|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-645 |
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: 900.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPKEILLAGLSRLEYRGYDSAGIALY-AHPFTVVKAVGKLEELKKKVEASkefELPYSMGIGHTRWATH 79
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLdDGGLEVRKAVGKLANLEEKLAEE---PLSGTIGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 80 GKASEKNAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRKEKDILKALFSVQKELKGS 159
Cdd:COG0449 78 GAPSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 160 FAFAIMFLEDANTLYAMRKDSPLIVGKGKNAFYLASDVSAFLDYTKKIYPVENREILSLSEKEIHIYNQNGEEVKRSSTI 239
Cdd:COG0449 158 YALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 240 AELSQSQIHKGDYLHFMEKEIFEQPKVVKDTLlyackqengkqlengkpeeyatpgakqfsSARKDPENAENPDfsyeAF 319
Cdd:COG0449 238 VDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTL-----------------------------RGRLDEDGRVVLD----EL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 320 SMAEKDFQDISRVRVIACGSAYHAGWVLKSVCESLARVPVQVELASEFRYNHPILENGELVLSISQSGETADTLAAVKEA 399
Cdd:COG0449 285 NLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 400 KKLGAKTLSIVNVKGSAIAKESDFVFYTQAGPEIAVATTKAYSCQLVAGYIFSLLLAKAKGKISREEASNLTEELFLLPG 479
Cdd:COG0449 365 KEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 480 KVQQCLSMDQEILPMAKELKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQ 559
Cdd:COG0449 445 KIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 560 EELAGKSISNIHEVRSRGAKCFAIKTEDIAIEEEDFAGSLSVAKTHPLFAGSLLVLPLQFLAYRVSLLKGFDPDKPRNLA 639
Cdd:COG0449 525 DELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLA 604
|
....*.
gi 496992313 640 KSVTVE 645
Cdd:COG0449 605 KSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-645 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 835.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPKEILLAGLSRLEYRGYDSAGIALY-AHPFTVVKAVGKLEELKKKVEaskEFELPYSMGIGHTRWATH 79
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLdDGGLEVRKAVGKVANLEAKLE---EEPLPGTTGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 80 GKASEKNAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRKEKDILKALFSVQKELKGS 159
Cdd:PRK00331 78 GKPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 160 FAFAIMFLEDANTLYAMRKDSPLIVGKGKNAFYLASDVSAFLDYTKKIYPVENREILSLSEKEIHIYNQNGEEVKRSSTI 239
Cdd:PRK00331 158 YALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 240 AELSQSQIHKGDYLHFMEKEIFEQPKVVKDTLLyackqenGKQLENGKPEEyatpgakqfssarkdpenaenpdfsyeaf 319
Cdd:PRK00331 238 VDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLE-------GRLDELGEGEL----------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 320 smAEKDFQDISRVRVIACGSAYHAGWVLKSVCESLARVPVQVELASEFRYNHPILENGELVLSISQSGETADTLAAVKEA 399
Cdd:PRK00331 282 --ADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 400 KKLGAKTLSIVNVKGSAIAKESDFVFYTQAGPEIAVATTKAYSCQLVAGYIFSLLLAKAKGKISREEASNLTEELFLLPG 479
Cdd:PRK00331 360 KELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 480 KVQQCLSMDQEILPMAKELKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQ 559
Cdd:PRK00331 440 LIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 560 EELAGKSISNIHEVRSRGAKCFAIKTE-DIAIEEEDFAgsLSVAKTHPLFAGSLLVLPLQFLAYRVSLLKGFDPDKPRNL 638
Cdd:PRK00331 520 DELYEKTKSNIQEVKARGARVIVIADEgDEVAEEADDV--IEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNL 597
|
....*..
