|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
28-706 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 926.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 28 GIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDggNDKDWEANACKIqlIKKKGKVKALDEEVHK---QQDM 104
Cdd:PLN02981 3 GIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLV--FREEGKIESLVRSVYEevaETDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 105 DLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 184
Cdd:PLN02981 79 NLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 185 YD--NRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtGKDKKGScn 262
Cdd:PLN02981 159 FDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKEL--------------PEEKNSS-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 263 lSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPG---------RAVQT 333
Cdd:PLN02981 223 -AVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGglsrpasveRALST 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 334 LQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDD----YTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVAT 409
Cdd:PLN02981 302 LEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGsgkaKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 410 RQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHI 489
Cdd:PLN02981 382 RPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 490 NAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMG 569
Cdd:PLN02981 462 NAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 570 RGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKED 649
Cdd:PLN02981 542 RGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGD 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613076 650 TETIKNTK--RTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 706
Cdd:PLN02981 622 ASSVCPSGgcRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
28-706 |
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: 781.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 28 GIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdld 107
Cdd:COG0449 3 GIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAVLDDG---------GLEVRKAVGKLANLEEKLAEE------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 108 iEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDn 187
Cdd:COG0449 62 -PLSGTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLK- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 188 resQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscnlsrvd 267
Cdd:COG0449 139 ---GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL-----------------GEG----------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 268 sttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDhpgRAVQTLQMELQQIMKGNFS 347
Cdd:COG0449 188 -------------ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE---REVKTVDWDAEAAEKGGYP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 348 SFMQKEIFEQPESVVNTMRGRVNfDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELAS 427
Cdd:COG0449 252 HFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIAS 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 428 DFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQF 507
Cdd:COG0449 331 EFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 508 VSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKE 586
Cdd:COG0449 411 AALYLLALYLARARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKE 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 587 ITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSV 666
Cdd:COG0449 491 ISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEVD 570
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1034613076 667 DCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 706
Cdd:COG0449 571 ELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
28-706 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 727.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 28 GIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAGVG-FDGGNdkdweanackIQLIKKKGKVKALDEEVHKQqdmdl 106
Cdd:PRK00331 3 GIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAvLDDGG----------LEVRKAVGKVANLEAKLEEE----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 107 diEFDVHLGIAHTRWATHGEPSPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 186
Cdd:PRK00331 62 --PLPGTTGIGHTRWATHGKPTERNAHPHT-DCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 187 nresQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscnlsrv 266
Cdd:PRK00331 139 ----EGGDLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL-----------------GEG---------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 267 dsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVvdGRLSIHrIKRTAGDHPGRAVQTLQMELQQIMKGNF 346
Cdd:PRK00331 188 --------------ENFLASDALALLPYTRRVIYLEDGEIAVL--TRDGVE-IFDFDGNPVEREVYTVDWDASAAEKGGY 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 347 SSFMQKEIFEQPESVVNTMRGRVNFDdytvnlGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELA 426
Cdd:PRK00331 251 RHFMLKEIYEQPEAIRDTLEGRLDEL------GEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 427 SDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQ 506
Cdd:PRK00331 325 SEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQ 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 507 FVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIK 585
Cdd:PRK00331 405 LAVLYLLALALAKARGTLsAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLK 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 586 EITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDtETIKNTKRTIKVPHS 665
Cdd:PRK00331 485 EISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGD-EVAEEADDVIEVPEV 563
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1034613076 666 VDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 706
Cdd:PRK00331 564 HELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
28-706 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 716.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 28 GIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQ------LIKKKGKVKALDEEVHKQ 101
