|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-624 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 1023.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGRRPAYVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLANLEEAVAEMPstaLSGTTGLGHTRWATH 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEP---LPGTTGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 81 GRPTDRNAHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHGetaDDFVGSVLAVLRRL 160
Cdd:PRK00331 78 GKPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEG---GDLLEAVRKALKRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 161 EGHFTLVFANADDPGTLVAARRSTPLVLGIGDNEMFVGSDVAAFIEHTREAVELGQDQAVVITADGYRISDFDGNDglqa 240
Cdd:PRK00331 155 EGAYALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNP---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 241 gRDFRPFHIDWDLAAAEKGGYEYFMLKEIAEQPAAVADTLLGHFvggrIVLDEQRLSDQELREIDKVFVVACGTAYHSGL 320
Cdd:PRK00331 231 -VEREVYTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRL----DELGEGELADEDLKKIDRIYIVACGTSYHAGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 321 LAKYAIEHWTRLPVEVELASEFRYRDPVLDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVL 400
Cdd:PRK00331 306 VAKYLIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 401 YTRAGPEIGVASTKTFLAQIAANYLLGLALAQARGTKYPDEVEREYHELEAMPDLVARVIAATGPVAELAHRFAQSSTVL 480
Cdd:PRK00331 386 YTHAGPEIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNAL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 481 FLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEDGLPVIVVMPSPKgsatLHAKLLSNIREIQTRGAVTI 560
Cdd:PRK00331 466 FLGRGVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDE----LYEKTKSNIQEVKARGARVI 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489513448 561 VIAEEGDEtVRPYADHLIEIPAVSTLLQPLLSTIPLQVFAASVARARGYDVDKPRNLAKSVTVE 624
Cdd:PRK00331 542 VIADEGDE-VAEEADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-624 |
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: 1019.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGRRPAYVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLANLEEAVAEMPstaLSGTTGLGHTRWATH 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEP---LSGTIGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 81 GRPTDRNAHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHGetaDDFVGSVLAVLRRL 160
Cdd:COG0449 78 GAPSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGG---GDLLEAVRKALKRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 161 EGHFTLVFANADDPGTLVAARRSTPLVLGIGDNEMFVGSDVAAFIEHTREAVELGQDQAVVITADGYRISDFDGNDglqa 240
Cdd:COG0449 155 EGAYALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEP---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 241 gRDFRPFHIDWDLAAAEKGGYEYFMLKEIAEQPAAVADTLLGHFVG-GRIVLDEQRLSDQELREIDKVFVVACGTAYHSG 319
Cdd:COG0449 231 -VEREVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEdGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 320 LLAKYAIEHWTRLPVEVELASEFRYRDPVLDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAV 399
Cdd:COG0449 310 LVGKYLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 400 LYTRAGPEIGVASTKTFLAQIAANYLLGLALAQARGTKYPDEVEREYHELEAMPDLVARVIAATGPVAELAHRFAQSSTV 479
Cdd:COG0449 390 LYTHAGPEIGVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 480 LFLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEDGLPVIVVMPSPKgsatLHAKLLSNIREIQTRGAVT 559
Cdd:COG0449 470 LFLGRGINYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDE----LYEKTLSNIQEVKARGGKV 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489513448 560 IVIAEEGDETVRPYADHLIEIPAVSTLLQPLLSTIPLQVFAASVARARGYDVDKPRNLAKSVTVE 624
Cdd:COG0449 546 IAIADEGDEEVEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-624 |
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: 933.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 2 CGIVGYVGRRPAYVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLANLEEAVAEMPstaLSGTTGLGHTRWATHG 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKP---LPGGVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 82 RPTDRNAHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHGetaDDFVGSVLAVLRRLE 161
Cdd:TIGR01135 78 KPTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREG---GDLLEAVQKALKQLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 162 GHFTLVFANADDPGTLVAARRSTPLVLGIGDNEMFVGSDVAAFIEHTREAVELGQDQAVVITADGYRISDFDGNDglqAG 241
Cdd:TIGR01135 155 GAYALAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAP---VQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 242 RDFRpfHIDWDLAAAEKGGYEYFMLKEIAEQPAAVADTLLGHFVGGRIVLDEQrLSDQELREIDKVFVVACGTAYHSGLL 321