gi 496992313 639 AKSVTVE 645
Cdd:PRK00331 598 AKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-645 |
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: 736.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 2 CGIVGFVGQGNPKEILLAGLSRLEYRGYDSAGIA-LYAHPFTVVKAVGKLEELKKKVeasKEFELPYSMGIGHTRWATHG 80
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAvVDEGKLFVRKAVGKVAELANKL---GEKPLPGGVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 81 KASEKNAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRKEKDILKALFSVQKELKGSF 160
Cdd:TIGR01135 78 KPTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 161 AFAIMFLEDANTLYAMRKDSPLIVGKGKNAFYLASDVSAFLDYTKKIYPVENREILSLSEKEIHIYNQNGEEVKRSSTIA 240
Cdd:TIGR01135 158 ALAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 241 ELSQSQIHKGDYLHFMEKEIFEQPKVVKDTLLYACKqENGKQLENGKPEEyatpgakqfssarkdpenaenpdfsyeafs 320
Cdd:TIGR01135 238 DWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIE-ENGGVFEELGAEE------------------------------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 321 maekDFQDISRVRVIACGSAYHAGWVLKSVCESLARVPVQVELASEFRYNHPILENGELVLSISQSGETADTLAAVKEAK 400
Cdd:TIGR01135 287 ----LLKNIDRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 401 KLGAKTLSIVNVKGSAIAKESDFVFYTQAGPEIAVATTKAYSCQLVAGYIFSLLLAKAKGKISREEASNLTEELFLLPGK 480
Cdd:TIGR01135 363 ELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 481 VQQCLSMDQEILPMAKELKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQE 560
Cdd:TIGR01135 443 VEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKD 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 561 ELAGKSISNIHEVRSRGAKCFAIKTEDIAIEEEDFAGSLSVAKTHPLFAGSLLVLPLQFLAYRVSLLKGFDPDKPRNLAK 640
Cdd:TIGR01135 523 SLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAK 602
|
....*
gi 496992313 641 SVTVE 645
Cdd:TIGR01135 603 SVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-644 |
2.44e-151 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 451.78 E-value: 2.44e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPKEILLAGLSRLEYRGYDSAGIAL-----------YAHPFTVVKAVgklEELKKKVEASkefELPYSM 69
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTissggelkttkYASDGTTSDSI---EILKEKLLDS---HKNSTI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 70 GIGHTRWATHGKASEKNAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRKEKDILKAL 149
Cdd:PTZ00295 98 GIAHTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 150 FSVQKELKGSFAFAIMFLEDANTLYAMRKDSPLIVGKGKNAFYLASDVSAFLDYTKKIYPVENREILSLSEKEIHIYNQN 229
Cdd:PTZ00295 178 KSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 230 GEEVKRSSTIAELSQSQihkgdYLHFMEKEIFEQPKVVKDTLLYackqengkqlengkpeeyatpGAKqFSSARKDPEna 309
Cdd:PTZ00295 258 RRVEKIPEEVIEKSPEP-----YPHWTLKEIFEQPIALSRALNN---------------------GGR-LSGYNNRVK-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 310 enpdfsYEAFSMAEKDFQDISRVRVIACGSAYHAGWVLKSVCESLARV-PVQVELASEF-RYNHPILENGelVLSISQSG 387
Cdd:PTZ00295 309 ------LGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVIDASELtLYRLPDEDAG--VIFISQSG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 388 ETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFVFYTQAGPEIAVATTKAYSCQLVAGYIFSLLLAKAKGKISREE- 466
Cdd:PTZ00295 381 ETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYk 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 467 ASNLTEELFLLPGKVQQCLSMDQEIL-PMAKELKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTIS 545
Cdd:PTZ00295 461 CSSLINSLHRLPTYIGMTLKSCEEQCkRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 546 LI--EKDSPVIGLLSQEELAGKSISNIHEVRSRGAkcFAIKTEDIAIEEEDFAGSLSVAKTHPLFAGSLLVLPLQFLAYR 623
Cdd:PTZ00295 541 LIdkEKNTPVILIILDDEHKELMINAAEQVKARGA--YIIVITDDEDLVKDFADEIILIPSNGPLTALLAVIPLQLLAYE 618
|
650 660
....*....|....*....|.