Cdd:PTZ00394 3 GIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAASAptprpcVVRSVGNISQLREKVFSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 102 QD----MDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETI 177
Cdd:PTZ00394 83 AVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 178 AKLVKYMYDNRESQdtSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSehklstdhipilyrtGKDK 257
Cdd:PTZ00394 162 SVLSEYLYTRKGIH--NFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRR---------------TDDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 258 KGSCNLSRVDsttclFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPGRAVQTLQME 337
Cdd:PTZ00394 225 GCVMKLQTYD-----LTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQHLDAK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 338 LQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDH-IKEIQRCRRLILIACGTSYHAGVATRQVLEEL 416
Cdd:PTZ00394 300 PEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPLFEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 417 TELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIG 496
Cdd:PTZ00394 380 VPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 497 VASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSM-DDEIQKLATELYHQKSVLIMGRGYHYA 575
Cdd:PTZ00394 460 VASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYDLA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 576 TCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKN 655
Cdd:PTZ00394 540 TAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAA 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1034613076 656 TKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 706
Cdd:PTZ00394 620 ASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
28-706 |
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: 633.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 28 GIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGFdggndkdweANACKIQLIKKKGKVKALDEEVhkqQDMDLD 107
Cdd:TIGR01135 2 GIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAV---------VDEGKLFVRKAVGKVAELANKL---GEKPLP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 108 IEFdvhlGIAHTRWATHGEPSPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDN 187
Cdd:TIGR01135 64 GGV----GIGHTRWATHGKPTDENAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 188 resqDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtGKDkkgscnlsrvd 267
Cdd:TIGR01135 139 ----GGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGL-----------------GDG----------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 268 sttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKrtaGDHPGRAVQTLQMELQQIMKGNFS 347
Cdd:TIGR01135 187 -------------ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFE---GAPVQREVRVIDWDLDAAEKGGYR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 348 SFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIqrcRRLILIACGTSYHAGVATRQVLEELTELPVMVELAS 427
Cdd:TIGR01135 251 HFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNI---DRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIAS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 428 DFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQF 507
Cdd:TIGR01135 328 EFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 508 VSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKE 586
Cdd:TIGR01135 408 TVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKE 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 587 ITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSV 666
Cdd:TIGR01135 488 ISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEVE 567
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1034613076 667 DCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 706
Cdd:TIGR01135 568 ELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
18-705 |
8.21e-153 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 457.56 E-value: 8.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 18 KKMNAHATASGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVG-FDGGND------KDWEANACKIQLIKKKGK 90
Cdd:PTZ00295 16 KKSRFYDYCCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGElkttkyASDGTTSDSIEILKEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 91 vkaldeEVHKQQdmdldiefdvHLGIAHTRWATHGEPSPVNSHPQrSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFES 170
Cdd:PTZ00295 90 ------DSHKNS----------TIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 171 ETDTETIAKLVKYMYDNRESqdtsFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklSTDHIpil 250
Cdd:PTZ00295 153 ETDSEVIANLIGLELDQGED----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGI------GDDSI--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 251 yrtgkdkkgscnlsrvdsttclfpveekaveyYFASDASAVIEHTNRVIFLEDDDVAAV-VDGRLSIHRIKRtagdhpgr 329
Cdd:PTZ00295 220 --------------------------------YVASEPSAFAKYTNEYISLKDGEIAELsLENVNDLYTQRR-------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 330 aVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTM--RGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGV 407
Cdd:PTZ00295 260 -VEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAAL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 408 ATRQVLEELTEL-PVMVELASDF-LDRNTpvfRDDVCF-FLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETD 484
Cdd:PTZ00295 339 FAASIMQKLKCFnTVQVIDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTD 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 485 CGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDR-ISMQE-RRKEIMLGLKRLPDLIKEVL-SMDDEIQKLATELYH 561
Cdd:PTZ00295 416 CGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNyKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKN 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 562 QKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKL--MPVIMIIMRDHTYAKCQNALQQVVARQG 639
Cdd:PTZ00295 496 AKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKARGA 575
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613076 640 RPVVICDKEDtETIKNTKRTIKVPhSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTV 705
