|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-665 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 879.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLNYLTPKSRQEVLDLLVTGLKRLEYRGYDSTGVAID---SPDNKNIVMVKRTGKVKVLEEAIQEHFSGREYS- 76
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDndpSLESSSPLVFREEGKIESLVRSVYEEVAETDLNl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 77 -EPVLTHVGIAHTRWATHGVPCEKNSHPHRSDDENGFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLW- 154
Cdd:PLN02981 81 dLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 155 KTHP---TYSFRELVEQAILQVEGAFAIAVKSKYFPGECVASRRSSPLLVGIKTktrlatdhipilygkvLPRSESTSEF 231
Cdd:PLN02981 161 KLNEeegDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKE----------------LPEEKNSSAV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 232 MPLE-------EKEVEYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKK-------SLDDPHA--REITTLKM 295
Cdd:PLN02981 225 FTSEgfltknrDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENekgrgggGLSRPASveRALSTLEM 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 296 EIQQIMKGNYDYFMQKEIFEQPDSVVNTMRGRVRFDGNA----IVLGGIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQL 371
Cdd:PLN02981 305 EVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGSGkakrVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 372 LEELTELPVMVELASDFLDRNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAG 451
Cdd:PLN02981 385 LEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 452 PEIGVASTKAYTSQFISLVMFALVMSEDRLSLQQRRLEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGY 531
Cdd:PLN02981 465 AEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGY 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 532 NFATCLEGALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEET 611
Cdd:PLN02981 545 NYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASS 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 320546263 612 K--AFSSRHLEIPRTVDCLQGILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTVE 665
Cdd:PLN02981 625 VcpSGGCRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-665 |
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: 807.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLnyltpkSRQEVLDLLVTGLKRLEYRGYDSTGVAIdsPDNKNIVMVKRTGKVKVLEEAIQEhfsgreysEPVL 80
Cdd:COG0449 1 MCGIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAV--LDDGGLEVRKAVGKLANLEEKLAE--------EPLS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 81 THVGIAHTRWATHGVPCEKNSHPHRSDDENgFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLWKThpTY 160
Cdd:COG0449 65 GTIGIGHTRWATHGAPSDENAHPHTSCSGR-IAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKG--GG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 161 SFRELVEQAILQVEGAFAIAVKSKYFPGECVASRRSSPLLVGIktktrlatdhipilyGkvlprsestsefmpleekEVE 240
Cdd:COG0449 142 DLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGL---------------G------------------EGE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 241 YFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKkslDDPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDSV 320
Cdd:COG0449 189 NFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLD---GEPVEREVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 321 VNTMRGRVRFDGNaIVLGGIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDDV 400
Cdd:COG0449 266 RDTLRGRLDEDGR-VVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVVDPGTL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 401 CFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMSEDR 480
Cdd:COG0449 345 VIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLARAR 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 481 LSL-QQRRLEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGEL 559
Cdd:COG0449 425 GTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEISYIHAEGYAAGEL 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 560 KHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETKAFSSRHLEIPRTVDCLQGILTVIPMQL 639
Cdd:COG0449 505 KHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEVDELLAPILAVVPLQL 584
|
650 660
....*....|....*....|....*.
