|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
121-799 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 921.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDggNDKDWEANACKIqlIKKKGKVKALDEEVHK---QQDM 197
Cdd:PLN02981 3 GIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLV--FREEGKIESLVRSVYEevaETDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 198 DLDIEFDVHFGIAHTRWATHGEPNPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 277
Cdd:PLN02981 79 NLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 278 YD--NQESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIAVRSEhklstdhipilyrtGKDKKGScn 355
Cdd:PLN02981 159 FDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKEL--------------PEEKNSS-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 356 lSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPG---------RAVQT 426
Cdd:PLN02981 223 -AVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGglsrpasveRALST 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 427 LQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDD----YTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVAT 502
Cdd:PLN02981 302 LEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGsgkaKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 503 RQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHI 582
Cdd:PLN02981 382 RPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 583 NAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMG 662
Cdd:PLN02981 462 NAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 663 RGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKED 742
Cdd:PLN02981 542 RGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGD 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622854038 743 TETIKNTK--RTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 799
Cdd:PLN02981 622 ASSVCPSGgcRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
121-799 |
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: 772.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdld 200
Cdd:COG0449 3 GIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAVLDDG---------GLEVRKAVGKLANLEEKLAEE------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 201 iEFDVHFGIAHTRWATHGEPNPVNSHPQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDn 280
Cdd:COG0449 62 -PLSGTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLK- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 281 qesQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIAVrsehklstdhipilyrtGKDkkgscnlsrvd 360
Cdd:COG0449 139 ---GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL-----------------GEG----------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 361 sttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDhpgRAVQTLQMELQQIMKGNFS 440
Cdd:COG0449 188 -------------ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE---REVKTVDWDAEAAEKGGYP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 441 SFMQKEIFEQPESVVNTMRGRVNfDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELAS 520
Cdd:COG0449 252 HFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIAS 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 521 DFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQF 600
Cdd:COG0449 331 EFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 601 VSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKE 679
Cdd:COG0449 411 AALYLLALYLARARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKE 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 680 ITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSV 759
Cdd:COG0449 491 ISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEVD 570
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1622854038 760 DCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 799
Cdd:COG0449 571 ELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
121-799 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 721.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAGVG-FDGGNdkdweanackIQLIKKKGKVKALDEEVHKQqdmdl 199
Cdd:PRK00331 3 GIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAvLDDGG----------LEVRKAVGKVANLEAKLEEE----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 200 diEFDVHFGIAHTRWATHGEPNPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 279
Cdd:PRK00331 62 --PLPGTTGIGHTRWATHGKPTERNAHPHT-DCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 280 nqesQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIAVrsehklstdhipilyrtGKDkkgscnlsrv 359
Cdd:PRK00331 139 ----EGGDLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL-----------------GEG---------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 360 dsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVvdGRLSIHrIKRTAGDHPGRAVQTLQMELQQIMKGNF 439
Cdd:PRK00331 188 --------------ENFLASDALALLPYTRRVIYLEDGEIAVL--TRDGVE-IFDFDGNPVEREVYTVDWDASAAEKGGY 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 440 SSFMQKEIFEQPESVVNTMRGRVNFDdytvnlGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELA 519
Cdd:PRK00331 251 RHFMLKEIYEQPEAIRDTLEGRLDEL------GEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 520 SDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQ 599
Cdd:PRK00331 325 SEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQ 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 600 FVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIK 678
Cdd:PRK00331 405 LAVLYLLALALAKARGTLsAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLK 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 679 EITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDtETIKNTKRTIKVPHS 758
Cdd:PRK00331 485 EISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGD-EVAEEADDVIEVPEV 563
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1622854038 759 VDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 799
Cdd:PRK00331 564 HELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
