|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-699 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 930.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGLDggNDKDWEANACKIqlIKKKGKVKALDEEVHK---QQ 77
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLV--FREEGKIESLVRSVYEevaET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 78 DMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVK 157
Cdd:PLN02981 77 DLNLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 158 YMYD--NWESQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSE-HKLSTDHipilyrtARTQIG 234
Cdd:PLN02981 157 FVFDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELpEEKNSSA-------VFTSEG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 235 SKFTWwgsqaergkdkkgscglsrvdsttclfpvEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKR 314
Cdd:PLN02981 230 FLTKN-----------------------------RDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFEN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 315 TARDHPG---------RAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDD----YTVNLGGLKDHIKEI 381
Cdd:PLN02981 281 EKGRGGGglsrpasveRALSTLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGsgkaKRVLLGGLKDHLKTI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 382 QRCRRLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALT 461
Cdd:PLN02981 361 RRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALC 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 462 VGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSM 541
Cdd:PLN02981 441 VGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKL 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 542 DDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQ 621
Cdd:PLN02981 521 DQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQ 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 622 NALQQVVARQGRPVVICDKEDTETIKNTK--RTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:PLN02981 601 SVIQQLRARKGRLIVICSKGDASSVCPSGgcRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-699 |
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: 792.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVG-LDGGndkdweanacKIQLIKKKGKVKALDEEVHKQqdm 79
Cdd:COG0449 1 MCGIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAvLDDG----------GLEVRKAVGKLANLEEKLAEE--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 80 dldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 159
Cdd:COG0449 62 ----PLSGTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 160 YDnwesQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtartqigskftw 239
Cdd:COG0449 137 LK----GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL---------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 240 wgsqaerGKDkkgscglsrvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDh 319
Cdd:COG0449 185 -------GEG------------------------ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 320 pgRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNfDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAG 399
Cdd:COG0449 233 --REVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 400 MATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCG 479
Cdd:COG0449 310 LVGKYLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAV 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 480 VHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSV 558
Cdd:COG0449 390 LYTHAGPEIGVASTKAFTTQLAALYLLALYLARARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNA 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 559 LIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVIC 638
Cdd:COG0449 470 LFLGRGINYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIA 549
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564347653 639 DKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:COG0449 550 DEGDEEVEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-699 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 735.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAGVG-LDGGNdkdweanackIQLIKKKGKVKALDEEVHKQqdm 79
Cdd:PRK00331 1 MCGIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAvLDDGG----------LEVRKAVGKVANLEAKLEEE--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 80 dldiEFDVHLGIAHTRWATHGEPSPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 159
Cdd:PRK00331 62 ----PLPGTTGIGHTRWATHGKPTERNAHPHT-DCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 160 YDnwesQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtartqigskftw 239
Cdd:PRK00331 137 LK----EGGDLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL---------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 240 wgsqaerGKDkkgscglsrvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDh 319
Cdd:PRK00331 185 -------GEG------------------------ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVE- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 320 pgRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDdytvnlGGLKDHIKEIQRCRRLILIACGTSYHAG 399
Cdd:PRK00331 233 --REVYTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDEL------GEGELADEDLKKIDRIYIVACGTSYHAG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 400 MATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCG 479
Cdd:PRK00331 305 LVAKYLIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAV 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 480 VHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSV 558
Cdd:PRK00331 385 LYTHAGPEIGVASTKAFTAQLAVLYLLALALAKARGTLsAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNA 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 559 LIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVIC 638
Cdd:PRK00331 465 LFLGRGVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIA 544