gi 320546263 640 LSYHIAVLRGCDVDCPRNLAKSVTVE 665
Cdd:COG0449 585 LAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-665 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 743.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLnyltpkSRQEVLDLLVTGLKRLEYRGYDSTGVAIdsPDNKNIVMVKRTGKVKVLEEAIQEhfsgreysEPVL 80
Cdd:PRK00331 1 MCGIVGYV------GQRNAAEILLEGLKRLEYRGYDSAGIAV--LDDGGLEVRKAVGKVANLEAKLEE--------EPLP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 81 THVGIAHTRWATHGVPCEKNSHPHRSDDENgFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLWKTHPty 160
Cdd:PRK00331 65 GTTGIGHTRWATHGKPTERNAHPHTDCSGR-IAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGG-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 161 SFRELVEQAILQVEGAFAIAVKSKYFPGECVASRRSSPLLVGIktktrlatdhipilygkvlprsestsefmpleeKEVE 240
Cdd:PRK00331 142 DLLEAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL---------------------------------GEGE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 241 YFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKkslDDPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDSV 320
Cdd:PRK00331 189 NFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFD---GNPVEREVYTVDWDASAAEKGGYRHFMLKEIYEQPEAI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 321 VNTMRGRVRFDGNaivlggIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDDV 400
Cdd:PRK00331 266 RDTLEGRLDELGE------GELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEFRYRDPVLSPKTL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 401 CFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMSEDR 480
Cdd:PRK00331 340 VIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALALAKAR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 481 LSLQQRRL-EILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGEL 559
Cdd:PRK00331 420 GTLSAEEEaDLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIHAEGYAAGEL 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 560 KHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETkAFSSRHLEIPRTVDCLQGILTVIPMQL 639
Cdd:PRK00331 500 KHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVA-EEADDVIEVPEVHELLAPLLYVVPLQL 578
|
650 660
....*....|....*....|....*.
gi 320546263 640 LSYHIAVLRGCDVDCPRNLAKSVTVE 665
Cdd:PRK00331 579 LAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-665 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 691.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLNYLTPKSRQEVLDLLVTGLKRLEYRGYDSTGVAIDS--------------PDNKNIVmVKRTGKVKVLEEAI 66
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDAnigsekedgtaasaPTPRPCV-VRSVGNISQLREKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 67 qehFSG------REYSEPVLTHVGIAHTRWATHGVPCEKNSHPHRSDDEnGFVVVHNGIITNYNDVKTFLSKRGYEFESD 140
Cdd:PTZ00394 80 ---FSEavaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNG-EFTIVHNGIVTNYMTLKELLKEEGYHFSSD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 141 TDTEVFAKLVHHLWKTHPTYSFRELVEQAILQVEGAFAIAVKSKYFPGECVASRRSSPLLVGIktktRLATDHIPILYGK 220
Cdd:PTZ00394 156 TDTEVISVLSEYLYTRKGIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGI----RRTDDRGCVMKLQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 221 VLPrsestsefMPLEEKEVEYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKKSLDDPHAREITTLKMEIQQI 300
Cdd:PTZ00394 232 TYD--------LTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQHLDAKPEGL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 301 MKGNYDYFMQKEIFEQPDSVVNTMRGRVRFDGNAIVLGGIKD-YIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELP 379
Cdd:PTZ00394 304 SKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQqSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 380 VMVELASDFLDRNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVAST 459
Cdd:PTZ00394 384 ISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVAST 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 460 KAYTSQFISLVMFALVMSEDRLSLQQRRLEILQALSKLADQIRDVLQLDSK-VKELAKDLYQHKSLLIMGRGYNFATCLE 538
Cdd:PTZ00394 464 KAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKITHDpVKALAARLKESSSILVLGRGYDLATAME 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 539 GALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETKAFSSRH 618
Cdd:PTZ00394 544 AALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEI 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 320546263 619 LEIPRTVDCLQGILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTVE 665
Cdd:PTZ00394 624 VLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-665 |
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: 652.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 2 CGIFAYLnyltpkSRQEVLDLLVTGLKRLEYRGYDSTGVAIDSPDNknIVMVKRTGKVKVLEEAIQEHfsgreysePVLT 81
Cdd:TIGR01135 1 CGIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGK--LFVRKAVGKVAELANKLGEK--------PLPG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 82 HVGIAHTRWATHGVPCEKNSHPHRsdDENG-FVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHhlWKTHPTY 160
Cdd:TIGR01135 65 GVGIGHTRWATHGKPTDENAHPHT--DEGGrIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIE--EELREGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 161 SFRELVEQAILQVEGAFAIAVKSKYFPGECVASRRSSPLLVGIKTKtrlatdhipilygkvlprsestsefmpleekevE 240
Cdd:TIGR01135 141 DLLEAVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGLGDG---------------------------------E 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 241 YFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKKSlddPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDSV 320
Cdd:TIGR01135 188 NFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGA---PVQREVRVIDWDLDAAEKGGYRHFMLKEIYEQPRAL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 321 VNTMRGRVRFDGNAIVLGGIKDyipEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDDV 400
Cdd:TIGR01135 265 RDTLEGRIEENGGVFEELGAEE---LLKNIDRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDTL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 401 CFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMSEDR 480
Cdd:TIGR01135 342 VIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKAR 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 481 --LSLQQRRlEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGE 558
Cdd:TIGR01135 422 gtLSAEEEA-ELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEGYPAGE 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 559 LKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETKAFSSRHLEIPRTVDCLQGILTVIPMQ 638
Cdd:TIGR01135 501 LKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEVEELLAPIVYTIPLQ 580
|
650 660
....*....|....*....|....*..