gi 496992313 624 VSLLKGFDPDKPRNLAKSVTV 644
Cdd:PTZ00295 619 IAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-645 |
7.88e-144 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 433.79 E-value: 7.88e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPK------EILLAGLSRLEYRGYDSAGIALYAHPFT------VVKAVGKLEELKKKVE---ASKEFEL 65
Cdd:PLN02981 1 MCGIFAYLNYNVPRerrfilEVLFNGLRRLEYRGYDSAGIAIDNDPSLesssplVFREEGKIESLVRSVYeevAETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 66 PYSM----GIGHTRWATHGKASEKNAHPHLS-MHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYR 140
Cdd:PLN02981 81 DLVFenhaGIAHTRWATHGPPAPRNSHPQSSgPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 141 K----EKDIL--KALFSVQKELKGSFAFAIMFLEDANTLYAMRKDSPLIVG----------------------KGKNA-- 190
Cdd:PLN02981 161 KlneeEGDVTfsQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkelpeeknssavftsegfltkNRDKPke 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 191 FYLASDVSAFLDYTKKIYPVENREILSLSEKEIHIYNQNGE------------EVKRSSTIAELSQSQIHKGDYLHFMEK 258
Cdd:PLN02981 241 FFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEkgrgggglsrpaSVERALSTLEMEVEQIMKGNYDHYMQK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 259 EIFEQPKVVKDTL---LYACKQENGKQLENGKPEEYatpgakqFSSARKDpenaenpdfsyeafsmaekdfqdiSRVRVI 335
Cdd:PLN02981 321 EIHEQPESLTTTMrgrLIRGGSGKAKRVLLGGLKDH-------LKTIRRS------------------------RRIVFI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 336 ACGSAYHAGWVLKSVCESLARVPVQVELASEFRYNH-PILENGELVLsISQSGETADTLAAVKEAKKLGAKTLSIVNVKG 414
Cdd:PLN02981 370 GCGTSYNAALAARPILEELSGVPVTMELASDLLDRQgPIYREDTAVF-VSQSGETADTLRALEYAKENGALCVGITNTVG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 415 SAIAKESDFVFYTQAGPEIAVATTKAYSCQLVAGYIFSLLLAK-AKGKISREEAsnLTEELFLLPGKVQQCLSMDQEILP 493
Cdd:PLN02981 449 SAISRGTHCGVHINAGAEIGVASTKAYTSQIVAMTMLALALGEdSISSRSRREA--IIDGLFDLPNKVREVLKLDQEMKE 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 494 MAKELKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQEELAGKSISNIHEV 573
Cdd:PLN02981 527 LAELLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQL 606
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496992313 574 RSRGAKCFAI--KTEDIAIEEEDFAGSLSVAKTHPLFAGSLLVLPLQFLAYRVSLLKGFDPDKPRNLAKSVTVE 645
Cdd:PLN02981 607 RARKGRLIVIcsKGDASSVCPSGGCRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-645 |
2.18e-133 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 406.57 E-value: 2.18e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPK------EILLAGLSRLEYRGYDSAGIALYAHPFT----------------VVKAVGKLEELKKKVE 58
Cdd:PTZ00394 1 MCGIFGYANHNVPRtveqilNVLLDGIQKVEYRGYDSAGLAIDANIGSekedgtaasaptprpcVVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 59 ASK--------EFELPYSMGIGHTRWATHGKASEKNAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEV 130
Cdd:PTZ00394 81 SEAvaatlppmDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 131 AVNLMEYYYRKEK--DILKALFSVQKELKGSFAFAIMFLEDANTLYAMRKDSPLIVG---------------------KG 187
Cdd:PTZ00394 161 ISVLSEYLYTRKGihNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGirrtddrgcvmklqtydltdlSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 188 KNAFYLASDVSAFLDYTKKIYPVENREILSLSEKEIHIYNQNGEE---VKRSSTIAELSQSQIHKGDYLHFMEKEIFEQP 264
Cdd:PTZ00394 241 PLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 265 KVVKDTLlyackqeNGKQlengkpeeyatpgakqfssarkdpenaenpDFSYEAFSMAEKDFQDIS------RVRVIACG 338
Cdd:PTZ00394 321 ESVISSM-------HGRI------------------------------DFSSGTVQLSGFTQQSIRailtsrRILFIACG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 339 SAYHAGWVLKSVCESLARVPVQVELASEFRYNHPILENGELVLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIA 418
Cdd:PTZ00394 364 TSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSIS 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 419 KESDFVFYTQAGPEIAVATTKAYSCQLVAGYIFSLLLAKAKGKIsREEASNLTEELFLLPGKVQQCLSMDQE-ILPMAKE 497
Cdd:PTZ00394 444 RLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRL-QERRNEIIRGLAELPAAISECLKITHDpVKALAAR 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 498 LKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQEELAGKSISNIHEVRSRG 577
Cdd:PTZ00394 523 LKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARG 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496992313 578 AKCFAIKTEDIAIEEEDFAGSLSVAKTHPLFAGSLLVLPLQFLAYRVSLLKGFDPDKPRNLAKSVTVE 645