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564347653 639 DKEDtETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:PRK00331 545 DEGD-EVAEEADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-699 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 722.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGLDGGNDKDWEANACKIQ------LIKKKGKVKALDEEVH 74
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAASAptprpcVVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 75 KQQD----MDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTE 150
Cdd:PTZ00394 81 SEAVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 151 TIAKLVKYMYdnweSQD--VSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRsehklstdhipilyrt 228
Cdd:PTZ00394 160 VISVLSEYLY----TRKgiHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR---------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 229 artqigskftwwgsqaeRGKDKKGSCGLSRVDsttclFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLS 308
Cdd:PTZ00394 220 -----------------RTDDRGCVMKLQTYD-----LTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 309 IHRIKRTARDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDH-IKEIQRCRRL 387
Cdd:PTZ00394 278 FYNAAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRI 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 388 ILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNT 467
Cdd:PTZ00394 358 LFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 468 VGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSM-DDEIQ 546
Cdd:PTZ00394 438 VGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 547 KLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQ 626
Cdd:PTZ00394 518 ALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQ 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564347653 627 VVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:PTZ00394 598 VKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-699 |
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: 636.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 2 CGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGLdggndkdweANACKIQLIKKKGKVKALDEEVhkqQDMDL 81
Cdd:TIGR01135 1 CGIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAV---------VDEGKLFVRKAVGKVAELANKL---GEKPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 82 DIEFdvhlGIAHTRWATHGEPSPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:TIGR01135 63 PGGV----GIGHTRWATHGKPTDENAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 162 NwesqDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGvrsehklstdhipilyrtartqIGSKftwwg 241
Cdd:TIGR01135 138 E----GGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVG----------------------LGDG----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 242 sqaergkdkkgscglsrvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHrikrtarDHPG 321
Cdd:TIGR01135 187 --------------------------------ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIY-------NFEG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 322 ----RAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIqrcRRLILIACGTSYH 397
Cdd:TIGR01135 228 apvqREVRVIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNI---DRIQIVACGTSYH 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 398 AGMATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETD 477
Cdd:TIGR01135 305 AGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREAD 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 478 CGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQK 556
Cdd:TIGR01135 385 HTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKR 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 557 SVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVV 636
Cdd:TIGR01135 465 NFLFLGRGLGYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIV 544
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564347653 637 ICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:TIGR01135 545 FAPEDDETIASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-698 |
6.57e-154 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 460.26 E-value: 6.57e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVG-LDGGND------KDWEANACKIQLIKKKGKvkaldeEV 73
Cdd:PTZ00295 24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGElkttkyASDGTTSDSIEILKEKLL------DS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 74 HKQQdmdldiefdvHLGIAHTRWATHGEPSPVNSHPQrSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIA 153
Cdd:PTZ00295 92 HKNS----------TIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 154 KLVKYMYDNWESqdvsFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklSTDHIpilyrtartqi 233
Cdd:PTZ00295 161 NLIGLELDQGED----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGI------GDDSI----------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 234 gskftwwgsqaergkdkkgscglsrvdsttclfpveekaveyYFASDASAVIEHTNRVIFLEDDDVAAV-VDGRLSIHRI 312
Cdd:PTZ00295 220 ------------------------------------------YVASEPSAFAKYTNEYISLKDGEIAELsLENVNDLYTQ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 313 KRtardhpgraVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTM--RGRVNFDDYTVNLGGLKDHIKEIQRCRRLILI 390
Cdd:PTZ00295 258 RR---------VEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILV 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 391 ACGTSYHAGMATRQVLEELTEL-PVMVELASDF-LDRNTpvfRDDVCF-FISQSGETADTLMGLRYCKERGALTVGITNT 467
Cdd:PTZ00295 329 GCGTSYYAALFAASIMQKLKCFnTVQVIDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNT 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 468 VGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDR-ISMQE-RRKEIMLGLKRLPDLIKEVL-SMDDE 544
Cdd:PTZ00295 406 VGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNyKCSSLINSLHRLPTYIGMTLkSCEEQ 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 545 IQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKL--MPVIMIIMRDHTYAKCQN 622
Cdd:PTZ00295 486 CKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMIN 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564347653 623 ALQQVVARQGRPVVICDKEDtETIKNTKRTIKVPhSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTV 698