Cdd:TIGR01135 232 REVR--VIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEEL-GAEELLKNIDRIQIVACGTSYHAGLV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 322 AKYAIEHWTRLPVEVELASEFRYRDPVLDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLY 401
Cdd:TIGR01135 309 AKYLIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 402 TRAGPEIGVASTKTFLAQIAANYLLGLALAQARGTKYPDEVEREYHELEAMPDLVARVIAATGPVAELAHRFAQSSTVLF 481
Cdd:TIGR01135 389 TRAGPEIGVASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 482 LGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEDGLPVIVVMPSPKgsatLHAKLLSNIREIQTRGAVTIV 561
Cdd:TIGR01135 469 LGRGLGYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDS----LLEKTKSNVEEVKARGARVIV 544
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489513448 562 IAEEGDETVRPYADHLIEIPAVSTLLQPLLSTIPLQVFAASVARARGYDVDKPRNLAKSVTVE 624
Cdd:TIGR01135 545 FAPEDDETIASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-623 |
9.69e-160 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 472.58 E-value: 9.69e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGRRPAYVVVMDALRRMEYRGYDSSGIALV-DGGTLTVRRRAGRLAN---LEEAVAEMPSTALSGTTGLGHTR 76
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTIsSGGELKTTKYASDGTTsdsIEILKEKLLDSHKNSTIGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 77 WATHGRPTDRNAHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHGEtadDFVGSVLAV 156
Cdd:PTZ00295 104 WATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGE---DFQEAVKSA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 157 LRRLEGHFTLVFANADDPGTLVAARRSTPLVLGIGDNEMFVGSDVAAFIEHTREAVELGQDQAVVITADGyrISDFDGNd 236
Cdd:PTZ00295 181 ISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLEN--VNDLYTQ- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 237 glqagrdFRPFHIDWDLAAAEKGGYEYFMLKEIAEQPAAVADTLLghfVGGRIVLDEQRLS-------DQELREIDKVFV 309
Cdd:PTZ00295 258 -------RRVEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALN---NGGRLSGYNNRVKlggldqyLEELLNIKNLIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 310 VACGTAYHSGLLAKYAIEHWTRL-PVEVELASEF-RYRDPvlDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAICNT 387
Cdd:PTZ00295 328 VGCGTSYYAALFAASIMQKLKCFnTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 388 NGSQIPRECDAVLYTRAGPEIGVASTKTFLAQIAANYLLGLALAQAR-GTKYPDEVEREYHELEAMPDLVARVIAAT-GP 465
Cdd:PTZ00295 406 VGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNYKCSSLINSLHRLPTYIGMTLKSCeEQ 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 466 VAELAHRFAQSSTVLFLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALI--EDGLPVIVVMPSPKgsatlHA 543
Cdd:PTZ00295 486 CKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIdkEKNTPVILIILDDE-----HK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 544 KLLSNI-REIQTRGAVTIVIAEEGDEtVRPYADHLIEIPAVStLLQPLLSTIPLQVFAASVARARGYDVDKPRNLAKSVT 622
Cdd:PTZ00295 561 ELMINAaEQVKARGAYIIVITDDEDL-VKDFADEIILIPSNG-PLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVT 638
|
.
gi 489513448 623 V 623
Cdd:PTZ00295 639 V 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-624 |
2.04e-156 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 465.38 E-value: 2.04e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVG------RRPAYVVVMDALRRMEYRGYDSSGIALVDGGTLT-----VRRRAGRLANLEEAVAEMPST----- 64
Cdd:PLN02981 1 MCGIFAYLNynvpreRRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLEsssplVFREEGKIESLVRSVYEEVAEtdlnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 65 --ALSGTTGLGHTRWATHGRPTDRNAHPH-RDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYR 141
Cdd:PLN02981 81 dlVFENHAGIAHTRWATHGPPAPRNSHPQsSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 142 --HGETAD-DFVGSVLAVLRRLEGHFTLVFANADDPGTLVAARRSTPLVLGIGD------------------------NE 194
Cdd:PLN02981 161 klNEEEGDvTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKElpeeknssavftsegfltknrdkpKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 195 MFVGSDVAAFIEHTREAVELGQDQAVVITADGYRISDFDGNDGLQAGRDFRPFHIDWDLAAAE-------KGGYEYFMLK 267
Cdd:PLN02981 241 FFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGGLSRPASVERALSTLEmeveqimKGNYDHYMQK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 268 EIAEQPAAVADTLLGHFVGG------RIVLDEQRLSDQELREIDKVFVVACGTAYHSGLLAKYAIEHWTRLPVEVELASE 341
Cdd:PLN02981 321 EIHEQPESLTTTMRGRLIRGgsgkakRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 342 FRYRDPVLDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRAGPEIGVASTKTFLAQIA 421
Cdd:PLN02981 401 LLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQIV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 422 ANYLLGLALAQARGTKYpDEVEREYHELEAMPDLVARVIAATGPVAELAHRFAQSSTVLFLGRHVGYPVALEGALKLKEL 501
