|
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: 929.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDggNDKDWEANACKIqlIKKKGKVKALDEEVHK---QQ 77
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID--NDPSLESSSPLV--FREEGKIESLVRSVYEevaET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 78 DMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVK 157
Cdd:PLN02981 77 DLNLDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 158 YMYD--NRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSE-HKLSTdhipilyrtartqiG 234
Cdd:PLN02981 157 FVFDklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELpEEKNS--------------S 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 235 SKFTrwgSQGERGKDKKgscnlsrvdsttclfpveeKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKR 314
Cdd:PLN02981 223 AVFT---SEGFLTKNRD-------------------KPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFEN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 315 TAGDHPG---------RAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDD----YTVNLGGLKDHIKEI 381
Cdd:PLN02981 281 EKGRGGGglsrpasveRALSTLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGsgkaKRVLLGGLKDHLKTI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 382 QRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALT 461
Cdd:PLN02981 361 RRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALC 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 462 VGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSM 541
Cdd:PLN02981 441 VGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKL 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 542 DDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQ 621
Cdd:PLN02981 521 DQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQ 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 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: 784.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmd 80
Cdd:COG0449 1 MCGIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAVLDDG---------GLEVRKAVGKLANLEEKLAEE---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 81 ldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMY 160
Cdd:COG0449 62 ---PLSGTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 161 DnresQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtartqigskftrw 240
Cdd:COG0449 138 K----GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL----------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 241 gsqgerGKDkkgscnlsrvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDhp 320
Cdd:COG0449 185 ------GEG------------------------ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE-- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 321 gRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNfDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGV 400
Cdd:COG0449 233 -REVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 401 ATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGV 480
Cdd:COG0449 311 VGKYLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVL 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 481 HINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVL 559
Cdd:COG0449 391 YTHAGPEIGVASTKAFTTQLAALYLLALYLARARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNAL 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 560 IMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICD 639
Cdd:COG0449 471 FLGRGINYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIAD 550
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 640 KEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:COG0449 551 EGDEEVEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 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: 731.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAGVG-FDGGNdkdweanackIQLIKKKGKVKALDEEVHKQqdm 79
Cdd:PRK00331 1 MCGIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAvLDDGG----------LEVRKAVGKVANLEAKLEEE--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 80 dldiEFDVHLGIAHTRWATHGEPSPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYM 159
Cdd:PRK00331 62 ----PLPGTTGIGHTRWATHGKPTERNAHPHT-DCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 160 YDnresQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklstdhipilyrtartqigskftr 239
Cdd:PRK00331 137 LK----EGGDLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL---------------------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 240 wgsqgerGKDkkgscnlsrvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVvdGRLSIHrIKRTAGDH 319
Cdd:PRK00331 185 -------GEG------------------------ENFLASDALALLPYTRRVIYLEDGEIAVL--TRDGVE-IFDFDGNP 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 320 PGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDdytvnlGGLKDHIKEIQRCRRLILIACGTSYHAG 399
Cdd:PRK00331 231 VEREVYTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDEL------GEGELADEDLKKIDRIYIVACGTSYHAG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 400 VATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCG 479
Cdd:PRK00331 305 LVAKYLIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAV 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 480 VHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISM-QERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSV 558
Cdd:PRK00331 385 LYTHAGPEIGVASTKAFTAQLAVLYLLALALAKARGTLsAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNA 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 559 LIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVIC 638
Cdd:PRK00331 465 LFLGRGVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIA 544