Cdd:PTZ00295 566 AAEQVKARGAYIIVITDDED-LVKDFADEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-302 |
4.20e-108 |
|
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: 326.71 E-value: 4.20e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 2 CGIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGLDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdl 81
Cdd:cd00714 1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---------SLEVVKAVGKVANLEEKLAEK----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 82 diEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNnEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00714 61 --PLSGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 162 nwesQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtartqigskftwwg 241
Cdd:cd00714 138 ----GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG--------------------------- 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564347653 242 sqaergkdkkgscglsrvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAV 302
Cdd:cd00714 187 --------------------------------ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
345-699 |
8.02e-70 |
|
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: 231.33 E-value: 8.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 345 KEIFEQPESVVNTmrgrvnFDDYTVNLGGLKDHIKEIQRcRRLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLD 424
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 425 RNTPVFRD-DVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSL 503
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 504 VM-FALMMCDDrismqerrkEIMLGLKRLPDLIKEVLSMDDEIQKLAtELYHQKSVLIMGRGYHYATCLEGALKIKEITY 582
Cdd:COG2222 155 LAlLAAWGGDD---------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 583 MHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTEtikntkrtIKVPHSVDC- 661
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAA--------ITLPAIPDLh 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 564347653 662 --LQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:COG2222 297 daLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
543-697 |
1.19e-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: 221.37 E-value: 1.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 543 DEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQN 622
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564347653 623 ALQQVVARQGRPVVICDKEDTETIKNTkrTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVT 697
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 ... |
386-511 |
2.25e-63 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 206.58 E-value: 2.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 386 RLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGIT 465
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 564347653 466 NTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMC 511
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-217 |
6.95e-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: 171.09 E-value: 6.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 2 CGIFAYLNYHVPRTRReiLETLIKGLQRLEYRGYDSAGVGLDGGndkdweanackiqlikKKGKVKALDEEVHKQQDMDL 81
Cdd:cd00352 1 CGIFGIVGADGAASLL--LLLLLRGLAALEHRGPDGAGIAVYDG----------------DGLFVEKRAGPVSDVALDLL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 82 DIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00352 63 DEPLKSGVALGHVRLATNGLPSEANAQPFRSE-DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564347653 162 NWEsqdvsFTTLVERVIQQLEGAFALVFKSVHfPGQAVGTRRG---SPLLIGVRSEHKL 217
Cdd:cd00352 142 EGG-----LFEAVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGITKDGGL 194
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
380-509 |
3.44e-41 |
|
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: 146.29 E-value: 3.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 380 EIQRCRRLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSGETADTLMGLRYCKERG 458
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564347653 459 ALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALM 509
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
551-682 |
6.07e-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: 123.18 E-value: 6.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 551 ELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQnALQQVVAR 630
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564347653 631 QGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLR 682
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-212 |
4.52e-20 |
|
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: 90.21 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 2 CGIFA-YLNYHVPRTrreiletLIKGLQRLEYRGYDSAG-VGLDGGndkdweanacKIQLIKKKGKVkaldEEVHKQQDM 79
Cdd:cd00715 1 CGVFGiYGAEDAARL-------TYLGLYALQHRGQESAGiATSDGK----------RFHTHKGMGLV----SDVFDEEKL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKY 158
Cdd:cd00715 60 R---RLPGNIAIGHVRYSTAGSSSLENAQPFVVNSPLGGIALaHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIAR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564347653 159 mydnwESQDVSFTTLVERVIQQLEGAFALVFksvhfpgqavGTRRGsplLIGVR 212
Cdd:cd00715 137 -----SLAKDDLFEAIIDALERVKGAYSLVI----------MTADG---LIAVR 172
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-189 |
1.02e-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: 92.78 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAG-VGLDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDM 79
Cdd:COG0034 7 ECGVFGIYG------HEDVAQLTYYGLYALQHRGQESAGiATSDGG----------RFHLHKGMGLVS----DVFDEEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHP-QRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKY 158
Cdd:COG0034 67 E---RLKGNIAIGHVRYSTTGSSSLENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAR 143
|
170 180 190
....*....|....*....|....*....|.