Cdd:PLN02981 481 AMTMLALALGEDSISSR-SRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 502 AYMHAEGFAAGELKHGPIALIEDGLPVIVVmpspkgsATLHA---KLLSNIREIQTRGAVTIVIAEEGDET-VRPY-ADH 576
Cdd:PLN02981 560 ALMHSEGILAGEMKHGPLALVDETLPIIVI-------ATRDAcfsKQQSVIQQLRARKGRLIVICSKGDASsVCPSgGCR 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 489513448 577 LIEIPAVSTLLQPLLSTIPLQVFAASVARARGYDVDKPRNLAKSVTVE 624
Cdd:PLN02981 633 VIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-624 |
3.22e-130 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 397.71 E-value: 3.22e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVG-RRPAYV-----VVMDALRRMEYRGYDSSGIAL-------VDGGTLT--------VRRRAGRLANLEEAVA 59
Cdd:PTZ00394 1 MCGIFGYANhNVPRTVeqilnVLLDGIQKVEYRGYDSAGLAIdanigseKEDGTAAsaptprpcVVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 60 EMPSTA--------LSGTTGLGHTRWATHGRPTDRNAHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEV 131
Cdd:PTZ00394 81 SEAVAAtlppmdatTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 132 AAHLVARAYRHgETADDFVGSVLAVLRRLEGHFTLVFANADDPGTLVAARRSTPLVLGI--------------------- 190
Cdd:PTZ00394 161 ISVLSEYLYTR-KGIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdls 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 191 GDNEMFVGSDVAAFIEHTREAVELgQDQAVVITADGyrISDFDGNDGLQAGRDFR-PFHIDWDLAAAEKGGYEYFMLKEI 269
Cdd:PTZ00394 240 GPLEVFFSSDVNSFAEYTREVVFL-EDGDIAHYCDG--ALRFYNAAERQRSIVKReVQHLDAKPEGLSKGNYPHFMLKEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 270 AEQPAAVADTLLGH--FVGGRIVLDEqrLSDQELREI---DKVFVVACGTAYHSGLLAKYAIEHWTRLPVEVELASEFRY 344
Cdd:PTZ00394 317 YEQPESVISSMHGRidFSSGTVQLSG--FTQQSIRAIltsRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 345 RDPVLDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRAGPEIGVASTKTFLAQIAANY 424
Cdd:PTZ00394 395 RRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 425 LLGLALA--QARGTKYPDEVEReyhELEAMPDLVARVIAATG-PVAELAHRFAQSSTVLFLGRHVGYPVALEGALKLKEL 501
Cdd:PTZ00394 475 LVALLLSsdSVRLQERRNEIIR---GLAELPAAISECLKITHdPVKALAARLKESSSILVLGRGYDLATAMEAALKVKEL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 502 AYMHAEGFAAGELKHGPIALIEDGLPVIVVMPSPKgsatlHAKL-LSNIREIQTRGAVTIVIAEEGDETVRPYADHLIEI 580
Cdd:PTZ00394 552 SYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDK-----HFGLsKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 489513448 581 PAVSTLLQPLLSTIPLQVFAASVARARGYDVDKPRNLAKSVTVE 624
Cdd:PTZ00394 627 PKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-222 |
3.82e-115 |
|
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: 3.82e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 2 CGIVGYVGRRPAYVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLANLEEAVAEMPstaLSGTTGLGHTRWATHG 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKP---LSGHVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 82 RPTDRNAHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHGEtadDFVGSVLAVLRRLE 161
Cdd:cd00714 78 EPTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGL---DLLEAVKKALKRLE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489513448 162 GHFTLVFANADDPGTLVAARRSTPLVLGIGDNEMFVGSDVAAFIEHTREAVELGQDQAVVI 222
Cdd:cd00714 155 GAYALAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
266-624 |
4.27e-74 |
|
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: 240.57 E-value: 4.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 266 LKEIAEQPAAVADTLlgHFVGGRIvldEQRLSDQELREIDKVFVVACGTAYHSGLLAKYAIEHWTRLPVEVELASEF-RY 344
Cdd:COG2222 1 AREIAQQPEAWRRAL--AALAAAI---AALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 345 RDPVLDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRAGPEIGVASTKTFLAQIAAny 424
Cdd:COG2222 76 PAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 425 llGLALAQARGtkyPDEVEREyhELEAMPDLVARVIAATGPVAELAhRFAQSSTVLFLGRHVGYPVALEGALKLKELAYM 504
Cdd:COG2222 154 --LLALLAAWG---GDDALLA--ALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 505 HAEGFAAGELKHGPIALIEDGLPVIVVMpSPKGSATLHAKLlsnIREIQTRGAVTIVIAEEGDETVrpyadHLIEIPAVS 584
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLA-SEDPTRELDLDL---AAELRALGARVVAIGAEDDAAI-----TLPAIPDLH 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489513448 585 TLLQPLLSTIPLQVFAASVARARGYDVDKPRNLAKSVTVE 624
Cdd:COG2222 297 DALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
306-431 |
6.66e-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: 198.49 E-value: 6.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 306 KVFVVACGTAYHSGLLAKYAIEHWTRLPVEVELASEFRYRDPVLDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAIC 385
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489513448 386 NTNGSQIPRECDAVLYTRAGPEIGVASTKTFLAQIAANYLLGLALA 431
