAHEFRYRDPI-IDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSIC 382
Cdd:cd05710 2 VFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLT 81
|
90
....*....|....*.
gi 2578770988 383 NTNGSTIPRESDAVLY 398
Cdd:cd05710 82 DDEDSPLAKLADYVIV 97
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-204 |
2.81e-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: 73.07 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGYIglpEKTSTHSALDVLLEGLRRLEYRG-YDSAGVATVAD------------GVIegrKKSGkLANLVAEIEAAP 68
Cdd:cd01907 1 CGIFGIM---SKDGEPFVGALLVEMLDAMQERGpGDGAGFALYGDpdafvyssgkdmEVF---KGVG-YPEDIARRYDLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 69 LREASLGIGHTRWATHGGPTDQNAHPHFGdqGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRYYRNAG 148
Cdd:cd01907 74 EYKGYHWIAHTRQPTNSAVWWYGAHPFSI--GDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2578770988 149 D-------------------LTEAMRLASNELEGAFTLLAVHvDQPDRVVASR-RNSPLVVGLGEGENFLGSDVSG 204
Cdd:cd01907 152 LpleyykhiirmpeeerellLALRLTYRLADLDGPFTIIVGT-PDGFIVIRDRiKLRPAVVAETDDYVAIASEECA 226
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
256-448 |
8.05e-14 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 72.27 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 256 GYDSFME------KEINEQPKAVED-TLLGRTDASGQL----------TLDELR--IDPEE-------LKNTSKIIVLAC 309
Cdd:COG1737 63 GFSGFPElklalaQELAEGLSSYERlRRLSPDDSLEDIlakvleaeiaNLEETLelLDEEAleravdlLAKARRIYIFGV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 310 GTAAYAGHVAKYAIEHwCRIPVEV--ELAHEFRYRDPIIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGS 387
Cdd:COG1737 143 GASAPVAEDLAYKLLR-LGKNVVLldGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLS 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2578770988 388 TIPRESDAVLYLHA-GPEIAVASTKAFLAMIAASYLLGLYLAQLRGQLFREEIKDILADLHK 448
Cdd:COG1737 222 PLAKLADVVLYVPSeEPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSE 283
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-143 |
9.41e-14 |
|
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: 70.66 E-value: 9.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGYIGLPEktsTHSALDVLLEGLRRLEYRGYDSAGVatvadgviegrkksgklanlvaeieaapLREASLGIGHTRW 81
Cdd:cd00712 1 CGIAGIIGLDG---ASVDRATLERMLDALAHRGPDGSGI----------------------------WIDEGVALGHRRL 49
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2578770988 82 ATHggPTDQNAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIGRY 143
Cdd:cd00712 50 SII--DLSGGAQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEW 109
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
298-423 |
6.37e-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: 66.10 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 298 LKNTSKIIVLACGTAayaGHVAKYAIEHWCRIPVEVEL---AHEFRYRDPIIDENTLVVSISQSGETMDTLMAVRYAKEQ 374
Cdd:cd05013 10 LAKARRIYIFGVGSS---GLVAEYLAYKLLRLGKPVVLlsdPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2578770988 375 GARTLSICNTNGSTIPRESDAVLYLHAGPEIAVAStkAFLAMIAASYLL 423
Cdd:cd05013 87 GAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSS--AFSSRIAQLALI 133
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-139 |
1.96e-12 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 69.87 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGLPEKTSThsalDVLLEGLRRLEYRGYDSAGVatvadgviegrkksgklanlvaeieaapLREASLGIGHTR 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGI----------------------------WVDGGVALGHRR 48
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2578770988 81 WA----THGGptDQnahPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKL 139
Cdd:COG0367 49 LSiidlSEGG--HQ---PMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-186 |