gi 564347653 159 mydnwESQDVSFTTLVERVIQQLEGAFALVF 189
Cdd:COG0034 144 -----ELTKEDLEEAIKEALRRVKGAYSLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-212 |
9.48e-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: 86.22 E-value: 9.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 2 CGIFAYlNYHVPRTRREIletlIKGLQRLEYRGYDSAGVGLDGGNdkdweanacKIQLIKKKGKVKaldeEVHKQQDMDl 81
Cdd:TIGR01134 1 CGVVGI-YGQEEVAASLT----YYGLYALQHRGQESAGISVFDGN---------RFRLHKGNGLVS----DVFNEEHLQ- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 82 diEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMY 160
Cdd:TIGR01134 62 --RLKGNVGIGHVRYSTAGSSGLENAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHND 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564347653 161 dnwESQDVSFTTlVERVIQQLEGAFALVFKSVHF------PgqaVGTRrgsPLLIGVR 212
Cdd:TIGR01134 140 ---ESKDDLFDA-VARVLERVRGAYALVLMTEDGlvavrdP---HGIR---PLVLGRR 187
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-213 |
1.86e-16 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 82.80 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYlnYHVPRTRREILEtlikGLQRLEYRGYDSAG-VGLDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDM 79
Cdd:PLN02440 1 ECGVVGI--FGDPEASRLCYL----GLHALQHRGQEGAGiVTVDGN----------RLQSITGNGLVS----DVFDESKL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHPqrsdknneFI---------VIHNGIITNYKDLKKFLESKGYDFESETDTE 150
Cdd:PLN02440 61 D---QLPGDIAIGHVRYSTAGASSLKNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTE 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564347653 151 TIAKLVKymydnwESQDVSFTTLVERVIQQLEGAFALVFKsvhFPGQAVGTR-----RgsPLLIGVRS 213
Cdd:PLN02440 130 VLLHLIA------ISKARPFFSRIVDACEKLKGAYSMVFL---TEDKLVAVRdphgfR--PLVMGRRS 186
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
386-477 |
5.56e-15 |
|
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: 71.84 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 386 RLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFISQSGETADTLMGLRYCKERGALTVGI 464
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 564347653 465 TNTVGSSISRETD 477
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-188 |
2.38e-14 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 75.84 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 2 CGIF-AYLNyhvprTRREILETLIKGLQRLEYRGYDSAGVGLdggndkdweANACKIQLIKKKGKVkaldEEVHKQQDMD 80
Cdd:PRK05793 15 CGVFgVFSK-----NNIDVASLTYYGLYALQHRGQESAGIAV---------SDGEKIKVHKGMGLV----SEVFSKEKLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 81 ldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKym 159
Cdd:PRK05793 77 ---GLKGNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIaHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIA-- 151
|
170 180
....*....|....*....|....*....
gi 564347653 160 ydnwESQDVSFTTLVERVIQQLEGAFALV 188
Cdd:PRK05793 152 ----RSAKKGLEKALVDAIQAIKGSYALV 176
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
90-189 |
4.46e-14 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 69.26 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 90 GIAHTRWATHGEPS----PVNShpqrSDKNneFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkymYDNWEs 165
Cdd:pfam13522 13 ALGHVRLAIVDLPDagnqPMLS----RDGR--LVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL----YEEWG- 81
|
90 100
....*....|....*....|....
gi 564347653 166 qdvsfttlvERVIQQLEGAFALVF 189
Cdd:pfam13522 82 ---------EDCLERLRGMFAFAI 96
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-160 |
5.41e-14 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 72.30 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 2 CGIFAYLNyhvpRTRREIL-ETLIKGLQRLEYRG-YDSAGVGLDGGND-------KDweanackIQLIKKKGkvkaLDEE 72
Cdd:cd01907 1 CGIFGIMS----KDGEPFVgALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgKD-------MEVFKGVG----YPED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 73 VHKQQDMDldiEFDVHLGIAHTRWATHgepSPVN---SHPqrsdknneF-----IVIHNGIITNYKDLKKFLESKGYDFE 144
Cdd:cd01907 66 IARRYDLE---EYKGYHWIAHTRQPTN---SAVWwygAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFE 131
|
170
....*....|....*.