gi 320546263 639 LLSYHIAVLRGCDVDCPRNLAKSVTVE 665
Cdd:TIGR01135 581 LLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-664 |
1.60e-148 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 445.23 E-value: 1.60e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLnyltpkSRQEVLDLLVTGLKRLEYRGYDSTGVAIDSPDNKNIVM----VKRTGK-VKVLEEAIQEHFSGrey 75
Cdd:PTZ00295 24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGISTISSGGELKTTkyasDGTTSDsIEILKEKLLDSHKN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 76 sepvlTHVGIAHTRWATHGVPCEKNSHPHrSDDENGFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHhlWK 155
Cdd:PTZ00295 95 -----STIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIG--LE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 156 THPTYSFRELVEQAILQVEGAFAIAVKSKYFPGECVASRRSSPLLVGIktktrlATDHIpilygkvlprsestsefmple 235
Cdd:PTZ00295 167 LDQGEDFQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGI------GDDSI--------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 236 ekeveyFFASDASAVIEHTNRVIYLEDDDVAAVRdgtlsihrLKKSLDDPHAREITTLKMEIQQIMKGNYDYFMQKEIFE 315
Cdd:PTZ00295 220 ------YVASEPSAFAKYTNEYISLKDGEIAELS--------LENVNDLYTQRRVEKIPEEVIEKSPEPYPHWTLKEIFE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 316 QPDSVVNTMRGRVRFDG--NAIVLGGIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTEL-PVMVELASDF-LDR 391
Cdd:PTZ00295 286 QPIALSRALNNGGRLSGynNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVIDASELtLYR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 392 NTpifRDDVCF-FISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLV 470
Cdd:PTZ00295 366 LP---DEDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 471 MFALVMSE--DRLSLQQRRLEILQALSKLADQIRDVLQL-DSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELT 547
Cdd:PTZ00295 443 LIALWFAQnkEYSCSNYKCSSLINSLHRLPTYIGMTLKScEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEIT 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 548 YMHSEGIMAGELKHGPLALVD--DSMPVLMIVLRDPVYVKCMNALQQVTSRkGCPIIICEEGDEETKAFSSRHLEIPrTV 625
Cdd:PTZ00295 523 YIHAEGFSGGALKHGPFALIDkeKNTPVILIILDDEHKELMINAAEQVKAR-GAYIIVITDDEDLVKDFADEIILIP-SN 600
|
650 660 670
....*....|....*....|....*....|....*....