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30923274 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: 720.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQ------LIKKKGKVKALDEEVH 74
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTAASAptprpcVVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 75 KQQD----MDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTE 150
Cdd:PTZ00394 81 SEAVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 151 TIAKLVKYMYDNRESQdtSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRsehklstdhipilyrtar 230
Cdd:PTZ00394 160 VISVLSEYLYTRKGIH--NFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 231 tqigskftrwgsqgeRGKDKKGSCNLSRVDsttclFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIH 310
Cdd:PTZ00394 220 ---------------RTDDRGCVMKLQTYD-----LTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFY 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 311 RIKRTAGDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDH-IKEIQRCRRLIL 389
Cdd:PTZ00394 280 NAAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 390 IACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVG 469
Cdd:PTZ00394 360 IACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 470 SSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSM-DDEIQKL 548
Cdd:PTZ00394 440 SSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKAL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 549 ATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVV 628
Cdd:PTZ00394 520 AARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVK 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30923274 629 ARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:PTZ00394 600 ARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 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: 631.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 2 CGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVGFdggndkdweANACKIQLIKKKGKVKALDEEVhkqQDMDL 81
Cdd:TIGR01135 1 CGIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAV---------VDEGKLFVRKAVGKVAELANKL---GEKPL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 82 DIEFdvhlGIAHTRWATHGEPSPVNSHPQRsDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:TIGR01135 63 PGGV----GIGHTRWATHGKPTDENAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 162 NresqDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGvrsehklstdhipilyrtartqIGSKftrwg 241
Cdd:TIGR01135 138 E----GGDLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVG----------------------LGDG----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 242 sqgergkdkkgscnlsrvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKrtaGDHPG 321
Cdd:TIGR01135 187 --------------------------------ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFE---GAPVQ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 322 RAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIqrcRRLILIACGTSYHAGVA 401
Cdd:TIGR01135 232 REVRVIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNI---DRIQIVACGTSYHAGLV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 402 TRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVH 481
Cdd:TIGR01135 309 AKYLIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLY 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 482 INAGPEIGVASTKAYTSQFVSLVMFALMMCDDR-ISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLI 560
Cdd:TIGR01135 389 TRAGPEIGVASTKAFTTQLTVLYLLALALAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLF 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 561 MGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDK 640
Cdd:TIGR01135 469 LGRGLGYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPE 548
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 30923274 641 EDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE 699
Cdd:TIGR01135 549 DDETIASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-698 |
5.61e-153 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 457.95 E-value: 5.61e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLnyhvprTRREILETLIKGLQRLEYRGYDSAGVG-FDGGND------KDWEANACKIQLIKKKGKvkaldeEV 73
Cdd:PTZ00295 24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGElkttkyASDGTTSDSIEILKEKLL------DS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 74 HKQQdmdldiefdvHLGIAHTRWATHGEPSPVNSHPQrSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIA 153
Cdd:PTZ00295 92 HKNS----------TIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 154 KLVKYMYDNRESqdtsFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVrsehklSTDHIpilyrtartqi 233
Cdd:PTZ00295 161 NLIGLELDQGED----FQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGI------GDDSI----------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 234 gskftrwgsqgergkdkkgscnlsrvdsttclfpveekaveyYFASDASAVIEHTNRVIFLEDDDVAAV-VDGRLSIHRI 312
Cdd:PTZ00295 220 ------------------------------------------YVASEPSAFAKYTNEYISLKDGEIAELsLENVNDLYTQ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 313 KRtagdhpgraVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTM--RGRVNFDDYTVNLGGLKDHIKEIQRCRRLILI 390
Cdd:PTZ00295 258 RR---------VEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILV 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 391 ACGTSYHAGVATRQVLEELTEL-PVMVELASDF-LDRNTpvfRDDVCF-FLSQSGETADTLMGLRYCKERGALTVGITNT 467
Cdd:PTZ00295 329 GCGTSYYAALFAASIMQKLKCFnTVQVIDASELtLYRLP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNT 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 468 VGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDR-ISMQE-RRKEIMLGLKRLPDLIKEVL-SMDDE 544