Cdd:PTZ00295 576 YIIVITDDED-LVKDFADEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
28-309 |
7.68e-109 |
|
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: 328.64 E-value: 7.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 28 GIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdld 107
Cdd:cd00714 2 GIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---------SLEVVKAVGKVANLEEKLAEK------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 108 iEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNnEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDn 187
Cdd:cd00714 61 -PLSGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 188 resQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtgkdkkgscnlsrvd 267
Cdd:cd00714 138 ---GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG---------------------------- 186
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034613076 268 sttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAV 309
Cdd:cd00714 187 -------------ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
352-706 |
8.86e-69 |
|
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: 228.63 E-value: 8.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 352 KEIFEQPESVVNTmrgrvnFDDYTVNLGGLKDHIKEIQRcRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLD 431
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 432 RNTPVFRD-DVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSL 510
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 511 VM-FALMMCDDrismqerrkEIMLGLKRLPDLIKEVLSMDDEIQKLAtELYHQKSVLIMGRGYHYATCLEGALKIKEITY 589
Cdd:COG2222 155 LAlLAAWGGDD---------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 590 MHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTEtikntkrtIKVPHSVDC- 668
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAA--------ITLPAIPDLh 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034613076 669 --LQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 706
Cdd:COG2222 297 daLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
550-704 |
1.87e-68 |
|
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: 220.98 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 550 DEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQN 629
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613076 630 ALQQVVARQGRPVVICDKEDTETIKNTkrTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVT 704
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAKDLADV--VIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
393-518 |
1.34e-61 |
|
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: 201.96 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 393 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGIT 472
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034613076 473 NTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMC 518
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
28-307 |
1.86e-49 |
|
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: 172.63 E-value: 1.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 28 GIFAYLNYHVPRTRReiLETLIKGLQRLEYRGYDSAGVGFDGGndkdweanackiqlikKKGKVKALDEEVHKQQDMDLD 107
Cdd:cd00352 2 GIFGIVGADGAASLL--LLLLLRGLAALEHRGPDGAGIAVYDG----------------DGLFVEKRAGPVSDVALDLLD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 108 IEFDVHLGIAHTRWATHGEPSPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDN 187
Cdd:cd00352 64 EPLKSGVALGHVRLATNGLPSEANAQPFRSE-DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 188 REsqdtsFTTLVERVIQQLEGAFALVFKSVHfPGQAVGTRRG---SPLLIGVRSEHklstdhipilyrtgkdkkgscnls 264
Cdd:cd00352 143 GG-----LFEAVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGITKDG------------------------ 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034613076 265 rvdsttclfpveekavEYYFASDASAVIEHT-NRVIFLEDDDVA 307
Cdd:cd00352 193 ----------------GLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
387-516 |
2.58e-40 |
|
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: 143.98 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 387 EIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFLSQSGETADTLMGLRYCKERG 465
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034613076 466 ALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALM 516
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
558-689 |
9.34e-33 |
|
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: 122.79 E-value: 9.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 558 ELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQnALQQVVAR 637
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1034613076 638 QGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLR 689
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
51-237 |
6.87e-21 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 92.52 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 51 GLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVkaldEEVHKQQDMDldiEFDVHLGIAHTRWATHGEPSP 129
Cdd:cd00715 19 GLYALQHRGQESAGiATSDGK----------RFHTHKGMGLV----SDVFDEEKLR---RLPGNIAIGHVRYSTAGSSSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 130 VNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnRESQDTSFTTLVERVIQQLEG 208
Cdd:cd00715 82 ENAQPFVVNSPLGGIALaHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA-----RSLAKDDLFEAIIDALERVKG 156
|
170 180
....*....|....*....|....*....
gi 1034613076 209 AFALVFksvhfpgqavGTRRGsplLIGVR 237
Cdd:cd00715 157 AYSLVI----------MTADG---LIAVR 172
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
51-214 |
4.16e-19 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 90.85 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 51 GLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDMDldiEFDVHLGIAHTRWATHGEPSP 129
Cdd:COG0034 26 GLYALQHRGQESAGiATSDGG----------RFHLHKGMGLVS----DVFDEEDLE---RLKGNIAIGHVRYSTTGSSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 130 VNSHP-QRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnRESQDTSFTTLVERVIQQLEG 208
Cdd:COG0034 89 ENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA-----RELTKEDLEEAIKEALRRVKG 163
|
....*.