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
466-622 |
1.87e-59 |
|
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: 195.56 E-value: 1.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 466 VAELAHRFAQSSTVLFLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEDGLPVIVVMPSPKgsatLHAKL 545
Cdd:cd05009 3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDR----LEEKL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489513448 546 LSNIREIQTRGAVTIVIAEEGDEtvRPYADHLIEIPAVSTLLQPLLSTIPLQVFAASVARARGYDVDKPRNLAKSVT 622
Cdd:cd05009 79 ESLIKEVKARGAKVIVITDDGDA--KDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-212 |
2.83e-59 |
|
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: 197.67 E-value: 2.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 2 CGIVGYVGRRPA----YVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLANLEEAVAEMPstaLSGTTGLGHTRW 77
Cdd:cd00352 1 CGIFGIVGADGAasllLLLLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEP---LKSGVALGHVRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 78 ATHGRPTDRNAHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHGetadDFVGSVLAVL 157
Cdd:cd00352 78 ATNGLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREG----GLFEAVEDAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489513448 158 RRLEGHFTLVFANAdDPGTLVAARRS---TPLVLGIG-DNEMFVGSDVAAFIEHTREAV 212
Cdd:cd00352 154 KRLDGPFAFALWDG-KPDRLFAARDRfgiRPLYYGITkDGGLVFASEPKALLALPFKGV 211
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-228 |
3.04e-39 |
|
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: 150.17 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGRRPAYVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAG------RLANLEEavaempstaLSGTTGLGH 74
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGlvsdvfDEEDLER---------LKGNIAIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 75 TRWATHGRPTDRNAHPH--RDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHgetaDDFVGS 152
Cdd:COG0034 78 VRYSTTGSSSLENAQPFyvNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTK----EDLEEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 153 VLAVLRRLEGHFTLVFAnadDPGTLVAAR-----RstPLVLGIGDNEMFVGSDVAAF----IEHTREaVELGqdQAVVIT 223
Cdd:COG0034 154 IKEALRRVKGAYSLVIL---TGDGLIAARdpngiR--PLVLGKLEDGYVVASESCALdilgAEFVRD-VEPG--EIVVID 225
|
....*
gi 489513448 224 ADGYR 228
Cdd:COG0034 226 EDGLR 230
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-232 |
6.94e-37 |
|
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: 137.98 E-value: 6.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 2 CGIVGYVGRRPAYVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLANL--EEAVAEmpstaLSGTTGLGHTRWAT 79
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVfdEEKLRR-----LPGNIAIGHVRYST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 80 HGRPTDRNAHPH--RDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHgetaDDFVGSVLAVL 157
Cdd:cd00715 76 AGSSSLENAQPFvvNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK----DDLFEAIIDAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 158 RRLEGHFTLVFANADdpgTLVAAR-----RstPLVLGIGDNEMFV-GSDVAAF----IEHTREaVELGqdQAVVITADGY 227
Cdd:cd00715 152 ERVKGAYSLVIMTAD---GLIAVRdphgiR--PLVLGKLEGDGYVvASESCALdiigAEFVRD-VEPG--EIVVIDDDGL 223
|
....*
gi 489513448 228 RISDF 232
Cdd:cd00715 224 ESSQR 228
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
300-429 |
1.18e-36 |
|
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: 133.19 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 300 ELREIDKVFVVACGTAYHSGLLAKYAIEHWTRLPVEVELASEFRYR-DPVLDRSTLVVAISQSGETADTLEAVRHAKEQK 378
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489513448 379 AKVLAICNTNGSQIPRECDAVLYTRAGPEIGVASTKTFLAQIAANYLLGLA 429
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-228 |
6.05e-31 |
|
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: 125.90 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 2 CGIVGYVGRRP-AYVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLANL--EEAVAEmpstaLSGTTGLGHTRWA 78
Cdd:TIGR01134 1 CGVVGIYGQEEvAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVfnEEHLQR-----LKGNVGIGHVRYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 79 THGRPTDRNAHP--HRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYrhgETADDFVGSVLAV 156
Cdd:TIGR01134 76 TAGSSGLENAQPfvVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHND---ESKDDLFDAVARV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 157 LRRLEGHFTLVFAnadDPGTLVAAR-----RstPLVLGIGDNEMFVGSDVAAF----IEHTREaVELGqdQAVVITADGY 227
Cdd:TIGR01134 153 LERVRGAYALVLM---TEDGLVAVRdphgiR--PLVLGRRGDGYVVASESCALdilgAEFVRD-VEPG--EVVVIFDGGL 224
|
.