Cdd:PTZ00295 406 VGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNyKCSSLINSLHRLPTYIGMTLkSCEEQ 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 545 IQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKL--MPVIMIIMRDHTYAKCQN 622
Cdd:PTZ00295 486 CKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMIN 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30923274 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 |
3.98e-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: 3.98e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 2 CGIFAYLNYhvprtrREILETLIKGLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKALDEEVHKQqdmdl 81
Cdd:cd00714 1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVIGDG---------SLEVVKAVGKVANLEEKLAEK----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 82 diEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNnEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00714 61 --PLSGHVGIGHTRWATHGEPTDVNAHPHRSCDG-EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 162 nresQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEhklstdhipilyrtartqigskftrwg 241
Cdd:cd00714 138 ----GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG--------------------------- 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30923274 242 sqgergkdkkgscnlsrvdsttclfpveekavEYYFASDASAVIEHTNRVIFLEDDDVAAV 302
Cdd:cd00714 187 --------------------------------ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
345-699 |
7.81e-69 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 228.63 E-value: 7.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 345 KEIFEQPESVVNTmrgrvnFDDYTVNLGGLKDHIKEIQRcRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLD 424
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 425 RNTPVFRD-DVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSL 503
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 504 VM-FALMMCDDrismqerrkEIMLGLKRLPDLIKEVLSMDDEIQKLAtELYHQKSVLIMGRGYHYATCLEGALKIKEITY 582
Cdd:COG2222 155 LAlLAAWGGDD---------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 583 MHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTEtikntkrtIKVPHSVDC- 661
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAA--------ITLPAIPDLh 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 30923274 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 |
1.13e-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: 1.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 543 DEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQN 622
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30923274 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 |
1.21e-61 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 201.96 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 386 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGIT 465
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 30923274 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 |
1.80e-49 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 172.63 E-value: 1.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 2 CGIFAYLNYHVPRTRReiLETLIKGLQRLEYRGYDSAGVGFDGGndkdweanackiqlikKKGKVKALDEEVHKQQDMDL 81
Cdd:cd00352 1 CGIFGIVGADGAASLL--LLLLLRGLAALEHRGPDGAGIAVYDG----------------DGLFVEKRAGPVSDVALDLL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 82 DIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDkNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYD 161
Cdd:cd00352 63 DEPLKSGVALGHVRLATNGLPSEANAQPFRSE-DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30923274 162 NREsqdtsFTTLVERVIQQLEGAFALVFKSVHfPGQAVGTRRG---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 |
1.57e-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: 144.75 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 380 EIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFLSQSGETADTLMGLRYCKERG 458
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30923274 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 |
6.13e-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: 6.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 551 ELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQnALQQVVAR 630
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 30923274 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 |
1.50e-21 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 94.45 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 2 CGIFA-YLNYHVPRTrreiletLIKGLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVkaldEEVHKQQDM 79
Cdd:cd00715 1 CGVFGiYGAEDAARL-------TYLGLYALQHRGQESAGiATSDGK----------RFHTHKGMGLV----SDVFDEEKL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKy 158
Cdd:cd00715 60 R---RLPGNIAIGHVRYSTAGSSSLENAQPFVVNSPLGGIALaHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30923274 159 mydnRESQDTSFTTLVERVIQQLEGAFALVFksvhfpgqavGTRRGsplLIGVR 212
Cdd:cd00715 136 ----RSLAKDDLFEAIIDALERVKGAYSLVI----------MTADG---LIAVR 172
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-189 |
2.61e-21 |
|
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: 97.40 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLNyhvprtRREILETLIKGLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDM 79
Cdd:COG0034 7 ECGVFGIYG------HEDVAQLTYYGLYALQHRGQESAGiATSDGG----------RFHLHKGMGLVS----DVFDEEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHP-QRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKy 158
Cdd:COG0034 67 E---RLKGNIAIGHVRYSTTGSSSLENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA- 142
|
170 180 190
....*....|....*....|....*....|.