121-799 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 708.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQ------LIKKKGKVKALDEEVHKQ 194
Cdd:PTZ00394 3 GIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAASAptprpcVVRSVGNISQLREKVFSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 195 QD----MDLDIEFDVHFGIAHTRWATHGEPNPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETI 270
Cdd:PTZ00394 83 AVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 271 AKLVKYMYDNQESQdtSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIAVRSehklstdhipilyrtGKDK 350
Cdd:PTZ00394 162 SVLSEYLYTRKGIH--NFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRR---------------TDDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 351 KGSCNLSRVDsttclFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPGRAVQTLQME 430
Cdd:PTZ00394 225 GCVMKLQTYD-----LTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQHLDAK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 431 LQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDH-IKEIQRCRRLILIACGTSYHAGVATRQVLEEL 509
Cdd:PTZ00394 300 PEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVRPLFEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 510 TELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIG 589
Cdd:PTZ00394 380 VPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 590 VASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSM-DDEIQKLATELYHQKSVLIMGRGYHYA 668
Cdd:PTZ00394 460 VASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYDLA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 669 TCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKN 748
Cdd:PTZ00394 540 TAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAA 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1622854038 749 TKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 799
Cdd:PTZ00394 620 ASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
121-799 |
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: 628.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGFdggndkdweANACKIQLIKKKGKVKALDEEVhkqQDMDLD 200
Cdd:TIGR01135 2 GIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAV---------VDEGKLFVRKAVGKVAELANKL---GEKPLP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 201 iefdVHFGIAHTRWATHGEPNPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDN 280
Cdd:TIGR01135 64 ----GGVGIGHTRWATHGKPTDENAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 281 QESqdtsFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIAVrsehklstdhipilyrtGKDkkgscnlsrvd 360
Cdd:TIGR01135 139 GGD----LLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGL-----------------GDG----------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 361 sttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKrtaGDHPGRAVQTLQMELQQIMKGNFS 440
Cdd:TIGR01135 187 -------------ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFE---GAPVQREVRVIDWDLDAAEKGGYR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 441 SFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIqrcRRLILIACGTSYHAGVATRQVLEELTELPVMVELAS 520
Cdd:TIGR01135 251 HFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNI---DRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIAS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 521 DFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQF 600
Cdd:TIGR01135 328 EFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 601 VSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKE 679
Cdd:TIGR01135 408 TVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKE 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 680 ITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSV 759
Cdd:TIGR01135 488 ISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEVE 567
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1622854038 760 DCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 799
Cdd:TIGR01135 568 ELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
121-798 |
1.38e-150 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 455.25 E-value: 1.38e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVG-FDGGND------KDWEANACKIQLIKKKGKvkaldeEVHK 193
Cdd:PTZ00295 26 GIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGElkttkyASDGTTSDSIEILKEKLL------DSHK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 194 QQdmdldiefdvHFGIAHTRWATHGEPNPVNSHPQrSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKL 273
Cdd:PTZ00295 94 NS----------TIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 274 VKYMYDNQESqdtsFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIAVrsehklSTDHIpilyrtgkdkkgs 353
Cdd:PTZ00295 163 IGLELDQGED----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGI------GDDSI------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 354 cnlsrvdsttclfpveekaveyYFASDASAVIEHTNRVIFLEDDDVAAV-VDGRLSIHRIKRtagdhpgraVQTLQMELQ 432
Cdd:PTZ00295 220 ----------------------YVASEPSAFAKYTNEYISLKDGEIAELsLENVNDLYTQRR---------VEKIPEEVI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 433 QIMKGNFSSFMQKEIFEQPESVVNTM--RGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELT 510
Cdd:PTZ00295 269 EKSPEPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 511 EL-PVMVELASDF-LDRNTpvfRDDVCF-FLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPE 587
Cdd:PTZ00295 349 CFnTVQVIDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGRE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 588 IGVASTKAYTSQFVSLVMFALMMCDDR-ISMQE-RRKEIMLGLKRLPDLIKEVL-SMDDEIQKLATELYHQKSVLIMGRG 664
Cdd:PTZ00295 426 VAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNyKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKNAKSMFILGKG 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 665 YHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKL--MPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKED 742
Cdd:PTZ00295 506 LGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKARGAYIIVITDDED 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622854038 743 tETIKNTKRTIKVPhSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTV 798