gi 489513448 228 R 228
Cdd:TIGR01134 225 E 225
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-226 |
8.30e-23 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 102.06 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGRRPAYVVVMDALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLANL--EEAVAEMPstalsGTTGLGHTRWA 78
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVfdESKLDQLP-----GDIAIGHVRYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 79 THGRPTDRNAHPHRDAA--GKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARayrhgETADDFVGSVLAV 156
Cdd:PLN02440 76 TAGASSLKNVQPFVANYrfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAI-----SKARPFFSRIVDA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489513448 157 LRRLEGHFTLVFANADdpgTLVAARRS---TPLVLGIGDNEMFV-GSDVAAF--IEHTREAvELGQDQAVVITADG 226
Cdd:PLN02440 151 CEKLKGAYSMVFLTED---KLVAVRDPhgfRPLVMGRRSNGAVVfASETCALdlIGATYER-EVNPGEVIVVDKDK 222
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-204 |
1.87e-21 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 97.80 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 2 CGIVGYVGRRPAYVVVMD--ALRRMEYRGYDSSGIALVDGGTLTVRRRAGRLAnleEAVAEMPSTALSGTTGLGHTRWAT 79
Cdd:PRK05793 15 CGVFGVFSKNNIDVASLTyyGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVS---EVFSKEKLKGLKGNSAIGHVRYST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 80 HGRPTDRNAHP--HRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHGetaddFVGSVLAVL 157
Cdd:PRK05793 92 TGASDLDNAQPlvANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKG-----LEKALVDAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489513448 158 RRLEGHFTLVFANADdpgTLVAARRST---PLVLGIGDNEMFVGSDVAAF 204
Cdd:PRK05793 167 QAIKGSYALVILTED---KLIGVRDPHgirPLCLGKLGDDYILSSESCAL 213
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-203 |
2.26e-21 |
|
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: 93.87 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 2 CGIVGYVGRRPAYVV---VMDALRRMEYRG-YDSSGIALVDGGTLTVRRRAGRLANLE-----EAVAEMPST-ALSGTTG 71
Cdd:cd01907 1 CGIFGIMSKDGEPFVgalLVEMLDAMQERGpGDGAGFALYGDPDAFVYSSGKDMEVFKgvgypEDIARRYDLeEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 72 LGHTRWATHGRPTDRNAHPHrdAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAYRHGETADDFVG 151
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPF--SIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYYK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489513448 152 SVLAVLR----------------RLEGHFTLVFANADDPGTLVAARRSTPLVLGIGDNEMFVGSDVAA 203
Cdd:cd01907 159 HIIRMPEeerelllalrltyrlaDLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECA 226
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-228 |
4.23e-20 |
|
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: 89.15 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 2 CGIVGYVGRRPAYV---VVMDALRRMEYRGYDSSGIALVDGgtltvrrragrlanleeavaempstalsgtTGLGHTRWA 78
Cdd:cd00712 1 CGIAGIIGLDGASVdraTLERMLDALAHRGPDGSGIWIDEG------------------------------VALGHRRLS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 79 ThgRPTDRNAHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHlvarAY-RHGETAddfvgsvlavL 157
Cdd:cd00712 51 I--IDLSGGAQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILH----LYeEWGEDC----------L 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489513448 158 RRLEGhftlVFANA---DDPGTLVAAR-RS--TPLVLGIGDNEMFVGSDVAAFIEHTREAVELGQDQAVVITADGYR 228
Cdd:cd00712 115 ERLNG----MFAFAlwdKRKRRLFLARdRFgiKPLYYGRDGGGLAFASELKALLALPGVPRELDEAALAEYLAFQYV 187
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
67-200 |
5.26e-20 |
|
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: 86.21 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 67 SGTTGLGHTRWATHGRPTDRNaHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVArayRHGEta 146
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYE---EWGE-- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489513448 147 ddfvgsvlAVLRRLEGHFTLVFANAdDPGTLVAARRST---PLVLGIGDNEMFVGSD 200
Cdd:pfam13522 83 --------DCLERLRGMFAFAIWDR-RRRTLFLARDRLgikPLYYGILGGGFVFASE 130
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
473-604 |
8.08e-20 |
|
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: 85.81 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 473 FAQSSTVLFLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEDGLPVIVVMPSPKGSATLHAkllsnIREI 552