gi 320546263 626 DCLQGILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTV 664
Cdd:PTZ00295 601 GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-268 |
1.09e-114 |
|
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: 342.50 E-value: 1.09e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 2 CGIFAYLNYltpksrQEVLDLLVTGLKRLEYRGYDSTGVAIDspDNKNIVMVKRTGKVKVLEEAIQEHfsgreysePVLT 81
Cdd:cd00714 1 CGIVGYIGK------REAVDILLEGLKRLEYRGYDSAGIAVI--GDGSLEVVKAVGKVANLEEKLAEK--------PLSG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 82 HVGIAHTRWATHGVPCEKNSHPHRSDDeNGFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLWKTHPtyS 161
Cdd:cd00714 65 HVGIGHTRWATHGEPTDVNAHPHRSCD-GEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGL--D 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 162 FRELVEQAILQVEGAFAIAVKSKYFPGECVASRRSSPLLVGIKtktrlatdhipilygkvlprsestsefmpleekEVEY 241
Cdd:cd00714 142 LLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIG---------------------------------DGEN 188
|
250 260
....*....|....*....|....*..
gi 320546263 242 FFASDASAVIEHTNRVIYLEDDDVAAV 268
Cdd:cd00714 189 FVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
311-665 |
1.80e-68 |
|
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: 227.09 E-value: 1.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 311 KEIFEQPDSVVNTmrgrvrFDGNAIVLGGIKDYIPEIKRcRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLD 390
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 391 RNTPIFRD-DVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISL 469
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 470 VMFALVMSEDRlslqqrrlEILQALSKLADQIRDVLQLDSKVKELAkDLYQHKSLLIMGRGYNFATCLEGALKVKELTYM 549
Cdd:COG2222 155 LALLAAWGGDD--------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 550 HSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETkafssRHLEIPRTVDCLQ 629
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAI-----TLPAIPDLHDALD 300
|
330 340 350
....*....|....*....|....*....|....*.
gi 320546263 630 GILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTVE 665
Cdd:COG2222 301 PLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
510-663 |
8.35e-66 |
|
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: 213.28 E-value: 8.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 510 KVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNA 589
Cdd:cd05009 2 DIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320546263 590 LQQVTSRKGCPIIICEEGDEETKAFssRHLEIPRTVDCLQGILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVT 663
Cdd:cd05009 82 IKEVKARGAKVIVITDDGDAKDLAD--VVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
352-477 |
1.90e-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: 200.80 E-value: 1.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 352 RLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGIT 431
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 320546263 432 NTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMS 477
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-266 |
1.48e-54 |
|
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: 185.73 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 2 CGIFAYLNYLTPKSRQEVLDLlvTGLKRLEYRGYDSTGVAIDSPDNKNIVMVKRTGkvkvleeaiqEHFSGREYSEPVLT 81
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLL--RGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPV----------SDVALDLLDEPLKS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 82 HVGIAHTRWATHGVPCEKNSHPHRSDDeNGFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLWKTHPtys 161
Cdd:cd00352 69 GVALGHVRLATNGLPSEANAQPFRSED-GRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 162 FRELVEQAILQVEGAFAIAVKSKYfPGECVASRRS---SPLLVGIKtktrlatdhipilygkvlprsestsefmpleeKE 238
Cdd:cd00352 145 LFEAVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGIT--------------------------------KD 191
|
250 260
....*....|....*....|....*....
gi 320546263 239 VEYFFASDASAVIEHT-NRVIYLEDDDVA 266
Cdd:cd00352 192 GGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
346-474 |
4.76e-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: 142.82 E-value: 4.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 346 EIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDR-NTPIFRDDVCFFISQSGETADTLMALRYCKQRG 424
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 320546263 425 ALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFAL 474
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAV 130
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
518-648 |
1.77e-22 |
|
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: 93.52 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 518 LYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMnALQQVTSRK 597
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 320546263 598 GCPIIICEEGDEETKAFSSRHLEIPRTVDCLQGILTVIPMQLLSYHIAVLR 648
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-181 |
2.16e-20 |
|
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: 94.70 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLnyltpkSRQEVLDLLVTGLKRLEYRGYDSTGVAidSPDNKNIVMVKRTGKVK-VLEEAIQEHFSGreysepv 79
Cdd:COG0034 7 ECGVFGIY------GHEDVAQLTYYGLYALQHRGQESAGIA--TSDGGRFHLHKGMGLVSdVFDEEDLERLKG------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 80 ltHVGIAHTRWATHGVPCEKNSHPHRSDDENG-FVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLWKTHp 158
Cdd:COG0034 72 --NIAIGHVRYSTTGSSSLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKE- 148
|
170 180
....*....|....*....|...