Cdd:PTZ00394 603 GAVVVFATEVDAELKAAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
4.02e-108 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 325.17 E-value: 4.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 2 CGIVGFVGQGNPKEILLAGLSRLEYRGYDSAGIALYA-HPFTVVKAVGKLEELKKKVeasKEFELPYSMGIGHTRWATHG 80
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGdGSLEVVKAVGKVANLEEKL---AEKPLSGHVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 81 KASEKNAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRKEKDILKALFSVQKELKGSF 160
Cdd:cd00714 78 EPTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496992313 161 AFAIMFLEDANTLYAMRKDSPLIVGKGKNAFYLASDVSAFLDYTKKIYPVENREI 215
Cdd:cd00714 158 ALAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDI 212
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
331-645 |
3.95e-79 |
|
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: 254.44 E-value: 3.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 331 RVRVIACGSAYHAGWVLKSVCESLARVPVQVELASEF-RYNHPILENGELVLSISQSGETADTLAAVKEAKKLGAKTLSI 409
Cdd:COG2222 36 RVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVYPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 410 VNVKGSAIAKESDFVFYTQAGPEIAVATTKAYSCQLVAGYifsLLLAKAKGkisreeASNLTEELFLLPGKVQQCLSMDQ 489
Cdd:COG2222 116 TNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALL---ALLAAWGG------DDALLAALDALPAALEAALAADW 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 490 EILPMAkELKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQEELAGKSISN 569
Cdd:COG2222 187 PAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDL 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496992313 570 IHEVRSRGAKCFAIKTEDIAIEEEDFAGSLsvaktHPLFAGSLLVLPLQFLAYRVSLLKGFDPDKPRNLAKSVTVE 645
Cdd:COG2222 266 AAELRALGARVVAIGAEDDAAITLPAIPDL-----HDALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-216 |
7.86e-61 |
|
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: 202.29 E-value: 7.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 2 CGIVGFVGQGNPKEILL----AGLSRLEYRGYDSAGIALYA-HPFTVVKAVGKLEELKKKVEASkefELPYSMGIGHTRW 76
Cdd:cd00352 1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYDgDGLFVEKRAGPVSDVALDLLDE---PLKSGVALGHVRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 77 ATHGKASEKNAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRkEKDILKALFSVQKEL 156
Cdd:cd00352 78 ATNGLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGR-EGGLFEAVEDALKRL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496992313 157 KGSFAFAIMFlEDANTLYAMRK---DSPLIVGKGK-NAFYLASDVSAFLDYT-KKIYPVENREIL 216
Cdd:cd00352 157 DGPFAFALWD-GKPDRLFAARDrfgIRPLYYGITKdGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
331-456 |
5.93e-59 |
|
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: 193.48 E-value: 5.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 331 RVRVIACGSAYHAGWVLKSVCESLARVPVQVELASEFRYNHPILENGELVLSISQSGETADTLAAVKEAKKLGAKTLSIV 410
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 496992313 411 NVKGSAIAKESDFVFYTQAGPEIAVATTKAYSCQLVAGYIFSLLLA 456
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
489-643 |
1.39e-58 |
|
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: 193.63 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 489 QEILPMAKELKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQEELAGKSIS 568
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496992313 569 NIHEVRSRGAKCFAIKTEDIAIEEEDFagSLSVAKTHPLFAGSLLVLPLQFLAYRVSLLKGFDPDKPRNLAKSVT 643
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAKDLADV--VIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-236 |
2.30e-37 |
|
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: 145.17 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPKEILLAGLSRLEYRGYDSAGIALY-AHPFTVVKAVG------KLEELKKkveaskefeLPYSMGIGH 73
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSdGGRFHLHKGMGlvsdvfDEEDLER---------LKGNIAIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 74 TRWATHGKASEKNAHPHL--SMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRKEkDILKALFS 151
Cdd:COG0034 78 VRYSTTGSSSLENAQPFYvnSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKE-DLEEAIKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 152 VQKELKGSFAFAIMfleDANTLYAMRkDS----PLIVGKGKNAFYLASDVSAF--LDYtKKIYPVENREILSLSEKEIHI 225
Cdd:COG0034 157 ALRRVKGAYSLVIL---TGDGLIAAR-DPngirPLVLGKLEDGYVVASESCALdiLGA-EFVRDVEPGEIVVIDEDGLRS 231
|
250
....*....|.