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAA-----AELA 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489513448 553 QTRGAVTIVIAEEGDETVRPYADHLIEIPAVSTLLQPLLSTIPLQVFAASVA 604
Cdd:pfam01380 77 KARGAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDAL 128
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
307-426 |
1.34e-18 |
|
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: 81.85 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 307 VFVVACGTAYHSGLLAKYAIEHWTRLPVEVELASEFRYRDPV-LDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAIC 385
Cdd:cd05710 2 VFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489513448 386 NTNGSQIPRECDAVLYTraGPEIGVASTKTFLAQIAANYLL 426
Cdd:cd05710 82 DDEDSPLAKLADYVIVY--GFEIDAVEEKYLLLYMLALRLL 120
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-207 |
5.11e-17 |
|
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: 84.50 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGRRPAY--VVVMDALRRMEYRGYDSSGIaLVDGGTltvrrragrlanleeavaempstalsgttGLGHTRWA 78
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGI-WVDGGV-----------------------------ALGHRRLS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 79 ThgrpTDRNAH---PHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHlvarAYRH-GEtaddfvgsvl 154
Cdd:COG0367 51 I----IDLSEGghqPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILH----AYEEwGE---------- 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489513448 155 AVLRRLEGHFTLVFANADDpGTLVAAR-R--STPLVLGIGDNEMFVGSDVAAFIEH 207
Cdd:COG0367 113 DCLERLNGMFAFAIWDRRE-RRLFLARdRfgIKPLYYAEDGGGLAFASELKALLAH 167
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
301-426 |
5.66e-15 |
|
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: 72.26 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 301 LREIDKVFVVACGtayHSGLLAKYAIEHWTRLPVEVELAS---EFRYRDPVLDRSTLVVAISQSGETADTLEAVRHAKEQ 377
Cdd:cd05013 10 LAKARRIYIFGVG---SSGLVAEYLAYKLLRLGKPVVLLSdphLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489513448 378 KAKVLAICNTNGSQIPRECDAVLYTRAgpEIGVASTKTFLAQIAANYLL 426
Cdd:cd05013 87 GAKVIAITDSANSPLAKLADIVLLVSS--EEGDFRSSAFSSRIAQLALI 133
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
74-204 |
9.15e-15 |
|
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: 71.01 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 74 HTRWATHGRPTDrnAHP-HRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVarAYRHGEtaddfvgs 152
Cdd:pfam13537 1 HRRLSIIDLEGG--AQPmVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLY--EAEWGE-------- 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489513448 153 vlAVLRRLEGHFTLVFANADDpGTLVAAR-RS--TPLVLGIGDNEMFV-GSDVAAF 204
Cdd:pfam13537 69 --DCVDRLNGMFAFAIWDRRR-QRLFLARdRFgiKPLYYGRDDGGRLLfASELKAL 121
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
291-444 |
1.92e-14 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 74.19 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 291 LDEQRLSD--QELREIDKVFVVACGTayhSGLLAKYAIEHWTRLPVEVEL----ASEFRYRDPVLDRSTLVVAISQSGET 364
Cdd:COG1737 119 LDEEALERavDLLAKARRIYIFGVGA---SAPVAEDLAYKLLRLGKNVVLldgdGHLQAESAALLGPGDVVIAISFSGYT 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 365 ADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRA-GPEIGVASTKTFLAQIAANYLLGLALAQARGTKYPDEVE 443
Cdd:COG1737 196 RETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSeEPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLE 275
|
.
gi 489513448 444 R 444
Cdd:COG1737 276 R 276
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-222 |
2.48e-11 |
|
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: 64.33 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGR---------RPAYVVVMDALRRMEYRGY---DSSGIALVD--GGTLTVRRR---AGRLANLEEAvaempS 63
Cdd:cd01908 1 MCRLLGYSGApipleplliRPSHSLLVQSGGPREMKGTvhaDGWGIGWYEgkGGRPFRYRSplpAWSDINLESL-----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 64 TALSGTTGLGHTRWATHGRPTDRNAHPHRdaAGKIAVVHNGIIENFAVLRRELETAGVEF-ASDTDTEVAAHLVAR--AY 140
Cdd:cd01908 76 RPIKSPLVLAHVRAATVGPVSLENCHPFT--RGRWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFALLLSrlLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 141 RHGETADDFVGSVLAVLRRLE-----GHFTLVFANADdpgTLVAARRSTPlvlgigdNEMFVGSDVAAFIE--HTREAVE 213
Cdd:cd01908 154 RDPLDPAELLDAILQTLRELAalappGRLNLLLSDGE---YLIATRYASA-------PSLYYLTRRAPFGCarLLFRSVT 223
|
....*....