Cdd:PTZ00295 586 -LVKDFADEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
121-402 |
1.75e-106 |
|
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: 325.17 E-value: 1.75e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdld 200
Cdd:cd00714 2 GIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---------SLEVVKAVGKVANLEEKLAEK------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 201 iEFDVHFGIAHTRWATHGEPNPVNSHPQRSDKNnEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDn 280
Cdd:cd00714 61 -PLSGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 281 qesQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIAVRSEhklstdhipilyrtgkdkkgscnlsrvd 360
Cdd:cd00714 138 ---GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG---------------------------- 186
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622854038 361 sttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAV 402
Cdd:cd00714 187 -------------ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
445-799 |
1.85e-67 |
|
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: 226.70 E-value: 1.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 445 KEIFEQPESVVNTmrgrvnFDDYTVNLGGLKDHIKEIQRcRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLD 524
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 525 RNTPVFRD-DVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSL 603
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 604 VM-FALMMCDDrismqerrkEIMLGLKRLPDLIKEVLSMDDEIQKLAtELYHQKSVLIMGRGYHYATCLEGALKIKEITY 682
Cdd:COG2222 155 LAlLAAWGGDD---------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 683 MHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTEtikntkrtIKVPHSVDC- 761
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAA--------ITLPAIPDLh 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622854038 762 --LQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 799
Cdd:COG2222 297 daLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
643-797 |
2.30e-67 |
|
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: 219.83 E-value: 2.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 643 DEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQN 722
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622854038 723 ALQQVVARQGRPVVICDKEDTETIKNTkrTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVT 797
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 ... |
486-611 |
6.19e-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: 201.57 E-value: 6.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 486 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGIT 565
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622854038 566 NTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMC 611
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
121-400 |
4.90e-48 |
|
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: 169.55 E-value: 4.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLNYHVPRTRReiLETLIKGLQRLEYRGYDSAGVGFDGGndkdweanackiqlikKKGKVKALDEEVHKQQDMDLD 200
Cdd:cd00352 2 GIFGIVGADGAASLL--LLLLLRGLAALEHRGPDGAGIAVYDG----------------DGLFVEKRAGPVSDVALDLLD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 201 IEFDVHFGIAHTRWATHGEPNPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDN 280
Cdd:cd00352 64 EPLKSGVALGHVRLATNGLPSEANAQPFRSE-DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 281 QEsqdtsFTTLVERVIQQLEGAFALVFKSVHfpgqavgTRRgsplLIAVRSEHKLStdhiPILYRTGKDKkgscnlsrvd 360
Cdd:cd00352 143 GG-----LFEAVEDALKRLDGPFAFALWDGK-------PDR----LFAARDRFGIR----PLYYGITKDG---------- 192
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622854038 361 sttclfpveekavEYYFASDASAVIEHT-NRVIFLEDDDVA 400
Cdd:cd00352 193 -------------GLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
480-609 |
4.65e-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: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 480 EIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFLSQSGETADTLMGLRYCKERG 558
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622854038 559 ALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALM 609
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
651-782 |
1.30e-32 |
|
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: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 651 ELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQnALQQVVAR 730
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622854038 731 QGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLR 782
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
144-330 |
1.99e-19 |
|
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: 88.67 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 144 GLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVkaldEEVHKQQDMDldiEFDVHFGIAHTRWATHGEPNP 222
Cdd:cd00715 19 GLYALQHRGQESAGiATSDGK----------RFHTHKGMGLV----SDVFDEEKLR---RLPGNIAIGHVRYSTAGSSSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 223 VNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnQESQDTSFTTLVERVIQQLEG 301
Cdd:cd00715 82 ENAQPFVVNSPLGGIALaHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA-----RSLAKDDLFEAIIDALERVKG 156
|
170 180
....*....|....*....|....*....
gi 1622854038 302 AFALVFksvhfpgqavGTRRGsplLIAVR 330
Cdd:cd00715 157 AYSLVI----------MTADG---LIAVR 172
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
144-307 |
1.74e-17 |
|
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: 86.23 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 144 GLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDMDldiEFDVHFGIAHTRWATHGEPNP 222
Cdd:COG0034 26 GLYALQHRGQESAGiATSDGG----------RFHLHKGMGLVS----DVFDEEDLE---RLKGNIAIGHVRYSTTGSSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 223 VNSHP-QRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnQESQDTSFTTLVERVIQQLEG 301
Cdd:COG0034 89 ENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA-----RELTKEDLEEAIKEALRRVKG 163
|
....*.