3.05e-11 |
|
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: 63.95 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGLPEkTSTHSALDVLLEGLRR----LEYRGY---DSAGVATV-ADGVIEGRKKSGKLA--NLVAEIEAAPLR 70
Cdd:cd01908 1 MCRLLGYSGAPI-PLEPLLIRPSHSLLVQsggpREMKGTvhaDGWGIGWYeGKGGRPFRYRSPLPAwsDINLESLARPIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 71 eASLGIGHTRWATHGGPTDQNAHPhFgDQGRLAVIHNGIIENFAELKQKLLAAG-EVFESETDTEVAAKLI-----GRYY 144
Cdd:cd01908 80 -SPLVLAHVRAATVGPVSLENCHP-F-TRGRWLFAHNGQLDGFRLLRRRLLRLLpRLPVGTTDSELAFALLlsrllERDP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2578770988 145 RNAGDLTEAMRLASNELEGAFTLLA---VHVDqPDRVVASRRNSP 186
Cdd:cd01908 157 LDPAELLDAILQTLRELAALAPPGRlnlLLSD-GEYLIATRYASA 200
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
2-185 |
6.03e-11 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 63.06 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 2 CGIVGYIGlPEKTSTHSALDVLLEGLRRleyRGYDSA--------GVATVADGVIEGRKKSGKLA--NLVAEIEAAPLRe 71
Cdd:COG0121 1 CRLLGYSG-NVPTDLEFLLLDPEHSLVR---QSGATRegphadgwGIGWYEGDGEPRLYRDPLPAwsDPNLRLLARPIK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 72 ASLGIGHTRWATHGGPTDQNAHPHFGdqGRLAVIHNGIIENFAELKQKLLAAGEVF-----ESETDTEVAAKLI-GRYYR 145
Cdd:COG0121 76 SRLVIAHVRKATVGPVSLENTHPFRG--GRWLFAHNGQLDGFDRLRRRLAEELPDElyfqpVGTTDSELAFALLlSRLRD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2578770988 146 NAGDLTEAMRLASNELE------GAFTLLAvhVDqPDRVVASRRNS 185
Cdd:COG0121 154 GGPDPAEALAEALRELAelarapGRLNLLL--SD-GERLYATRYTS 196
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
100-140 |
5.89e-09 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 54.45 E-value: 5.89e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2578770988 100 GRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLI 140
Cdd:pfam13537 22 GRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLY 62
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-135 |
1.07e-08 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 58.00 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 1 MCGIVGYIGLpeKTSTHSALDVLLEGLRRLEYRGYDSAGVATVADGVIegrkksgklanlvaeieaaplreaslgiGHTR 80
Cdd:PRK09431 1 MCGIFGILDI--KTDADELRKKALEMSRLMRHRGPDWSGIYASDNAIL----------------------------GHER 50
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2578770988 81 WAT---HGGptdqnAHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEvFESETDTEV 135
Cdd:PRK09431 51 LSIvdvNGG-----AQPLYNEDGTHVLAVNGEIYNHQELRAELGDKYA-FQTGSDCEV 102
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
299-612 |
1.71e-08 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 56.55 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 299 KNTSKIIVLACGTAAYAGHVAKYAIEHWCRIPVEVELAHEFRYRDPI-IDENTLVVSISQSGETMDTLMAVRYAKEQGAR 377
Cdd:PRK11382 42 RDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYrLDDRCAVIGVSDYGKTEEVIKALELGRACGAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 378 TLSICNTNGSTIPRESDAVLYLHAGpeiavastkaflaMIAASYLLGLY---LAQLRGQLFREEIKDILADLHKIPAKIQ 454
Cdd:PRK11382 122 TAAFTKRADSPITSAAEFSIDYQAD-------------CIWEIHLLLCYsvvLEMITRLAPNAEIGKIKNDLKQLPNALG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 455 KILDSSEDI-KALARAMKDTPSVLFLG----RHVGFPvalEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQPVFVVV 529
Cdd:PRK11382 189 HLVRTWEEKgRQLGELASQWPMIYTVAagplRPLGYK---EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 530 psprGRDSLHSKVVSNIQEVRARGAKTITVAEAgddavrEFSETVffvpetSPLLMPLLTTVPLQIFACALAAEKGYDVD 609
Cdd:PRK11382 266 ----GNDESRHTTERAINFVKQRTDNVIVIDYA------EISQGL------HPWLAPFLMFVPMEWLCYYLSIYKDHNPD 329
|
...