gi 30923274 159 mydnRESQDTSFTTLVERVIQQLEGAFALVF 189
Cdd:COG0034 143 ----RELTKEDLEEAIKEALRRVKGAYSLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-212 |
1.46e-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: 88.92 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 2 CGIFAYlNYHVPRTRREIletlIKGLQRLEYRGYDSAGVGFDGGNdkdweanacKIQLIKKKGKVKaldeEVHKQQDMDl 81
Cdd:TIGR01134 1 CGVVGI-YGQEEVAASLT----YYGLYALQHRGQESAGISVFDGN---------RFRLHKGNGLVS----DVFNEEHLQ- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 82 diEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYmy 160
Cdd:TIGR01134 62 --RLKGNVGIGHVRYSTAGSSGLENAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAH-- 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30923274 161 dNRESQDTSFTTlVERVIQQLEGAFALVFKSVHF------PgqaVGTRrgsPLLIGVR 212
Cdd:TIGR01134 138 -NDESKDDLFDA-VARVLERVRGAYALVLMTEDGlvavrdP---HGIR---PLVLGRR 187
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-284 |
2.84e-17 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 85.11 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYlnYHVPRTRREILEtlikGLQRLEYRGYDSAG-VGFDGGndkdweanacKIQLIKKKGKVKaldeEVHKQQDM 79
Cdd:PLN02440 1 ECGVVGI--FGDPEASRLCYL----GLHALQHRGQEGAGiVTVDGN----------RLQSITGNGLVS----DVFDESKL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 80 DldiEFDVHLGIAHTRWATHGEPSPVNSHPqrsdknneFI---------VIHNGIITNYKDLKKFLESKGYDFESETDTE 150
Cdd:PLN02440 61 D---QLPGDIAIGHVRYSTAGASSLKNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 151 TIAKLVKymydnrESQDTSFTTLVERVIQQLEGAFALVFKsvhFPGQAVGTR-----RgsPLLIGVRsehklSTDHIPIL 225
Cdd:PLN02440 130 VLLHLIA------ISKARPFFSRIVDACEKLKGAYSMVFL---TEDKLVAVRdphgfR--PLVMGRR-----SNGAVVFA 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30923274 226 YRT-ARTQIGSKFTRWGSQGE-----RGKDKKGSCNLSRVDSTTCLFpveekavEY-YFASDASAV 284
Cdd:PLN02440 194 SETcALDLIGATYEREVNPGEvivvdKDKGVSSQCLMPHPEPKPCIF-------EHiYFARPNSIV 252
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-291 |
5.63e-15 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 77.77 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 2 CGIF-AYLNyhvprTRREILETLIKGLQRLEYRGYDSAGVGFdggndkdweANACKIQLIKKKGKVkaldEEVHKQQDMD 80
Cdd:PRK05793 15 CGVFgVFSK-----NNIDVASLTYYGLYALQHRGQESAGIAV---------SDGEKIKVHKGMGLV----SEVFSKEKLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 81 ldiEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVI-HNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKym 159
Cdd:PRK05793 77 ---GLKGNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIaHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 160 ydnRESQdTSFTTLVERVIQQLEGAFALVfksVHFPGQAVGTR-----RgsPLLIGvrsehKLSTDHIPILYRTARTQIG 234
Cdd:PRK05793 152 ---RSAK-KGLEKALVDAIQAIKGSYALV---ILTEDKLIGVRdphgiR--PLCLG-----KLGDDYILSSESCALDTIG 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30923274 235 SKFTRWGSQGERGK-DKKGSCNLSRVDST---TCLFpveekavEY-YFASDASaVIE----HTNRV 291
Cdd:PRK05793 218 AEFIRDVEPGEIVIiDEDGIKSIKFAEKTkcqTCAF-------EYiYFARPDS-VIDgisvYESRV 275
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
386-477 |
3.13e-14 |
|
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240214 [Multi-domain] Cd Length: 120 Bit Score: 69.53 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 386 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFLSQSGETADTLMGLRYCKERGALTVGI 464
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 30923274 465 TNTVGSSISRETD 477
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-160 |
9.50e-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: 71.53 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 2 CGIFAYLNyhvpRTRREIL-ETLIKGLQRLEYRG-YDSAGVGFDGGND-------KDweanackIQLIKKKGkvkaLDEE 72
Cdd:cd01907 1 CGIFGIMS----KDGEPFVgALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgKD-------MEVFKGVG----YPED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 73 VHKQQDMDldiEFDVHLGIAHTRWATHgepSPVN---SHPqrsdknneF-----IVIHNGIITNYKDLKKFLESKGYDFE 144
Cdd:cd01907 66 IARRYDLE---EYKGYHWIAHTRQPTN---SAVWwygAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFE 131
|
170
....*....|....*.
gi 30923274 145 SETDTETIAKLVKYMY 160
Cdd:cd01907 132 TETDTEVIAYYLDLLL 147
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
90-189 |
3.98e-13 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 66.56 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 90 GIAHTRWATHGEPS----PVNShpqrSDKNneFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkYMYdnres 165
Cdd:pfam13522 13 ALGHVRLAIVDLPDagnqPMLS----RDGR--LVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL--YEE----- 79
|
90 100
....*....|....*....|....