gi 1622854038 302 AFALVF 307
Cdd:COG0034 164 AYSLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
144-333 |
2.43e-16 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 82.37 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 144 GLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKaldeEVHKQQDMDldiEFDVHFGIAHTRWATHGEPNPV 223
Cdd:TIGR01134 20 GLYALQHRGQESAGISVFDGN---------RFRLHKGNGLVS----DVFNEEHLQ---RLKGNVGIGHVRYSTAGSSGLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 224 NSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYdnqESQDTSFTTlVERVIQQLEGA 302
Cdd:TIGR01134 84 NAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHND---ESKDDLFDA-VARVLERVRGA 159
|
170 180 190
....*....|....*....|....*....|.
gi 1622854038 303 FALVFKSVHFpgqavgtrrgsplLIAVRSEH 333
Cdd:TIGR01134 160 YALVLMTEDG-------------LVAVRDPH 177
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
486-577 |
4.62e-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: 69.14 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 486 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFLSQSGETADTLMGLRYCKERGALTVGI 564
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 1622854038 565 TNTVGSSISRETD 577
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
144-307 |
9.83e-14 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 74.33 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 144 GLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDMDldiEFDVHFGIAHTRWATHGEPNP 222
Cdd:PLN02440 20 GLHALQHRGQEGAGiVTVDGN----------RLQSITGNGLVS----DVFDESKLD---QLPGDIAIGHVRYSTAGASSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 223 VNSHPqrsdknneFI---------VIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnqESQDTSFTTLVE 293
Cdd:PLN02440 83 KNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIA------ISKARPFFSRIV 148
|
170
....*....|....
gi 1622854038 294 RVIQQLEGAFALVF 307
Cdd:PLN02440 149 DACEKLKGAYSMVF 162
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
144-306 |
1.16e-13 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 74.30 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 144 GLQRLEYRGYDSAGVGFdggndkdweANACKIQLIKKKGKVkaldEEVHKQQDMDldiEFDVHFGIAHTRWATHGEPNPV 223
Cdd:PRK05793 35 GLYALQHRGQESAGIAV---------SDGEKIKVHKGMGLV----SEVFSKEKLK---GLKGNSAIGHVRYSTTGASDLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 224 NSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKymydnqESQDTSFTTLVERVIQQLEGA 302
Cdd:PRK05793 99 NAQPLVANYKLGSIAIaHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIA------RSAKKGLEKALVDAIQAIKGS 172
|
....
gi 1622854038 303 FALV 306
Cdd:PRK05793 173 YALV 176
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
208-307 |
2.79e-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: 67.33 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 208 GIAHTRWATHGEPN----PVNShpqrSDKNneFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkYMYdnqes 283
Cdd:pfam13522 13 ALGHVRLAIVDLPDagnqPMLS----RDGR--LVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL--YEE----- 79
|
90 100
....*....|....*....|....
gi 1622854038 284 qdtsfttLVERVIQQLEGAFALVF 307
Cdd:pfam13522 80 -------WGEDCLERLRGMFAFAI 96
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
227-306 |
3.40e-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: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 227 PQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYdnqesqdtsfttlVERVIQQLEGAFALV 306
Cdd:pfam13537 15 PMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW-------------GEDCVDRLNGMFAFA 81
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
121-278 |
9.97e-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: 65.75 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 121 GIFAYLNyhvpRTRREIL-ETLIKGLQRLEYRG-YDSAGVGFDGGND-------KDweanackIQLIKKKGkvkaLDEEV 191
Cdd:cd01907 2 GIFGIMS----KDGEPFVgALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgKD-------MEVFKGVG----YPEDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 192 HKQQDMDldiEFDVHFGIAHTRWATHGEPNPVNSHPqrsdknneF-----IVIHNGIITNYKDLKKFLESKGYDFESETD 266
Cdd:cd01907 67 ARRYDLE---EYKGYHWIAHTRQPTNSAVWWYGAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFETETD 135
|
170
....*....|..