gi 496992313 226 YnQNGEEVKRS 236
Cdd:COG0034 232 R-QFAEKPRPA 241
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-200 |
4.07e-34 |
|
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: 130.27 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 2 CGIVGFVGQGNPKEILLAGLSRLEYRGYDSAGIALYAHP-FTVVKAVG------KLEELKKkveaskefeLPYSMGIGHT 74
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKrFHTHKGMGlvsdvfDEEKLRR---------LPGNIAIGHV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 75 RWATHGKASEKNAHPHL--SMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEyYYRKEKDILKALFSV 152
Cdd:cd00715 72 RYSTAGSSSLENAQPFVvnSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA-RSLAKDDLFEAIIDA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496992313 153 QKELKGSFAFAIMFledANTLYAMRkDS----PLIVGK-GKNAFYLASDVSAF 200
Cdd:cd00715 151 LERVKGAYSLVIMT---ADGLIAVR-DPhgirPLVLGKlEGDGYVVASESCAL 199
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-200 |
5.72e-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: 126.28 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 2 CGIVGFVGQGNP-KEILLAGLSRLEYRGYDSAGIALYA-HPFTVVKAVGKLEELkkkVEASKEFELPYSMGIGHTRWATH 79
Cdd:TIGR01134 1 CGVVGIYGQEEVaASLTYYGLYALQHRGQESAGISVFDgNRFRLHKGNGLVSDV---FNEEHLQRLKGNVGIGHVRYSTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 80 GKASEKNAHPHL--SMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRKEKDILKALFSVQKELK 157
Cdd:TIGR01134 78 GSSGLENAQPFVvnSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496992313 158 GSFAFAIMFLEDantLYAMRkDS----PLIVGKGKNAFYLASDVSAF 200
Cdd:TIGR01134 158 GAYALVLMTEDG---LVAVR-DPhgirPLVLGRRGDGYVVASESCAL 200
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
326-451 |
1.16e-26 |
|
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: 105.46 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 326 FQDISRVRVIACGSAYHAGWVLKSVCESLARVPVQVELASEFRYNH-PILENGELVLSISQSGETADTLAAVKEAKKLGA 404
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 496992313 405 KTLSIVNVKGSAIAKESDFVFYTQAGPEIAVATTKAYSCQLVAGYIF 451
Cdd:pfam01380 82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDAL 128
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-241 |
1.25e-25 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 110.51 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 2 CGIVGFVGQGNPK--EILLAGLSRLEYRGYDSAGIALY-AHPFTVVKAVGKLEELKKKvEASKEFElpYSMGIGHTRWAT 78
Cdd:PRK05793 15 CGVFGVFSKNNIDvaSLTYYGLYALQHRGQESAGIAVSdGEKIKVHKGMGLVSEVFSK-EKLKGLK--GNSAIGHVRYST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 79 HGKASEKNAHPHLSMHK--EVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRkeKDILKALFSVQKEL 156
Cdd:PRK05793 92 TGASDLDNAQPLVANYKlgSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK--KGLEKALVDAIQAI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 157 KGSFAFAIMFledANTLYAMRKDS---PLIVGKGKNAFYLASDvSAFLDY--TKKIYPVENREILSLSEKEIHIYNQNgE 231
Cdd:PRK05793 170 KGSYALVILT---EDKLIGVRDPHgirPLCLGKLGDDYILSSE-SCALDTigAEFIRDVEPGEIVIIDEDGIKSIKFA-E 244
|
250
....*....|
gi 496992313 232 EVKRSSTIAE 241
Cdd:PRK05793 245 KTKCQTCAFE 254
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-211 |
2.53e-25 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 109.77 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPKEILLAGLSRLEYRGYDSAGIALY-AHPFTVVKAVGkleeLKKKV-EASKEFELPYSMGIGHTRWAT 78
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVdGNRLQSITGNG----LVSDVfDESKLDQLPGDIAIGHVRYST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 79 HGKASEKNAHPHL--SMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEyyYRKEKDILKALFSVQKEL 156
Cdd:PLN02440 77 AGASSLKNVQPFVanYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIA--ISKARPFFSRIVDACEKL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496992313 157 KGsfAFAIMFL-EDanTLYAMRKDS---PLIVGKGKN-AFYLASDVSAF----LDYTKKIYPVE 211
Cdd:PLN02440 155 KG--AYSMVFLtED--KLVAVRDPHgfrPLVMGRRSNgAVVFASETCALdligATYEREVNPGE 214
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-226 |
1.70e-23 |
|
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: 100.04 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 2 CGIVGFV---GQGNPKEILLAGLSRLEYRG-YDSAGIALYAHP----------FTVVKAVG---------KLEELKKKve 58
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPdafvyssgkdMEVFKGVGypediarryDLEEYKGY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 59 askefelpysMGIGHTRWATHGKASEKNAHPHLSMHkeVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYY 138
Cdd:cd01907 79 ----------HWIAHTRQPTNSAVWWYGAHPFSIGD--IAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 139 YRKEKDILKALFSVQ----------KELKGSFAFAImfLEDANTLYAMRKDS-----------PLIVGKGKNAFYLASDV 197
Cdd:cd01907 147 LRKGGLPLEYYKHIIrmpeeerellLALRLTYRLAD--LDGPFTIIVGTPDGfivirdriklrPAVVAETDDYVAIASEE 224
|
250 260
....*....|....*....|....*....