gi 320546263 159 tySFRELVEQAILQVEGAFAIAV 181
Cdd:COG0034 149 --DLEEAIKEALRRVKGAYSLVI 169
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-174 |
1.15e-19 |
|
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: 88.86 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 2 CGIFAYlnYLTPKSRQeVLDLLVTGLKRLEYRG-YDSTGVAI-DSPD------NKNIVMVKRTGkvkvLEEAIQEHFSGR 73
Cdd:cd01907 1 CGIFGI--MSKDGEPF-VGALLVEMLDAMQERGpGDGAGFALyGDPDafvyssGKDMEVFKGVG----YPEDIARRYDLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 74 EYSepvlTHVGIAHTRWATHGVPCEKNSHPHRSDDEngfVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHL 153
Cdd:cd01907 74 EYK----GYHWIAHTRQPTNSAVWWYGAHPFSIGDI---AVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLL 146
|
170 180
....*....|....*....|.
gi 320546263 154 WKTHptYSFRELVEQAILQVE 174
Cdd:cd01907 147 LRKG--GLPLEYYKHIIRMPE 165
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-181 |
6.80e-17 |
|
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: 80.97 E-value: 6.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 2 CGIFAYLNyltpksRQEVLDLLVTGLKRLEYRGYDSTGVAIDspDNKNIVMVKRTGKVK-VLEEAIQEHFSGreysepvl 80
Cdd:cd00715 1 CGVFGIYG------AEDAARLTYLGLYALQHRGQESAGIATS--DGKRFHTHKGMGLVSdVFDEEKLRRLPG-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 81 tHVGIAHTRWATHGVPCEKNSHPHRSDDENGFV-VVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLV-HHLwkthP 158
Cdd:cd00715 65 -NIAIGHVRYSTAGSSSLENAQPFVVNSPLGGIaLAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIaRSL----A 139
|
170 180
....*....|....*....|...
gi 320546263 159 TYSFRELVEQAILQVEGAFAIAV 181
Cdd:cd00715 140 KDDLFEAIIDALERVKGAYSLVI 162
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
82-181 |
1.21e-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: 70.80 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 82 HVGIAHTRWATHGVPCEKNsHPHRSDDEnGFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLvhhlwkthptys 161
Cdd:pfam13522 11 GVALGHVRLAIVDLPDAGN-QPMLSRDG-RLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL------------ 76
|
90 100
....*....|....*....|
gi 320546263 162 FRELVEQAILQVEGAFAIAV 181
Cdd:pfam13522 77 YEEWGEDCLERLRGMFAFAI 96
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-181 |
1.37e-14 |
|
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: 76.59 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 2 CGIFAYLNyltpkSRQEVLDLLVTGLKRLEYRGYDSTGVAIDspDNKNIVMVKRTGKV-KVLEEAIQEHFSGreysepvl 80
Cdd:TIGR01134 1 CGVVGIYG-----QEEVAASLTYYGLYALQHRGQESAGISVF--DGNRFRLHKGNGLVsDVFNEEHLQRLKG-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 81 tHVGIAHTRWATHGVPCEKNSHPHRSDDENGFV-VVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLwkTHPT 159
Cdd:TIGR01134 66 -NVGIGHVRYSTAGSSGLENAQPFVVNSPYGGLaLAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHN--DESK 142
|
170 180
....*....|....*....|..