gi 489513448 214 LGQDQAVVI 222
Cdd:cd01908 224 TPNDDGVVV 232
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-207 |
1.16e-10 |
|
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: 64.28 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 4 IVGYVGRRPAYVVVMDALRRM----EYRGYDSSGIALVDGGTltvrrragrlanleeavaempstalsgttGLGHTRWAT 79
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMsdtiAHRGPDASGIEYKDGNA-----------------------------ILGHRRLAI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 80 hgrpTDRN--AHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHlvarAYR-HGETAddfvgsvlav 156
Cdd:TIGR01536 52 ----IDLSggAQPMSNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILH----LYEeWGEEC---------- 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489513448 157 LRRLEGHFTLVFANADDpGTLVAARRS---TPLVLGIGDNEMFVGSDVAAFIEH 207
Cdd:TIGR01536 114 VDRLDGMFAFALWDSEK-GELFLARDRfgiKPLYYAYDGGQLYFASEIKALLAH 166
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
354-431 |
1.13e-07 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 51.00 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 354 LVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRAGPE---IGVASTKTFLAQIAanylLGLAL 430
Cdd:cd05014 50 VVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEacpLGLAPTTSTTAMLA----LGDAL 125
|
.
gi 489513448 431 A 431
Cdd:cd05014 126 A 126
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
307-385 |
1.38e-07 |
|
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: 49.29 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 307 VFVVACGTAYHSGLLAKYAIEHWTRLPVEVELASEFRYRDPV--LDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAI 384
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLslLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 489513448 385 C 385
Cdd:cd04795 81 T 81
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
299-384 |
2.10e-07 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 53.06 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 299 QELREIDKVFVVACGTAYHSG-LLAKYAIEHWtrlPVEVelaseFRYRD----PVLDRSTLVVAISQSGETADTLEAVRH 373
Cdd:PRK08674 29 EDLEKIDNIVISGMGGSGIGGdLLRILLFDEL---KVPV-----FVNRDytlpAFVDEKTLVIAVSYSGNTEETLSAVEQ 100
|
90
....*....|.
gi 489513448 374 AKEQKAKVLAI 384
Cdd:PRK08674 101 ALKRGAKIIAI 111
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-181 |
2.60e-07 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 53.76 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGR-------RPayvVVMDALRRMEYRGYDSSGIALVDGGTLtvrrragrlanleeavaempstalsgttglG 73
Cdd:PRK09431 1 MCGIFGILDIktdadelRK---KALEMSRLMRHRGPDWSGIYASDNAIL------------------------------G 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 74 HTRWA----THGrptdrnAHPHRDAAGKIAVVHNGIIENFAVLRRELETaGVEFASDTDTEVAAHLvaraYRhgETADDF 149
Cdd:PRK09431 48 HERLSivdvNGG------AQPLYNEDGTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILAL----YQ--EKGPDF 114
|
170 180 190
....*....|....*....|....*....|..
gi 489513448 150 vgsvlavLRRLEGHFTLVFANADDpGTLVAAR 181
Cdd:PRK09431 115 -------LDDLDGMFAFALYDSEK-DAYLIAR 138
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
344-404 |
1.25e-06 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 50.53 E-value: 1.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489513448 344 YRDP--------VLDRSTLVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRA 404
Cdd:PRK11337 172 YDDAhimlmsaaLLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTA 240
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
302-562 |
1.63e-06 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 50.39 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 302 REIDKVFVVACGTAYHSGLLAKYAIEHWTRLPVEVELASEFRYRDPV-LDRSTLVVAISQSGETADTLEAVRHAKEQKAK 380
Cdd:PRK11382 42 RDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYrLDDRCAVIGVSDYGKTEEVIKALELGRACGAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 381 VLAICNTNGSQIPR--------ECDAV--------------LYTRAGPEIGVASTKTFLAQiaanyllglaLAQARG--T 436
Cdd:PRK11382 122 TAAFTKRADSPITSaaefsidyQADCIweihlllcysvvleMITRLAPNAEIGKIKNDLKQ----------LPNALGhlV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 437 KYPDEVEREYHELEAMPDLVARViaATGPVAELAHRfaqsstvlflgrhvgypvalEGALKLKELAYMHAEGFAAGELKH 516
Cdd:PRK11382 192 RTWEEKGRQLGELASQWPMIYTV--AAGPLRPLGYK--------------------EGIVTLMEFTWTHGCVIESGEFRH 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489513448 517 GPIALIEDGLPVIVVMPSPKGSATLHAKllsnIREIQTRGAVTIVI 562
Cdd:PRK11382 250 GPLEIVEPGVPFLFLLGNDESRHTTERA----INFVKQRTDNVIVI 291
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
306-385 |
2.34e-06 |
|
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: 46.87 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 306 KVFVVACGTAYHSGLLAKYAIEHWTRLPVevelaseFRYRDPVL----DRSTLVVAISQSGETADTLEAVRHAKEQKAKV 381
Cdd:cd05017 1 NIVILGMGGSGIGGDLLESLLLDEAKIPV-------YVVKDYTLpafvDRKTLVIAVSYSGNTEETLSAVEQAKERGAKI 73
|
....