gi 496992313 198 SAFldytKKIYPVENREILSLSEKEIHIY 226
Cdd:cd01907 225 CAI----REIPDRDNAKVWEPRPGEYVIW 249
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-202 |
7.48e-19 |
|
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: 85.69 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 2 CGIVGFVGQGNP---KEILLAGLSRLEYRGYDSAGIALYAHpftvvkavgkleelkkkveaskefelpysMGIGHTRWAT 78
Cdd:cd00712 1 CGIAGIIGLDGAsvdRATLERMLDALAHRGPDGSGIWIDEG-----------------------------VALGHRRLSI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 79 HGKASEknAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLmeyyYRKE-KDILkalfsvqKELK 157
Cdd:cd00712 52 IDLSGG--AQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL----YEEWgEDCL-------ERLN 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496992313 158 GSFAFAImFLEDANTLYAMR-----KdsPLIVGKGKNAFYLASDVSAFLD 202
Cdd:cd00712 119 GMFAFAL-WDKRKRRLFLARdrfgiK--PLYYGRDGGGLAFASELKALLA 165
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
97-202 |
1.19e-18 |
|
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: 82.18 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 97 VVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRKEkdilkalfsVQKELKGSFAFAIMFlEDANTLYAM 176
Cdd:pfam13537 24 YVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEWGED---------CVDRLNGMFAFAIWD-RRRQRLFLA 93
|
90 100 110
....*....|....*....|....*....|..
gi 496992313 177 R-----KdsPLIVGKGK-NAFYLASDVSAFLD 202
Cdd:pfam13537 94 RdrfgiK--PLYYGRDDgGRLLFASELKALLA 123
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
497-628 |
3.03e-18 |
|
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: 81.19 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 497 ELKDADNIFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQEELAgKSISNIHEVRSR 576
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETK-DLLAAAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 496992313 577 GAKCFAI-KTEDIAIEEEDFAGSLSVAKTHPLFAgSLLVLPLQFLAYRVSLLK 628
Cdd:pfam01380 80 GAKIIAItDSPGSPLAREADHVLYINAGPETGVA-STKSITAQLAALDALAVA 131
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-201 |
1.21e-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: 86.43 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVG--QGNPKEILLAGLSRLEYRGYDSAGIalYAHPftvvkavgkleelkkkveaskefelpySMGIGHTR--- 75
Cdd:COG0367 1 MCGIAGIIDfdGGADREVLERMLDALAHRGPDGSGI--WVDG---------------------------GVALGHRRlsi 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 76 --WATHGkaseknahpHLSMHKE---VVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLmeyYYRKEKDILkalf 150
Cdd:COG0367 52 idLSEGG---------HQPMVSEdgrYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA---YEEWGEDCL---- 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496992313 151 svqKELKGSFAFAImFLEDANTLYAMR-----KdsPLIVGKGKNAFYLASDVSAFL 201
Cdd:COG0367 116 ---ERLNGMFAFAI-WDRRERRLFLARdrfgiK--PLYYAEDGGGLAFASELKALL 165
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
70-196 |
9.00e-17 |
|
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: 76.96 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 70 GIGHTRWATHGKASEKNaHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYyrkEKDILKAl 149
Cdd:pfam13522 13 ALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEW---GEDCLER- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 496992313 150 fsvqkeLKGSFAFAImFLEDANTLYAMRKD---SPLIVGKGKNAFYLASD 196
Cdd:pfam13522 88 ------LRGMFAFAI-WDRRRRTLFLARDRlgiKPLYYGILGGGFVFASE 130
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
331-450 |
4.07e-15 |
|
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240214 [Multi-domain] Cd Length: 120 Bit Score: 71.84 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 331 RVRVIACGSAYHAGWVLKSVCESLARVPVQVELASEFRY-NHPILENGELVLSISQSGETADTLAAVKEAKKLGAKTLSI 409
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHtGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 496992313 410 VNVKGSAIAKESDFVFYTqaGPEIAVATTKAYSCQLVAGYI 450
Cdd:cd05710 81 TDDEDSPLAKLADYVIVY--GFEIDAVEEKYLLLYMLALRL 119
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
327-636 |
1.25e-11 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 66.56 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 327 QDISRVRVIACGSAYHAGWVLKSVCESLARVPVQVELASEFRYNHPI-LENGELVLSISQSGETADTLAAVKEAKKLGAK 405
Cdd:PRK11382 42 RDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYrLDDRCAVIGVSDYGKTEEVIKALELGRACGAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 406 TLSIVNVKGSAIAKESDFVFYTQAgpeiavatTKAYSCQLVAGYifSLLLAKAKGKISREEASNLTEELFLLPGKVQQCL 485
Cdd:PRK11382 122 TAAFTKRADSPITSAAEFSIDYQA--------DCIWEIHLLLCY--SVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 486 -SMDQEILPMAKELKDADNIFFLGRG-LDWAISMEGALKLKEISYIHCESYSSGELKHGTISLIEKDSPVIGLLSQEELA 563