gi 30923274 166 qdtsfttLVERVIQQLEGAFALVF 189
Cdd:pfam13522 80 -------WGEDCLERLRGMFAFAI 96
|
|
| 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 30923274 109 PQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYdnresqdtsfttlVERVIQQLEGAFALV 188
Cdd:pfam13537 15 PMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW-------------GEDCVDRLNGMFAFA 81
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
432-509 |
1.50e-10 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 62.88 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 432 DDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF--A 507
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstG 211
|
..
gi 30923274 508 LM 509
Cdd:PRK05441 212 VM 213
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-188 |
4.61e-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: 60.26 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 2 CGIFAYLNYHVPRTRREILETLikgLQRLEYRGYDSAGvgfdggndkdweanackiqlikkkgkvkaldeevhkqqdmdl 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERM---LDALAHRGPDGSG------------------------------------------ 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 82 dIEFDVHLGIAHTRWATHGepsPVNSH-PQRSDKNNeFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLvkYM- 159
Cdd:cd00712 36 -IWIDEGVALGHRRLSIID---LSGGAqPMVSEDGR-LVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL--YEe 108
|
170 180
....*....|....*....|....*....
gi 30923274 160 YDnresqdtsfttlvERVIQQLEGAFALV 188
Cdd:cd00712 109 WG-------------EDCLERLNGMFAFA 124
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
419-510 |
6.43e-10 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 60.23 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 419 ASDFLDRNTPvfRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 496
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90
....*....|....*.
gi 30923274 497 TSQFVSLVMF--ALMM 510
Cdd:cd05007 186 TAQKLALNMLstAVMI 201
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
386-690 |
1.15e-09 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 60.40 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 386 RLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFL--SQSGETADTLMGLRYCKERGALTVG 463
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 464 ITNTVGSSISRETDCGVHINAGPEIGVASTKAYTsqfVSLVMFAlmmcddRISMQERRKEIMLGLKRLPDLIKEVLSMDD 543
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS---VVLEMIT------RLAPNAEIGKIKNDLKQLPNALGHLVRTWE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 544 EIQKLATELYHQKSVL-------IMGRGYHyatclEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHT 616
Cdd:PRK11382 196 EKGRQLGELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDES 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30923274 617 YAKCQNALQQVVARQGRPVVICDKEDTETIKntkrtikvphsvDCLQGILSVIPLQLLAFHLAVLRGYDVDFPR 690
Cdd:PRK11382 271 RHTTERAINFVKQRTDNVIVIDYAEISQGLH------------PWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-155 |
2.30e-09 |
|
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: 60.62 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLNYHVPRTRreilETLIKGLQRLEYRGYDSAGVGFDGgndkdweanackiqlikkkgkvkaldeevhkqqdmd 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------ 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30923274 81 ldiefdvHLGIAHTRWATHGEPSpvNSHpQ-RSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKL 155
Cdd:COG0367 41 -------GVALGHRRLSIIDLSE--GGH-QpMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
387-465 |
2.38e-09 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 54.69 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 387 LILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFLSQSGETADTLMGLRYCKERGALTVGI 464
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 30923274 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 |
9.91e-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: 57.41 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 419 ASDFLDRN-TPvfrDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIgVA-ST--K 494
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 30923274 495 AYTSQFVSLVMF--ALM 509
Cdd:COG2103 198 AGTAQKLVLNMLstAAM 214
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
385-511 |
2.11e-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: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 385 RRLILIACGTSYHAG---VATRQVleelTELPvmvelaSDFLDrntP----------VFRDDVCFFLSQSGETADTLMGL 451
Cdd:cd05014 1 GKVVVTGVGKSGHIArkiAATLSS----TGTP------AFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30923274 452 RYCKERGALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFVSLVMF-ALMMC 511
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 ... |
378-505 |
2.74e-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: 53.00 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 378 IKEIQRCRRLILIACGTSYHAG--VATRqvleeLTELPVMVELASD---FLDRNTPVFRDDVCFFLSQSGETADTLMGLR 452
Cdd:cd05013 7 VDLLAKARRIYIFGVGSSGLVAeyLAYK-----LLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30923274 453 YCKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVM 505
Cdd:cd05013 82 IAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
378-511 |
5.82e-07 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 51.85 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 378 IKEIQRCRRLILIACGTSYHAGVATRQVLEEL----TELPVMVELASDFLDRNTPvfrDDVCFFLSQSGETADTLMGLRY 453
Cdd:COG1737 128 VDLLAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARL 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30923274 454 CKERGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFVSLVMF-ALMMC 511
Cdd:COG1737 205 AKERGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALIdALAAA 261
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
88-156 |
1.63e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 49.96 E-value: 1.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30923274 88 HLGIAHTRWATHGEPSPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-----ESETDTETIAKLV 156
Cdd:COG0121 77 RLVIAHVRKATVGPVSLENTHPFRGG---RWLFAHNGQLDGFDRLRRRLAEELPDElyfqpVGTTDSELAFALL 147
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
431-511 |
4.34e-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: 49.20 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 431 RDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDcgVHINAGPE-----IGVASTkayTSQFVSLVM 505
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
....*..