gi 2578770988 610 QPR 612
Cdd:PRK11382 330 ERR 332
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
304-382 |
3.08e-08 |
|
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: 51.22 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 304 IIVLACGTAAYAGHVAKYAIEHWCRIPVEVELAHEFRYRDP--IIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSI 381
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLlsLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 2578770988 382 C 382
Cdd:cd04795 81 T 81
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
295-564 |
3.64e-08 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 55.76 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 295 PEELKNTSKIIVLACGTAAYAGHVAKyAIEHW-CRIPVevelaheFRYRD----PIIDENTLVVSISQSGETMDTLMAVR 369
Cdd:PRK08674 28 EEDLEKIDNIVISGMGGSGIGGDLLR-ILLFDeLKVPV-------FVNRDytlpAFVDEKTLVIAVSYSGNTEETLSAVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 370 YAKEQGARTLSIcnTNG---STIPRESD-AVLYLHAG--PEIAVA-STKAFLAMIAASYLLGLYLAQlrgqlfREEIKDI 442
Cdd:PRK08674 100 QALKRGAKIIAI--TSGgklKEMAKEHGlPVIIVPGGyqPRAALGyLFTPLLKILEKLGLIPDKSAE------VLETKIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 443 LADL-HKIPAKIQKIldsSEDIKALARAMKDTPSVLFlGRHVGFPVAL-------EGAlklKELAYIHaegfAAGELKHG 514
Cdd:PRK08674 172 LSELaEGLKEKVPTL---KNLAKRLAGKLYGRIPVIY-GSGLTLAVAYrwktqinENA---KYPAFYN----EIPELNHN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2578770988 515 PIALIEQDQ----PVFVVVPSPRGRDSLHSKVVSNIQEVRARGAKTITVAEAGD 564
Cdd:PRK08674 241 EIVGYERPQsllkYFFVVVLRDSEHPRIKKRVEITIDILTEAVINVIEIYPEGN 294
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
303-382 |
7.24e-08 |
|
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: 51.11 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 303 KIIVLACGTAAYAGHVAKYAIEHWCRIPVEVelaHEFRYRDPIIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSIC 382
Cdd:cd05017 1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYV---VKDYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
346-410 |
4.99e-07 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 51.37 E-value: 4.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2578770988 346 IDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHAGPEIAVAST 410
Cdd:cd05007 116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGST 180
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-282 |
7.52e-07 |
|
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: 51.95 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 4 IVGYIGLPEKTSThsALDVLLEGLRRLEYRGYDSAGVATVADGVIegrkksgklanlvaeieaaplreaslgIGHTRWAT 83
Cdd:TIGR01536 1 IAGFFDLDDKAVE--EDEAIKRMSDTIAHRGPDASGIEYKDGNAI---------------------------LGHRRLAI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 84 hggpTDQN--AHPHFGDQGRLAVIHNGIIENFAELKQKLLAAGEVFESETDTEVAAKLIgRYYRNAgdlteamrlASNEL 161
Cdd:TIGR01536 52 ----IDLSggAQPMSNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY-EEWGEE---------CVDRL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 162 EG--AFTLlavhVDQPDRVVASRRN----SPLVVGLGEGENFLGSDVSGFID------FTREAVELEQDQIVTITTDDVA 229
Cdd:TIGR01536 118 DGmfAFAL----WDSEKGELFLARDrfgiKPLYYAYDGGQLYFASEIKALLAhpnikpFPDGAALAPGFGFVRVPPPSTF 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2578770988 230 IIN-FDGTPAEGKRFHIDWDASAAEKGGYDSFMEKEINEQPKAVEDTLLGRTDA 282
Cdd:TIGR01536 194 FRGvFELEPGHDLPLDDDGLNIERYYWERRDEHTDSEEDLVDELRSLLEDAVKR 247
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
346-412 |
1.64e-06 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 50.17 E-value: 1.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2578770988 346 IDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHAGPEIAVAST--KA 412
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKA 197
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
346-412 |
2.13e-06 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 49.71 E-value: 2.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2578770988 346 IDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHAGPEIAVAST--KA 412
Cdd:COG2103 130 LGPGDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEVITGSTrlKA 198
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
334-397 |
4.20e-06 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 48.99 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 334 ELAHEF--------RYRDP--------IIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVL 397
Cdd:PRK11337 157 DVQHKFlrigvrcqAYDDAhimlmsaaLLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
327-432 |
3.86e-05 |
|
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: 44.18 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 327 CRIPVEVELAHEFRYRdPI--IDENTLVVSISQSGETMDTLMA-VRYAKEQGARTLSICNTNGStiPRESDAVLYLHAGP 403
Cdd:cd05009 39 SYIHAEAYSAGEFKHG-PIalVDEGTPVIFLAPEDRLEEKLESlIKEVKARGAKVIVITDDGDA--KDLADVVIRVPATV 115
|
90 100
....*....|....*....|....*....