Cdd:PRK11382 192 rTWEEKGRQLGELASQWPMIYTVAAGpLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESR 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496992313 564 GKSISNIHEVRSRGAKCFAIKTEDIAieeedfagslsvAKTHPLFAGSLLVLPLQFLAYRVSLLKGFDPDKPR 636
Cdd:PRK11382 272 HTTERAINFVKQRTDNVIVIDYAEIS------------QGLHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-209 |
1.53e-11 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 67.24 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPKEIL----LAGLSRLEYRGYDSAGIalyahpFTVVKAVgkleelkkkveaskefelpysmgIGHTRW 76
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGI------YASDNAI-----------------------LGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 77 ATHGKASekNAHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKgYSFYSDTDTEVAVNLmeyYYRKEKDILkalfsvqKEL 156
Cdd:PRK09431 52 SIVDVNG--GAQPLYNEDGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL---YQEKGPDFL-------DDL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496992313 157 KGSFAFAImFLEDANTLYAMRkDS----PLIVGKGKN-AFYLASDVSAFLDYTKKIYP 209
Cdd:PRK09431 119 DGMFAFAL-YDSEKDAYLIAR-DPigiiPLYYGYDEHgNLYFASEMKALVPVCKTIKE 174
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
95-202 |
6.73e-11 |
|
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: 65.05 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 95 KEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYYRkekdilkalFSVQKeLKGSFAFAIMFLEDaNTLY 174
Cdd:TIGR01536 66 KTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEEWGE---------ECVDR-LDGMFAFALWDSEK-GELF 134
|
90 100 110
....*....|....*....|....*....|..
gi 496992313 175 AMRkD----SPLIVGKGKNAFYLASDVSAFLD 202
Cdd:TIGR01536 135 LAR-DrfgiKPLYYAYDGGQLYFASEIKALLA 165
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
374-457 |
2.66e-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: 58.78 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 374 LENGELVLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFVFYTQAGPEIAVATtkAYSCQLVAGYIFSL 453
Cdd:cd05013 58 LTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSS--AFSSRIAQLALIDA 135
|
....
gi 496992313 454 LLAK 457
Cdd:cd05013 136 LFLA 139
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-209 |
1.13e-09 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 61.27 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 1 MCGIVGFVGQGNPKEILLA---GLS-RLEYRGYDSAGIALYahpftvvkavgkleelkkkvEASKEFelpYSMgIGHTRW 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRkalELSkRLRHRGPDWSGIIVL--------------------ENSPGT---YNI-LAHERL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 77 ATHGKASEKnaHPHLSMHKEVVLVHNGIIENFAEIKNFLQEKGYSFYSDTDTEVAVNLMEYYyrKEKDILkalfsvqKEL 156
Cdd:PTZ00077 57 AIVDLSDGK--QPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEY--GPKDFW-------NHL 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496992313 157 KGSFAFaIMFLEDANTLYAMRKD---SPLIVGKGKN-AFYLASDVSAFLD--YTKKIYP 209
Cdd:PTZ00077 126 DGMFAT-VIYDMKTNTFFAARDHigiIPLYIGYAKDgSIWFSSELKALHDqcVEVKQFP 183
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
374-433 |
4.88e-09 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 57.53 E-value: 4.88e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 374 LENGELVLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFVFYTQAGPEI 433
Cdd:cd05007 116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEV 175
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
374-429 |
5.01e-09 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 58.02 E-value: 5.01e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 496992313 374 LENGELVLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFVFYTQA 429
Cdd:COG1737 180 LGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPS 235
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
373-429 |
1.56e-08 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 56.31 E-value: 1.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 496992313 373 ILENGELVLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFVFYTQA 429
Cdd:PRK11337 184 LLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTA 240
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
50-225 |
2.85e-08 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 54.97 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 50 LEELKKKVEASkefelpysMGIGHTRWATHGKASEKNAHPHlsMHKEVVLVHNGIIENFAEIKNFLQEKGYSFY-----S 124
Cdd:COG0121 67 LRLLARPIKSR--------LVIAHVRKATVGPVSLENTHPF--RGGRWLFAHNGQLDGFDRLRRRLAEELPDELyfqpvG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 125 DTDTEVA-VNLMEYYYRKEKDILKALFSVQKELK------GSFAFAIMfleDANTLYAMRKDSPlivGKGKNAFYL---- 193
Cdd:COG0121 137 TTDSELAfALLLSRLRDGGPDPAEALAEALRELAelarapGRLNLLLS---DGERLYATRYTSD---DPYPTLYYLtrtt 210
|
170 180 190
....*....|....*....|....*....|....*...