gi 1622854038 267 TETIAKLVKYMY 278
Cdd:cd01907 136 TEVIAYYLDLLL 147
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
538-609 |
3.42e-10 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 62.11 E-value: 3.42e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622854038 538 LSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--ALM 609
Cdd:PRK05441 138 IAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstGVM 213
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
486-787 |
1.34e-09 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 60.40 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 486 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFL--SQSGETADTLMGLRYCKERGALTVG 563
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 564 ITNTVGSSISRETDCGVHINAGPEIGVASTKAYTsqfVSLVMFAlmmcddRISMQERRKEIMLGLKRLPDLIKEVLSMDD 643
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMIT------RLAPNAEIGKIKNDLKQLPNALGHLVRTWE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 644 EIQKLATELYHQKSVL-------IMGRGYHyatclEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHT 716
Cdd:PRK11382 196 EKGRQLGELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDES 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622854038 717 YAKCQNALQQVVARQGRPVVICDKEDTETIKntkrtikvphsvDCLQGILSVIPLQLLAFHLAVLRGYDVD 787
Cdd:PRK11382 271 RHTTERAINFVKQRTDNVIVIDYAEISQGLH------------PWLAPFLMFVPMEWLCYYLSIYKDHNPD 329
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
519-610 |
1.87e-09 |
|
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: 59.07 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 519 ASDFLDRNTPvfRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 596
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90
....*....|....*.
gi 1622854038 597 TSQFVSLVMF--ALMM 610
Cdd:cd05007 186 TAQKLALNMLstAVMI 201
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
487-565 |
4.25e-09 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 53.92 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 487 LILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFLSQSGETADTLMGLRYCKERGALTVGI 564
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1622854038 565 T 565
Cdd:cd04795 81 T 81
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
120-306 |
1.04e-08 |
|
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: 56.41 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 120 SGIFAYLNYHVPRTRREILETLikgLQRLEYRGYDSAGvgfdggndkdweanackiqlikkkgkvkaldeevhkqqdmdl 199
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERM---LDALAHRGPDGSG------------------------------------------ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 200 dIEFDVHFGIAHTRWATHGepnPVNSH-PQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkYM- 277
Cdd:cd00712 36 -IWIDEGVALGHRRLSIID---LSGGAqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL--YEe 108
|
170 180
....*....|....*....|....*....
gi 1622854038 278 YDnqesqdtsfttlvERVIQQLEGAFALV 306
Cdd:cd00712 109 WG-------------EDCLERLNGMFAFA 124
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
519-609 |
2.91e-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: 55.87 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 519 ASDFLDRN-TPvfrDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIgVA-ST--K 594
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 1622854038 595 AYTSQFVSLVMF--ALM 609
Cdd:COG2103 198 AGTAQKLVLNMLstAAM 214
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
485-611 |
2.96e-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: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 485 RRLILIACGTSYHAG---VATRQVleelTELPvmvelaSDFLDrntP----------VFRDDVCFFLSQSGETADTLMGL 551
Cdd:cd05014 1 GKVVVTGVGKSGHIArkiAATLSS----TGTP------AFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622854038 552 RYCKERGALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFVSLVMF-ALMMC 611
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 ... |
478-605 |
4.12e-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: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 478 IKEIQRCRRLILIACGTSYHAG--VATRqvleeLTELPVMVELASD---FLDRNTPVFRDDVCFFLSQSGETADTLMGLR 552
Cdd:cd05013 7 VDLLAKARRIYIFGVGSSGLVAeyLAYK-----LLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622854038 553 YCKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM 605
Cdd:cd05013 82 IAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
478-611 |
9.21e-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: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 478 IKEIQRCRRLILIACGTSYHAGVATRQVLEEL----TELPVMVELASDFLDRNTPvfrDDVCFFLSQSGETADTLMGLRY 553
Cdd:COG1737 128 VDLLAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARL 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622854038 554 CKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVMF-ALMMC 611