gi 2578770988 404 EIAVAstkafLAMIAASYLLGLYLAQLRG 432
Cdd:cd05009 116 EELSP-----LLYIVPLQLLAYHLAVARG 139
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
344-462 |
8.62e-05 |
|
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: 43.72 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 344 PIIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHagpeiavASTKAFLAMIAASyll 423
Cdd:cd05005 71 PAIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIP-------AATKDDHGGEHKS--- 140
|
90 100 110
....*....|....*....|....*....|....*....
gi 2578770988 424 glylAQLRGQLFrEEIKDILADLhkIPAKIQKILDSSED 462
Cdd:cd05005 141 ----IQPLGTLF-EQSALVFLDA--VIAKLMEELGVSEE 172
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
345-416 |
2.60e-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: 43.43 E-value: 2.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2578770988 345 IIDENTLVVSISQSGETMDTLMAVRYAKEQGARTLSICNTNGSTIPRESDAVLYLHAGPE------IAVASTKAFLAM 416
Cdd:COG0794 88 MITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREacplnlAPTTSTTATLAL 165
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
348-411 |
1.82e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 40.83 E-value: 1.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2578770988 348 ENTLVVSISQSGETMDTLMAVRYAKEQGARTLSI-CNtNGSTIPRESDAVLYLHAGPEIAVASTK 411
Cdd:PRK12570 127 ADDVVVGIAASGRTPYVIGALEYAKQIGATTIALsCN-PDSPIAKIADIAISPVVGPEVLTGSTR 190
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
459-584 |
2.48e-03 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 40.30 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 459 SSEDIKALARAMKDTPSVLFLGRHVGFPVALEGALKLKELAY-IHAEGFAAGELKHGPIALIEQDqpVFVVVpSPRGRds 537
Cdd:COG1737 120 DEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKnVVLLDGDGHLQAESAALLGPGD--VVIAI-SFSGY-- 194
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2578770988 538 lHSKVVSNIQEVRARGAKTITVAEAGDDAVREFSETVFFVPETSPLL 584
Cdd:COG1737 195 -TRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTL 240
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
476-611 |
2.73e-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: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2578770988 476 VLFLGRHVGFPVALEGALKLKELA--YIHAEGFAAGELKHGPIALIEQDQPVFVVVPS-PRGR----DSLhskvvsniQE 548
Cdd:cd05010 1 VVYLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNdPYTRqydlDLL--------KE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2578770988 549 VRARG--AKTITVAEAGDDAVREFSETVFFVPETSP---LLMPLLttVPLQIFACALAAEKGYDVDQP 611
Cdd:cd05010 73 LRRDGiaARVIAISPESDAGIEDNSHYYLPGSRDLDdvyLAFPYI--LYAQLFALFNSIALGLTPDNP 138
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
486-562 |
8.37e-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: 35.81 E-value: 8.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2578770988 486 PVALEGALKLKELAYIHAEGFAAGELKHGPIALIEQDQPVFVVVpSPRGRdslHSKVVSNIQEVRARGAKTITVAEA 562
Cdd:cd04795 11 AIAAYFALELLELTGIEVVALIATELEHASLLSLLRKGDVVIAL-SYSGR---TEELLAALEIAKELGIPVIAITDA 83
|
|
| |