gi 320546263 160 YSFRELVEQAILQVEGAFAIAV 181
Cdd:TIGR01134 143 DDLFDAVARVLERVRGAYALVL 164
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
352-443 |
4.58e-14 |
|
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240214 [Multi-domain] Cd Length: 120 Bit Score: 69.14 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 352 RLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDD-VCFFISQSGETADTLMALRYCKQRGALIVGI 430
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 320546263 431 TNTVGSSICRESH 443
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-184 |
1.42e-12 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 70.45 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 2 CGIF-AYLNyltpkSRQEVLDLLVTGLKRLEYRGYDSTGVAIDspDNKNIVMVKRTGKV-KVLEEAIQEHFSGreysepv 79
Cdd:PRK05793 15 CGVFgVFSK-----NNIDVASLTYYGLYALQHRGQESAGIAVS--DGEKIKVHKGMGLVsEVFSKEKLKGLKG------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 80 ltHVGIAHTRWATHGVPCEKNSHPHRSDDENGFV-VVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLWKthp 158
Cdd:PRK05793 81 --NSAIGHVRYSTTGASDLDNAQPLVANYKLGSIaIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK--- 155
|
170 180
....*....|....*....|....*.
gi 320546263 159 tYSFRELVEQAILQVEGAFAIAVKSK 184
Cdd:PRK05793 156 -KGLEKALVDAIQAIKGSYALVILTE 180
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-181 |
5.39e-12 |
|
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: 65.66 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 2 CGIFAYLNYltpKSRQEVLDLLVTGLKRLEYRGYDSTGVAIDSpdnknivmvkrtgkvkvleeaiqehfsgreysepvlt 81
Cdd:cd00712 1 CGIAGIIGL---DGASVDRATLERMLDALAHRGPDGSGIWIDE------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 82 HVGIAHTRWAThgVPCEKNSHPHRSDDEnGFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVfakLVHhlwkthptyS 161
Cdd:cd00712 41 GVALGHRRLSI--IDLSGGAQPMVSEDG-RLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEV---ILH---------L 105
|
170 180
....*....|....*....|
gi 320546263 162 FRELVEQAILQVEGAFAIAV 181
Cdd:cd00712 106 YEEWGEDCLERLNGMFAFAL 125
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-181 |
5.21e-11 |
|
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: 65.63 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLNYLTPKSRQEVLDLLvtglKRLEYRGYDSTGVAIDSpdnknivmvkrtgkvkvleeaiqehfsgreysepvl 80
Cdd:COG0367 1 MCGIAGIIDFDGGADREVLERML----DALAHRGPDGSGIWVDG------------------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 81 tHVGIAHTRWAThgVPCEKNSH-PHRSDDEnGFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVfakLVHhlwkthpt 159
Cdd:COG0367 41 -GVALGHRRLSI--IDLSEGGHqPMVSEDG-RYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEV---ILH-------- 105
|
170 180
....*....|....*....|..
gi 320546263 160 ySFRELVEQAILQVEGAFAIAV 181
Cdd:COG0367 106 -AYEEWGEDCLERLNGMFAFAI 126
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
87-181 |
7.65e-11 |
|
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: 59.84 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 87 HTRWATHGVPcekNSH-PHRSDDENGFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVFAKLVHHLWkthptysfrel 165
Cdd:pfam13537 1 HRRLSIIDLE---GGAqPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW----------- 66
|
90
....*....|....*.
gi 320546263 166 VEQAILQVEGAFAIAV 181
Cdd:pfam13537 67 GEDCVDRLNGMFAFAI 82
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-179 |
9.94e-11 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 64.31 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLNyltpksRQEVLDLLVTGLKRLEYRGYDSTGvaIDSPDNKNIVMVKRTGKVK-VLEEAIQEHFSGreysepv 79
Cdd:PLN02440 1 ECGVVGIFG------DPEASRLCYLGLHALQHRGQEGAG--IVTVDGNRLQSITGNGLVSdVFDESKLDQLPG------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 80 ltHVGIAHTRWATHGVPCEKNSHPHRSDDENGFV-VVHNGIITNYNDVKTFLSKRGYEFESDTDTEVfaklVHHLWKTHP 158
Cdd:PLN02440 66 --DIAIGHVRYSTAGASSLKNVQPFVANYRFGSIgVAHNGNLVNYEELRAKLEENGSIFNTSSDTEV----LLHLIAISK 139
|
170 180
....*....|....*....|.