gi 489513448 382 LAIC 385
Cdd:cd05017 74 VAIT 77
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-203 |
2.34e-06 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 50.48 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGIVGYVGRRPAYVVVMD-AL---RRMEYRGYDSSGIALVDGGTLTvrrragrlanleeavaempstalsgTTGLGHTR 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRkALelsKRLRHRGPDWSGIIVLENSPGT-------------------------YNILAHER 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 77 WATHGRPTDRnaHPHRDAAGKIAVVHNGIIENFAVLRRELETAGVEFASDTDTEVAAHLVARAyrhgeTADDFVGsvlav 156
Cdd:PTZ00077 56 LAIVDLSDGK--QPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEY-----GPKDFWN----- 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489513448 157 lrRLEGHFTLVFANADDpGTLVAARRS---TPLVLGIG-DNEMFVGSDVAA 203
Cdd:PTZ00077 124 --HLDGMFATVIYDMKT-NTFFAARDHigiIPLYIGYAkDGSIWFSSELKA 171
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-203 |
4.92e-06 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 49.38 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 1 MCGI---VGYVGRRPAYVVVMDAL-RRMEYRGYDSSGIALvdggtltvrrragrlanleeavaempstalSGTTGLGHTR 76
Cdd:PLN02549 1 MCGIlavLGCSDDSQAKRSRVLELsRRLRHRGPDWSGLYG------------------------------NEDCYLAHER 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 77 WATHGrPTDRNaHPHRDAAGKIAVVHNGIIENFAVLRRELETagVEFASDTDTEVAAHLVArayRHGEtadDFVgsvlav 156
Cdd:PLN02549 51 LAIMD-PESGD-QPLYNEDKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYE---EHGE---EFV------ 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489513448 157 lRRLEGHFTLVFANADDpGTLVAARRS---TPLVLGIG-DNEMFVGSDVAA 203
Cdd:PLN02549 115 -DMLDGMFSFVLLDTRD-NSFIAARDHigiTPLYIGWGlDGSVWFASEMKA 163
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
354-413 |
2.50e-05 |
|
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: 46.36 E-value: 2.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 354 LVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRAGPEIGVAST 413
Cdd:cd05007 121 VVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGST 180
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
354-435 |
4.13e-05 |
|
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: 46.12 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 354 LVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRAGPE---IGVASTKTFLAQIAanylLGLAL 430
Cdd:COG0794 94 VVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREacpLNLAPTTSTTATLA----LGDAL 169
|
....*....
gi 489513448 431 A----QARG 435
Cdd:COG0794 170 AvallEARG 178
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
355-413 |
6.85e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 45.16 E-value: 6.85e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489513448 355 VVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLYTRAGPEIGVAST 413
Cdd:PRK05441 135 VVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGST 193
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
354-401 |
7.06e-05 |
|
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: 43.72 E-value: 7.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489513448 354 LVVAISQSGETADTLEAVRHAKEQKAKVLAICNTNGSQIPRECDAVLY 401
Cdd:cd05005 78 LLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
488-564 |
1.18e-03 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 38.12 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489513448 488 YPVALEGALKLKELAYMHAEGFAAGELKHGP-IALIEDGLPVIVVMPSPKGSATLHAkllsnIREIQTRGAVTIVIAE 564
Cdd:cd04795 10 GAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGRTEELLAA-----LEIAKELGIPVIAITD 82
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
74-186 |
6.55e-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: 38.85 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513448 74 HTRWATHGRPTDRNAHPH-RDAAGK-IAVVHNGIIENFA-VLRRELETAGvefasDTDTEVA-AHL---VARAYRHGETA 146
Cdd:pfam13230 77 HIRKATQGRVTLENTHPFmRELWGRyWIFAHNGDLKGYApKLSGRFQPVG-----STDSELAfCWLldrLASRFPYARPS 151
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489513448 147 DDFVGSVLAVL-RRLEGH--FTLVFANADDpgtLVaARRSTPL 186
Cdd:pfam13230 152 AGELFRALRELaREIAAHgtFNFLLSDGRD---LF-AHCSTRL 190
|
|
| |