gi 496992313 194 ASDVSAF-----LDYTKKIYPVENREILSLSE-KEIHI 225
Cdd:COG0121 211 PDDRVVVvasepLTDDEGWTEVPPGELLVVRDgLEVEV 248
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
380-433 |
1.53e-07 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 53.63 E-value: 1.53e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 496992313 380 VLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFVFYTQAGPEI 433
Cdd:PRK05441 135 VVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEV 188
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
332-410 |
6.36e-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: 47.75 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 332 VRVIACGSAYHAGWVLKSVCESLARVPVQVELASEFRYNHP--ILENGELVLSISQSGETADTLAAVKEAKKLGAKTLSI 409
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLlsLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 496992313 410 V 410
Cdd:cd04795 81 T 81
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
372-424 |
1.15e-06 |
|
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: 49.11 E-value: 1.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 496992313 372 PILENGELVLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFV 424
Cdd:cd05005 71 PAIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVV 123
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
71-177 |
3.07e-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: 48.92 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 71 IGHTRWATHGKASEKNAHPHlsMHKEVVLVHNGIIENFAEIKNFLQEKGYSFY-SDTDTEVAV-----NLMEYYYRKEKD 144
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPF--TRGRWLFAHNGQLDGFRLLRRRLLRLLPRLPvGTTDSELAFalllsRLLERDPLDPAE 161
|
90 100 110
....*....|....*....|....*....|....*...
gi 496992313 145 ILKALFSVQKEL-----KGSFAFAIMfleDANTLYAMR 177
Cdd:cd01908 162 LLDAILQTLRELaalapPGRLNLLLS---DGEYLIATR 196
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
504-635 |
1.57e-05 |
|
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli. It is similar to the glucosamine-6-phosphate synthases (GlmS) which catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source.
Pssm-ID: 240143 [Multi-domain] Cd Length: 151 Bit Score: 45.31 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 504 IFFLGRGLDWAISMEGALKLKEIS--YIHCESYSSGELKHGTISLIEKDSPVIGLLSQEELAGK-SISNIHEVRSRGAKC 580
Cdd:cd05010 1 VVYLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQyDLDLLKELRRDGIAA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496992313 581 FAiktedIAIEEEDFAGsLSVAKTHPLFAGSLL---------VLPLQFLAYRVSLLKGFDPDKP 635
Cdd:cd05010 81 RV-----IAISPESDAG-IEDNSHYYLPGSRDLddvylafpyILYAQLFALFNSIALGLTPDNP 138
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
377-432 |
2.04e-04 |
|
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: 43.81 E-value: 2.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 496992313 377 GELVLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFVFYTQAGPE 432
Cdd:COG0794 92 GDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVERE 147
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
312-409 |
2.41e-04 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 43.82 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496992313 312 PDFSYEAFSMA-----EKDFQDISRVRVIACGSAYHAGWVLKSVCESLARVPVQVelaseFR-YNHPILENG-ELVLSIS 384
Cdd:PRK08674 12 PEQFEEALEIAisldlEEDLEKIDNIVISGMGGSGIGGDLLRILLFDELKVPVFV-----NRdYTLPAFVDEkTLVIAVS 86
|
90 100
....*....|....*....|....*
gi 496992313 385 QSGETADTLAAVKEAKKLGAKTLSI 409
Cdd:PRK08674 87 YSGNTEETLSAVEQALKRGAKIIAI 111
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
504-558 |
1.53e-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: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 496992313 504 IFFLGRGLDWAISMEGALKLKEISYIHCESYSSGELKHG-TISLIEKDSPVIGLLS 558
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHAsLLSLLRKGDVVIALSY 56
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
374-439 |
1.93e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 40.83 E-value: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496992313 374 LENGELVLSISQSGETADTLAAVKEAKKLGAKTLSIVNVKGSAIAKESDFVFYTQAGPEIAVATTK 439
Cdd:PRK12570 125 LTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTR 190
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
379-409 |
6.64e-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: 36.86 E-value: 6.64e-03
10 20 30
....*....|....*....|....*....|.
gi 496992313 379 LVLSISQSGETADTLAAVKEAKKLGAKTLSI 409
Cdd:cd05017 46 LVIAVSYSGNTEETLSAVEQAKERGAKIVAI 76
|
|
| |