gi 320546263 159 TYSFRELVEQAILQVEGAFAI 179
Cdd:PLN02440 140 ARPFFSRIVDACEKLKGAYSM 160
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
347-471 |
1.04e-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: 59.94 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 347 IKRCRRLMLIGCGTSYHSAvatRQLLEELTELPVMVELASD---FLDRNTPIFRDDVCFFISQSGETADTLMALRYCKQR 423
Cdd:cd05013 10 LAKARRIYIFGVGSSGLVA---EYLAYKLLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 320546263 424 GALIVGITNTVGSSICRESHcgVHINAGPEIGVASTKAYTSQFISLVM 471
Cdd:cd05013 87 GAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
355-431 |
1.21e-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: 58.15 E-value: 1.21e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320546263 355 LIGCGTSYHSAVATRQLLEELTELPVMVELASDFLD--RNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGIT 431
Cdd:cd04795 3 VIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAIT 81
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
347-497 |
4.57e-10 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 61.10 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 347 IKRCRRLMLIGCGTSYHSAVATRQLLEEL----TELPVMVELASDFLDRNTPifrDDVCFFISQSGETADTLMALRYCKQ 422
Cdd:COG1737 131 LAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARLAKE 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320546263 423 RGALIVGITNTVGSSICRESHcgVHINAGPEIGVASTKAYTSQFISLVM----FALVMSEDRLSLQQRRLEILQALSKL 497
Cdd:COG1737 208 RGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALidalAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-162 |
7.68e-10 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 62.04 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 1 MCGIFAYLNYLtpKSRQEVLDLLVTGLKRLEYRGYDSTGVaidspdnknivmvkrtgkvKVLEeaiqehfsgreySEPVL 80
Cdd:PTZ00077 1 MCGILAIFNSK--GERHELRRKALELSKRLRHRGPDWSGI-------------------IVLE------------NSPGT 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 81 THVgIAHTRWAThgVPCEKNSHPHRSDDENgFVVVHNGIITNYNDVKTFLSKRGYEFESDTDTEVfaklVHHLWKTHPTY 160
Cdd:PTZ00077 48 YNI-LAHERLAI--VDLSDGKQPLLDDDET-VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEI----IGHLYKEYGPK 119
|
..
gi 320546263 161 SF 162
Cdd:PTZ00077 120 DF 121
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
76-174 |
2.29e-08 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 55.36 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 76 SEPVLTHVGIAHTRWATHGVPCEKNSHPHRSDdenGFVVVHNGIITNYNDVKTFLSKR-----GYEFESDTDTEV-FAKL 149
Cdd:COG0121 71 ARPIKSRLVIAHVRKATVGPVSLENTHPFRGG---RWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELaFALL 147
|
90 100
....*....|....*....|....*
gi 320546263 150 VHHLWKTHPTySFRELVEqAILQVE 174
Cdd:COG0121 148 LSRLRDGGPD-PAEALAE-ALRELA 170
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
385-476 |
2.86e-08 |
|
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: 55.22 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 385 ASDFLDRNTPifRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVAST--KAY 462
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90
....*....|....*
gi 320546263 463 TSQFISLVMFA-LVM 476
Cdd:cd05007 186 TAQKLALNMLStAVM 200
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
351-477 |
3.74e-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: 52.16 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 351 RRLMLIGCGTSYHSA---VATrqlleeLTELpvmvELASDFLDrntP----------IFRDDVCFFISQSGETADTLMAL 417
Cdd:cd05014 1 GKVVVTGVGKSGHIArkiAAT------LSST----GTPAFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320546263 418 RYCKQRGALIVGITNTVGSSICRESH----CGVHINAGPeIGVASTkayTSQFISLVMF-ALVMS 477
Cdd:cd05014 68 PHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALGdALAVA 128
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
352-653 |
4.24e-08 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 55.39 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 352 RLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDrNTPIFRDDVCFFI--SQSGETADTLMALRYCKQRGALIVG 429
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 430 ITNTVGSSICRESHCGVHINAGPEIGVASTKAYtsqfiSLVMFALVMSEDRLSLQQRRLEILQALSKLADQIRDVLQLDS 509
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCY-----SVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRTWEEKGR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 510 KVKELAKD---LYQHKSLLIMGRGYNfatclEGALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKC 586
Cdd:PRK11382 200 QLGELASQwpmIYTVAAGPLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTT 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320546263 587 MNALQQVTSRKGCPIIIceegdeetkafssRHLEIPRTVD-CLQGILTVIPMQLLSYHIAVLRGCDVD 653
Cdd:PRK11382 275 ERAINFVKQRTDNVIVI-------------DYAEISQGLHpWLAPFLMFVPMEWLCYYLSIYKDHNPD 329
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
398-476 |
4.28e-08 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 55.17 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 398 DDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVAST--KAYTSQFISLVMFA-L 474
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIStG 211
|
..