gi 1034613076 209 AFALVF 214
Cdd:COG0034 164 AYSLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
51-237 |
9.30e-18 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 86.60 E-value: 9.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 51 GLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKaldeEVHKQQDMDldiEFDVHLGIAHTRWATHGEPSPV 130
Cdd:TIGR01134 20 GLYALQHRGQESAGISVFDGN---------RFRLHKGNGLVS----DVFNEEHLQ---RLKGNVGIGHVRYSTAGSSGLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 131 NSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYmydNRESQDTSFTTlVERVIQQLEGA 209
Cdd:TIGR01134 84 NAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAH---NDESKDDLFDA-VARVLERVRGA 159
|
170 180 190
....*....|....*....|....*....|....
gi 1034613076 210 FALVFKSVHF------PgqaVGTRrgsPLLIGVR 237
Cdd:TIGR01134 160 YALVLMTEDGlvavrdP---HGIR---PLVLGRR 187
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
51-238 |
1.92e-15 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 79.34 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 51 GLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDMDldiEFDVHLGIAHTRWATHGEPSP 129
Cdd:PLN02440 20 GLHALQHRGQEGAGiVTVDGN----------RLQSITGNGLVS----DVFDESKLD---QLPGDIAIGHVRYSTAGASSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 130 VNSHPqrsdknneFI---------VIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnrESQDTSFTTLVE 200
Cdd:PLN02440 83 KNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIA------ISKARPFFSRIV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034613076 201 RVIQQLEGAFALVFKsvhFPGQAVGTR-----RgsPLLIGVRS 238
Cdd:PLN02440 149 DACEKLKGAYSMVFL---TEDKLVAVRdphgfR--PLVMGRRS 186
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
393-484 |
3.42e-14 |
|
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: 69.53 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 393 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFLSQSGETADTLMGLRYCKERGALTVGI 471
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 1034613076 472 TNTVGSSISRETD 484
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
51-213 |
3.56e-14 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 75.46 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 51 GLQRLEYRGYDSAGVGFdggndkdweANACKIQLIKKKGKVkaldEEVHKQQDMDldiEFDVHLGIAHTRWATHGEPSPV 130
Cdd:PRK05793 35 GLYALQHRGQESAGIAV---------SDGEKIKVHKGMGLV----SEVFSKEKLK---GLKGNSAIGHVRYSTTGASDLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 131 NSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnRESQdTSFTTLVERVIQQLEGA 209
Cdd:PRK05793 99 NAQPLVANYKLGSIAIaHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIA-----RSAK-KGLEKALVDAIQAIKGS 172
|
....
gi 1034613076 210 FALV 213
Cdd:PRK05793 173 YALV 176
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
115-214 |
4.03e-13 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 66.56 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 115 GIAHTRWATHGEPS----PVNShpqrSDKNneFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkYMYdnres 190
Cdd:pfam13522 13 ALGHVRLAIVDLPDagnqPMLS----RDGR--LVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL--YEE----- 79
|
90 100
....*....|....*....|....
gi 1034613076 191 qdtsfttLVERVIQQLEGAFALVF 214
Cdd:pfam13522 80 -------WGEDCLERLRGMFAFAI 96
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
28-185 |
2.67e-12 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 67.29 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 28 GIFAYLNyhvpRTRREIL-ETLIKGLQRLEYRG-YDSAGVGFDGGND-------KDweanackIQLIKKKGkvkaLDEEV 98
Cdd:cd01907 2 GIFGIMS----KDGEPFVgALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgKD-------MEVFKGVG----YPEDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 99 HKQQDMDldiEFDVHLGIAHTRWATHgepSPVN---SHPqrsdknneF-----IVIHNGIITNYKDLKKFLESKGYDFES 170
Cdd:cd01907 67 ARRYDLE---EYKGYHWIAHTRQPTN---SAVWwygAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFET 132
|
170
....*....|....*
gi 1034613076 171 ETDTETIAKLVKYMY 185
Cdd:cd01907 133 ETDTEVIAYYLDLLL 147
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
134-213 |
3.00e-12 |
|
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: 64.08 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 134 PQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYdnresqdtsfttlVERVIQQLEGAFALV 213
Cdd:pfam13537 15 PMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW-------------GEDCVDRLNGMFAFA 81
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
445-516 |
1.59e-10 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 62.88 E-value: 1.59e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613076 445 LSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--ALM 516
Cdd:PRK05441 138 IAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstGVM 213
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
426-517 |
6.57e-10 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 60.23 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 426 ASDFLDRNTPvfRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 503
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90
....*....|....*.