Cdd:COG1737 205 AKERGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALIdALAAA 261
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
120-273 |
1.60e-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: 51.38 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 120 SGIFAYLNYHVPRTRreilETLIKGLQRLEYRGYDSAGVGFDGgndkdweanackiqlikkkgkvkaldeevhkqqdmdl 199
Cdd:COG0367 2 CGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------- 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622854038 200 diefdvHFGIAHTRWATHGEPNpvNSHpQ-RSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKL 273
Cdd:COG0367 41 ------GVALGHRRLSIIDLSE--GGH-QpMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
209-274 |
7.03e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 48.42 E-value: 7.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622854038 209 IAHTRWATHGEPNPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-----ESETDTETIAKLV 274
Cdd:COG0121 80 IAHVRKATVGPVSLENTHPFRGG---RWLFAHNGQLDGFDRLRRRLAEELPDElyfqpVGTTDSELAFALL 147
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
238-307 |
8.07e-06 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 49.25 E-value: 8.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 238 VIHNGIITNYKDLKKFLESKGYDFESETDTETIakLVKYMYDNqesqdtsfttlvERVIQQLEGAFALVF 307
Cdd:TIGR01536 70 IVFNGEIYNHEELREELEAKGYTFQTDSDTEVI--LHLYEEWG------------EECVDRLDGMFAFAL 125
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
531-611 |
8.23e-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: 48.43 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 531 RDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDcgVHINAGPE-----IGVASTkayTSQFVSLVM 605
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
....*..
gi 1622854038 606 F-ALMMC 611
Cdd:COG0794 166 GdALAVA 172
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
209-300 |
9.59e-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: 44.69 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 209 IAHTRWATHGEPNPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-ESETDTETIAKLV-KYMYDNQESQDT 286
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFALLlSRLLERDPLDPA 160
|
90
....*....|....
gi 1622854038 287 SFTTLVERVIQQLE 300
Cdd:cd01908 161 ELLDAILQTLRELA 174
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
231-306 |
9.67e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 45.86 E-value: 9.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622854038 231 DKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYmYDNQEsqdtsfttlverVIQQLEGAFALV 306
Cdd:PTZ00077 70 DDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKE-YGPKD------------FWNHLDGMFATV 132
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
532-606 |
1.66e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 44.30 E-value: 1.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622854038 532 DDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF 606
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
237-391 |
5.46e-04 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 43.36 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 237 IVIHNGIITNYKDLKKFLESKgYDFESETDTETIAKLvkYmydnqESQDTSFttlvervIQQLEGAFALVFksvhfpgqa 316
Cdd:PRK09431 71 VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL--Y-----QEKGPDF-------LDDLDGMFAFAL--------- 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622854038 317 VGTRRGSpLLIAvRsehklstDHIPI--LYrTGKDKKGscnlsrvdsttclfpveekavEYYFASDASAVIEHTNRV 391
Cdd:PRK09431 127 YDSEKDA-YLIA-R-------DPIGIipLY-YGYDEHG---------------------NLYFASEMKALVPVCKTI 172
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
658-740 |
8.75e-04 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 38.89 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 658 VLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGP-LALVDKLMPVIMIIMRdHTYAKCQNALQQVVARQGRPVV 736
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYS-GRTEELLAALEIAKELGIPVIA 79
|
....
gi 1622854038 737 ICDK 740
Cdd:cd04795 80 ITDA 83
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
209-330 |
1.36e-03 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 41.55 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854038 209 IAHTRWATHGEPNPVNSHP-QRSDKNNEFIVIHNGiitnykDLKKFLESKGYDFE--SETDTETI-----AKLVKYMYDN 280
Cdd:pfam13230 75 IAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNG------DLKGYAPKLSGRFQpvGSTDSELAfcwllDRLASRFPYA 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622854038 281 QESQDTSFTTLVE--RVIQQLeGAFALVFKSvhfpGQAVGTRRGSPLLIAVR 330
Cdd:pfam13230 149 RPSAGELFRALRElaREIAAH-GTFNFLLSD----GRDLFAHCSTRLHYILR 195
|
|
| |