gi 320546263 475 VM 476
Cdd:PRK05441 212 VM 213
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
52-181 |
1.09e-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: 51.57 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 52 MVKRTGKVKVLEEAIQE------H----FSGREYSEpvlTHVGIAHTRWAThgVPCEKNSHPHRSDDEnGFVVVHNGIIT 121
Cdd:TIGR01536 4 FFDLDDKAVEEDEAIKRmsdtiaHrgpdASGIEYKD---GNAILGHRRLAI--IDLSGGAQPMSNEGK-TYVIVFNGEIY 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 122 NYNDVKTFLSKRGYEFESDTDTEVfakLVHhlwkthptySFRELVEQAILQVEGAFAIAV 181
Cdd:TIGR01536 78 NHEELREELEAKGYTFQTDSDTEV---ILH---------LYEEWGEECVDRLDGMFAFAL 125
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
76-173 |
1.77e-06 |
|
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: 49.69 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 76 SEPVLTHVGIAHTRWATHGVPCEKNSHPHRsddENGFVVVHNGIITNYNDVKT-FLSKRGYEFESDTDTEVFAKLVHHLW 154
Cdd:cd01908 75 ARPIKSPLVLAHVRAATVGPVSLENCHPFT---RGRWLFAHNGQLDGFRLLRRrLLRLLPRLPVGTTDSELAFALLLSRL 151
|
90
....*....|....*....
gi 320546263 155 KTHPTYSFRELVEqAILQV 173
Cdd:cd01908 152 LERDPLDPAELLD-AILQT 169
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
385-476 |
2.90e-06 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 49.71 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 385 ASDFLDRN-TPifrDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIgVA-ST--K 460
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 320546263 461 AYTSQFISLVMFA-LVM 476
Cdd:COG2103 198 AGTAQKLVLNMLStAAM 214
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
397-487 |
6.68e-06 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 48.43 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 397 RDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHcgVHINAGPE-----IGVASTkayTSQFISLVM 471
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
90
....*....|....*..
gi 320546263 472 F-ALVMsedrlSLQQRR 487
Cdd:COG0794 166 GdALAV-----ALLEAR 177
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
398-443 |
2.54e-04 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 43.60 E-value: 2.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 320546263 398 DDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESH 443
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLAD 233
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| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
398-472 |
1.32e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 41.22 E-value: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320546263 398 DDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVAST--KAYTSQFISLVMF 472
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
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| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
392-450 |
5.59e-03 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 38.33 E-value: 5.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 392 NTP-IFRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINA 450
Cdd:cd05005 69 TTPaIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPA 128
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| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
352-431 |
9.44e-03 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 36.47 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546263 352 RLMLIGCGTSYHSAVATRQLLEELTELPVMVeLASDFLDRntPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGIT 431
Cdd:cd05017 1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYV-VKDYTLPA--FVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77
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