gi 1034613076 504 TSQFVSLVMF--ALMM 517
Cdd:cd05007 186 TAQKLALNMLstAVMI 201
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
393-694 |
1.18e-09 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 60.40 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 393 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFL--SQSGETADTLMGLRYCKERGALTVG 470
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 471 ITNTVGSSISRETDCGVHINAGPEIGVASTKAYTsqfVSLVMFAlmmcddRISMQERRKEIMLGLKRLPDLIKEVLSMDD 550
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMIT------RLAPNAEIGKIKNDLKQLPNALGHLVRTWE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 551 EIQKLATELYHQKSVL-------IMGRGYHyatclEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHT 623
Cdd:PRK11382 196 EKGRQLGELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDES 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034613076 624 YAKCQNALQQVVARQGRPVVICDKEDTETIKntkrtikvphsvDCLQGILSVIPLQLLAFHLAVLRGYDVD 694
Cdd:PRK11382 271 RHTTERAINFVKQRTDNVIVIDYAEISQGLH------------PWLAPFLMFVPMEWLCYYLSIYKDHNPD 329
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
394-472 |
2.45e-09 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 54.69 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 394 LILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFLSQSGETADTLMGLRYCKERGALTVGI 471
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1034613076 472 T 472
Cdd:cd04795 81 T 81
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
27-213 |
9.89e-09 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 56.03 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 27 SGIFAYLNYHVPRTRREILETLikgLQRLEYRGYDSAGvgfdggndkdweanackiqlikkkgkvkaldeevhkqqdmdl 106
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERM---LDALAHRGPDGSG------------------------------------------ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 107 dIEFDVHLGIAHTRWATHGepsPVNSH-PQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkYM- 184
Cdd:cd00712 36 -IWIDEGVALGHRRLSIID---LSGGAqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL--YEe 108
|
170 180
....*....|....*....|....*....
gi 1034613076 185 YDnresqdtsfttlvERVIQQLEGAFALV 213
Cdd:cd00712 109 WG-------------EDCLERLNGMFAFA 124
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
426-516 |
1.16e-08 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 57.02 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 426 ASDFLDRN-TPvfrDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIgVA-ST--K 501
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 1034613076 502 AYTSQFVSLVMF--ALM 516
Cdd:COG2103 198 AGTAQKLVLNMLstAAM 214
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
392-518 |
2.13e-08 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 52.93 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 392 RRLILIACGTSYHAG---VATRQVleelTELPvmvelaSDFLDrntP----------VFRDDVCFFLSQSGETADTLMGL 458
Cdd:cd05014 1 GKVVVTGVGKSGHIArkiAATLSS----TGTP------AFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613076 459 RYCKERGALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFVSLVMF-ALMMC 518
Cdd:cd05014 68 PHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALGdALAVA 128
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
385-512 |
3.55e-08 |
|
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: 52.62 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 385 IKEIQRCRRLILIACGTSYHAG--VATRqvleeLTELPVMVELASD---FLDRNTPVFRDDVCFFLSQSGETADTLMGLR 459
Cdd:cd05013 7 VDLLAKARRIYIFGVGSSGLVAeyLAYK-----LLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034613076 460 YCKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM 512
Cdd:cd05013 82 IAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
385-518 |
6.17e-07 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 51.47 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 385 IKEIQRCRRLILIACGTSYHAGVATRQVLEEL----TELPVMVELASDFLDRNTPvfrDDVCFFLSQSGETADTLMGLRY 460
Cdd:COG1737 128 VDLLAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARL 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613076 461 CKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVMF-ALMMC 518
Cdd:COG1737 205 AKERGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALIdALAAA 261
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
27-180 |
1.03e-06 |
|
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: 51.76 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 27 SGIFAYLNYHVPRTRreilETLIKGLQRLEYRGYDSAGVGFDGgndkdweanackiqlikkkgkvkaldeevhkqqdmdl 106