gi 564347653 145 SETDTETIAKLVKYMY 160
Cdd:cd01907 132 TETDTEVIAYYLDLLL 147
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
109-188 |
3.33e-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: 63.69 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 109 PQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYdnwesqdvsfttlVERVIQQLEGAFALV 188
Cdd:pfam13537 15 PMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW-------------GEDCVDRLNGMFAFA 81
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
432-509 |
5.95e-11 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 64.03 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 432 DDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--A 507
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstG 211
|
..
gi 564347653 508 LM 509
Cdd:PRK05441 212 VM 213
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-188 |
1.04e-10 |
|
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: 62.19 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 2 CGIFAYLNYHVPRTRREILETLikgLQRLEYRGYDSAGvgldggndkdweanackiqlikkkgkvkaldeevhkqqdmdl 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERM---LDALAHRGPDGSG------------------------------------------ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 82 dIEFDVHLGIAHTRWATHGepsPVNSH-PQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkymY 160
Cdd:cd00712 36 -IWIDEGVALGHRRLSIID---LSGGAqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL----Y 106
|
170 180
....*....|....*....|....*...
gi 564347653 161 DNWEsqdvsfttlvERVIQQLEGAFALV 188
Cdd:cd00712 107 EEWG----------EDCLERLNGMFAFA 124
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-188 |
2.64e-10 |
|
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: 63.32 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLNYHVPRTRreilETLIKGLQRLEYRGYDSAGVGLDGgndkdweanackiqlikkkgkvkaldeevhkqqdmd 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 81 ldiefdvHLGIAHTRWATHGEPSpvNSHpQ-RSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkym 159
Cdd:COG0367 41 -------GVALGHRRLSIIDLSE--GGH-QpMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA---- 106
|
170 180
....*....|....*....|....*....
gi 564347653 160 YDNWEsqdvsfttlvERVIQQLEGAFALV 188
Cdd:COG0367 107 YEEWG----------EDCLERLNGMFAFA 125
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
419-510 |
2.87e-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: 61.38 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 419 ASDFLDRNTPvfRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 496
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90
....*....|....*.
gi 564347653 497 TSQFVSLVMF--ALMM 510
Cdd:cd05007 186 TAQKLALNMLstAVMI 201
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
386-690 |
3.49e-10 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 62.33 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 386 RLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFI--SQSGETADTLMGLRYCKERGALTVG 463
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 464 ITNTVGSSISRETDCGVHINAGPEIGVASTKAYTsqfVSLVMFAlmmcddRISMQERRKEIMLGLKRLPDLIKEVLSMDD 543
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMIT------RLAPNAEIGKIKNDLKQLPNALGHLVRTWE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 544 EIQKLATELYHQKSVL-------IMGRGYHyatclEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHT 616
Cdd:PRK11382 196 EKGRQLGELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDES 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564347653 617 YAKCQNALQQVVARQGRPVVICDKEDTETIKntkrtikvphsvDCLQGILSVIPLQLLAFHLAVLRGYDVDFPR 690
Cdd:PRK11382 271 RHTTERAINFVKQRTDNVIVIDYAEISQGLH------------PWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
378-505 |
7.57e-10 |
|
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: 57.62 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 378 IKEIQRCRRLILIACGTSYHAG--MATRqvleeLTELPVMVELASD---FLDRNTPVFRDDVCFFISQSGETADTLMGLR 452
Cdd:cd05013 7 VDLLAKARRIYIFGVGSSGLVAeyLAYK-----LLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564347653 453 YCKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM 505
Cdd:cd05013 82 IAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
387-465 |
7.67e-10 |
|
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: 55.84 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 387 LILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFISQSGETADTLMGLRYCKERGALTVGI 464
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 564347653 465 T 465
Cdd:cd04795 81 T 81
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
419-509 |
2.59e-09 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 58.95 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 419 ASDFLDRN-TPvfrDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIgVA-ST--K 494
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 564347653 495 AYTSQFVSLVMF--ALM 509
Cdd:COG2103 198 AGTAQKLVLNMLstAAM 214
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
378-511 |
2.14e-08 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 56.09 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 378 IKEIQRCRRLILIACGTSYHAGMATRQVLEEL----TELPVMVELASDFLDRNTPvfrDDVCFFISQSGETADTLMGLRY 453
Cdd:COG1737 128 VDLLAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARL 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 564347653 454 CKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVMF-ALMMC 511
Cdd:COG1737 205 AKERGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALIdALAAA 261
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
431-511 |
5.38e-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: 51.77 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 431 RDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFVSLVMF 506
Cdd:cd05014 47 PGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALG 122
|
....*.