gi 30923274 506 F-ALMMC 511
Cdd:COG0794 166 GdALAVA 172
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
120-189 |
7.83e-06 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 48.87 E-value: 7.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 120 VIHNGIITNYKDLKKFLESKGYDFESETDTETIakLVKYMYDNresqdtsfttlvERVIQQLEGAFALVF 189
Cdd:TIGR01536 70 IVFNGEIYNHEELREELEAKGYTFQTDSDTEVI--LHLYEEWG------------EECVDRLDGMFAFAL 125
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-188 |
1.43e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 48.17 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLNYhvpRTRREILETLIKGL-QRLEYRGYDSAGVgfdggndkdweanackiqlikkkgkvkaldeevhkqqdM 79
Cdd:PTZ00077 1 MCGILAIFNS---KGERHELRRKALELsKRLRHRGPDWSGI--------------------------------------I 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 80 DLDIEFDVHLGIAHTRWATHGepsPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYm 159
Cdd:PTZ00077 40 VLENSPGTYNILAHERLAIVD---LSDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKE- 115
|
170 180
....*....|....*....|....*....
gi 30923274 160 YDNREsqdtsfttlverVIQQLEGAFALV 188
Cdd:PTZ00077 116 YGPKD------------FWNHLDGMFATV 132
|
|
| 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 30923274 88 HLGIAHTRWATHGEPSPVNSHPQRSDknnEFIVIHNGIITNYKDLKKFLESKGYDF-ESETDTETIAKL 155
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFAL 146
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-152 |
6.88e-05 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 46.05 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 1 MCGIFAYLNYH--VPRTRREILEtlikGLQRLEYRGYDSAGVgFDGGNdkdweanackiqlikkkgkvkaldeevhkqqd 78
Cdd:PRK09431 1 MCGIFGILDIKtdADELRKKALE----MSRLMRHRGPDWSGI-YASDN-------------------------------- 43
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30923274 79 mdldiefdvhlGI-AHTRWA----THGEPSPVNShpqrsDKNNefIVIHNGIITNYKDLKKFLESKgYDFESETDTETI 152
Cdd:PRK09431 44 -----------AIlGHERLSivdvNGGAQPLYNE-----DGTH--VLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVI 103
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
432-506 |
1.24e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 44.68 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30923274 432 DDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFVSLVMF 506
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
558-640 |
5.29e-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: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 558 VLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGP-LALVDKLMPVIMIIMRdHTYAKCQNALQQVVARQGRPVV 636
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYS-GRTEELLAALEIAKELGIPVIA 79
|
....
gi 30923274 637 ICDK 640
Cdd:cd04795 80 ITDA 83
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
88-207 |
1.95e-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: 40.78 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30923274 88 HLGIAHTRWATHGEPSPVNSHP-QRSDKNNEFIVIHNGiitnykDLKKFLESKGYDFE--SETDTETI-----AKLVKYM 159
Cdd:pfam13230 72 RNVIAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNG------DLKGYAPKLSGRFQpvGSTDSELAfcwllDRLASRF 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 30923274 160 YDNRESQDTSFTTLVE--RVIQQLeGAFALVFKSvhfpGQAVGTRRGSPL 207
Cdd:pfam13230 146 PYARPSAGELFRALRElaREIAAH-GTFNFLLSD----GRDLFAHCSTRL 190
|
|
| |