Cdd:COG0367 2 CGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------- 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613076 107 diefdvHLGIAHTRWATHGEPSpvNSHpQ-RSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKL 180
Cdd:COG0367 41 ------GVALGHRRLSIIDLSE--GGH-QpMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
113-181 |
1.65e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 49.96 E-value: 1.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613076 113 HLGIAHTRWATHGEPSPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-----ESETDTETIAKLV 181
Cdd:COG0121 77 RLVIAHVRKATVGPVSLENTHPFRGG---RWLFAHNGQLDGFDRLRRRLAEELPDElyfqpVGTTDSELAFALL 147
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
438-518 |
5.43e-06 |
|
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: 48.82 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 438 RDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDcgVHINAGPE-----IGVASTkayTSQFVSLVM 512
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
....*..
gi 1034613076 513 F-ALMMC 518
Cdd:COG0794 166 GdALAVA 172
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
145-214 |
7.47e-06 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 48.87 E-value: 7.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 145 VIHNGIITNYKDLKKFLESKGYDFESETDTETIakLVKYMYDNresqdtsfttlvERVIQQLEGAFALVF 214
Cdd:TIGR01536 70 IVFNGEIYNHEELREELEAKGYTFQTDSDTEVI--LHLYEEWG------------EECVDRLDGMFAFAL 125
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
113-180 |
3.31e-05 |
|
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: 46.23 E-value: 3.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613076 113 HLGIAHTRWATHGEPSPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-ESETDTETIAKL 180
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFAL 146
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
138-213 |
9.54e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 45.48 E-value: 9.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613076 138 DKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYmYDNREsqdtsfttlverVIQQLEGAFALV 213
Cdd:PTZ00077 70 DDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKE-YGPKD------------FWNHLDGMFATV 132
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
439-513 |
1.26e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 44.68 E-value: 1.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613076 439 DDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF 513
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
144-298 |
3.25e-04 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 43.74 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 144 IVIHNGIITNYKDLKKFLESKgYDFESETDTETIAKLvkYmydnrESQDTSFttlvervIQQLEGAFALVfksvhfpgqa 223
Cdd:PRK09431 71 VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL--Y-----QEKGPDF-------LDDLDGMFAFA---------- 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613076 224 vgtrrgspLLIGVRSEHKLSTDHIPI--LYrTGKDKKGscnlsrvdsttclfpveekavEYYFASDASAVIEHTNRV 298
Cdd:PRK09431 126 --------LYDSEKDAYLIARDPIGIipLY-YGYDEHG---------------------NLYFASEMKALVPVCKTI 172
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
565-647 |
5.51e-04 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 39.28 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 565 VLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGP-LALVDKLMPVIMIIMRdHTYAKCQNALQQVVARQGRPVV 643
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYS-GRTEELLAALEIAKELGIPVIA 79
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....
gi 1034613076 644 ICDK 647
Cdd:cd04795 80 ITDA 83
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| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
113-232 |
1.97e-03 |
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Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 40.78 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613076 113 HLGIAHTRWATHGEPSPVNSHP-QRSDKNNEFIVIHNGiitnykDLKKFLESKGYDFE--SETDTETI-----AKLVKYM 184
Cdd:pfam13230 72 RNVIAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNG------DLKGYAPKLSGRFQpvGSTDSELAfcwllDRLASRF 145
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1034613076 185 YDNRESQDTSFTTLVE--RVIQQLeGAFALVFKSvhfpGQAVGTRRGSPL 232
Cdd:pfam13230 146 PYARPSAGELFRALRElaREIAAH-GTFNFLLSD----GRDLFAHCSTRL 190
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