gi 564347653 507 -ALMMC 511
Cdd:cd05014 123 dALAVA 128
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
120-189 |
4.76e-07 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 52.72 E-value: 4.76e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 120 VIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkymYDNWEsqdvsfttlvERVIQQLEGAFALVF 189
Cdd:TIGR01536 70 IVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHL----YEEWG----------EECVDRLDGMFAFAL 125
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
88-182 |
1.04e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 50.35 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 88 HLGIAHTRWATHGEPSPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-----ESETDTETIAKLvkyMYDN 162
Cdd:COG0121 77 RLVIAHVRKATVGPVSLENTHPFRGG---RWLFAHNGQLDGFDRLRRRLAEELPDElyfqpVGTTDSELAFAL---LLSR 150
|
90 100
....*....|....*....|
gi 564347653 163 WESQDVSFTTLVERVIQQLE 182
Cdd:COG0121 151 LRDGGPDPAEALAEALRELA 170
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
431-521 |
2.45e-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: 49.97 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 431 RDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDcgVHINAGPE-----IGVASTkayTSQFVSLVM 505
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
90
....*....|....*..
gi 564347653 506 F-ALMMCddrisMQERR 521
Cdd:COG0794 166 GdALAVA-----LLEAR 177
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-188 |
1.10e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 48.56 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLNYhvpRTRREILETLIKGL-QRLEYRGYDSAGVgldggndkdweanackiqlikkkgkvkaldeevhkqqdM 79
Cdd:PTZ00077 1 MCGILAIFNS---KGERHELRRKALELsKRLRHRGPDWSGI--------------------------------------I 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 80 DLDIEFDVHLGIAHTRWATHGepsPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkym 159
Cdd:PTZ00077 40 VLENSPGTYNILAHERLAIVD---LSDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL---- 112
|
170 180
....*....|....*....|....*....
gi 564347653 160 YDNWESQDvsfttlverVIQQLEGAFALV 188
Cdd:PTZ00077 113 YKEYGPKD---------FWNHLDGMFATV 132
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
432-506 |
3.22e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 46.22 E-value: 3.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564347653 432 DDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF 506
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
88-155 |
3.27e-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: 3.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564347653 88 HLGIAHTRWATHGEPSPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-ESETDTETIAKL 155
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFAL 146
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-152 |
8.60e-05 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 45.67 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 1 MCGIFAYLNYH--VPRTRREILEtlikGLQRLEYRGYDSAGVGLDGGndkdweanackiqlikkkgkvkaldeevhkqqd 78
Cdd:PRK09431 1 MCGIFGILDIKtdADELRKKALE----MSRLMRHRGPDWSGIYASDN--------------------------------- 43
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564347653 79 mdldiefdvhlGI-AHTRWA----THGEPSPVNShpqrsDKNNefIVIHNGIITNYKDLKKFLESKgYDFESETDTETI 152
Cdd:PRK09431 44 -----------AIlGHERLSivdvNGGAQPLYNE-----DGTH--VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVI 103
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
558-640 |
5.40e-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: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347653 558 VLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGP-LALVDKLMPVIMIIMRdHTYAKCQNALQQVVARQGRPVV 636
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYS-GRTEELLAALEIAKELGIPVIA 79
|
....
gi 564347653 637 ICDK 640
Cdd:cd04795 80 ITDA 83
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
432-477 |
6.38e-03 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 39.36 E-value: 6.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 564347653 432 DDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETD 477
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLAD 233
|
|
| |
