|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-367 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 551.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 1 MKGPYKHFMQKEIFEQPDSAFNTMRGRI----DFENCVVTLGGLKSWLSTIRRCRRIIMIACGTSYHSCLATRSIFEELT 76
Cdd:PLN02981 310 MKGNYDHYMQKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 77 EIPVSVELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGV 156
Cdd:PLN02981 390 GVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGV 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 157 ASTKAYTSQYIALVMFALSLSNDSISRKGRHEEIIKGLQKIPEQIKQVLKLENKIKDLCnSSLNDQKSLLLLGRGYQFAT 236
Cdd:PLN02981 470 ASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELA-ELLIDEQSLLVFGRGYNYAT 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 237 ALEGALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDA-IISND 315
Cdd:PLN02981 549 ALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDAsSVCPS 628
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
2POC_B 316 KVHTTLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:PLN02981 629 GGCRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
2-367 |
5.72e-164 |
|
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: 471.80 E-value: 5.72e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 2 KGPYKHFMQKEIFEQPDSAFNTMRGRIDFENcVVTLGGLKSWLSTIRRCRRIIMIACGTSYHSCLATRSIFEELTEIPVS 81
Cdd:COG0449 247 KGGYPHFMLKEIHEQPEAIRDTLRGRLDEDG-RVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 82 VELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVASTKA 161
Cdd:COG0449 326 VEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 162 YTSQYIALVMFALSLS--NDSISRKgRHEEIIKGLQKIPEQIKQVLKLENKIKDLCNsSLNDQKSLLLLGRGYQFATALE 239
Cdd:COG0449 406 FTTQLAALYLLALYLAraRGTLSAE-EEAELLEELRKLPEKIEEVLDLEEQIEELAE-KYADARNALFLGRGINYPVALE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 240 GALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDAIISNDKVHt 319
Cdd:COG0449 484 GALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADD- 562
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
2POC_B 320 TLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:COG0449 563 VIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-367 |
1.92e-133 |
|
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: 393.93 E-value: 1.92e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 2 KGPYKHFMQKEIFEQPDSAFNTMRGRIDFENCVVTLGGLKSWLSTIRRCRRIimiACGTSYHSCLATRSIFEELTEIPVS 81
Cdd:TIGR01135 246 KGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNIDRIQIV---ACGTSYHAGLVAKYLIERLAGIPVE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 82 VELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVASTKA 161
Cdd:TIGR01135 323 VEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 162 YTSQYIALVMFALSLSNDSISRKGRHE-EIIKGLQKIPEQIKQVLKLENKIKDLCNsSLNDQKSLLLLGRGYQFATALEG 240
Cdd:TIGR01135 403 FTTQLTVLYLLALALAKARGTLSAEEEaELVDALRRLPDLVEQVLLADESIAELAE-RYADKRNFLFLGRGLGYPIALEG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 241 ALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDAIISNDKVHtT 320
Cdd:TIGR01135 482 ALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADD-V 560
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
2POC_B 321 LEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:TIGR01135 561 IKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
219-365 |
1.10e-69 |
|
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: 215.20 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 219 LNDQKSLLLLGRGYQFATALEGALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARD 298
Cdd:cd05009 10 LKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLIKEVKARG 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2POC_B 299 GRPIVICNEGDAIISNDKVhttLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVT 365
Cdd:cd05009 90 AKVIVITDDGDAKDLADVV---IRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
57-175 |
3.69e-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: 127.80 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 57 ACGTSYHSCLATRSIFEELTEIPVSVELASDFLDR-RSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVG 135
Cdd:pfam01380 12 GRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPG 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
2POC_B 136 SSMSRQTHCGVHINAGPEIGVASTKAYTSQYIALVMFALS 175
Cdd:pfam01380 92 SPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-367 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 551.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 1 MKGPYKHFMQKEIFEQPDSAFNTMRGRI----DFENCVVTLGGLKSWLSTIRRCRRIIMIACGTSYHSCLATRSIFEELT 76
Cdd:PLN02981 310 MKGNYDHYMQKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 77 EIPVSVELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGV 156
Cdd:PLN02981 390 GVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGV 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 157 ASTKAYTSQYIALVMFALSLSNDSISRKGRHEEIIKGLQKIPEQIKQVLKLENKIKDLCnSSLNDQKSLLLLGRGYQFAT 236
Cdd:PLN02981 470 ASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELA-ELLIDEQSLLVFGRGYNYAT 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 237 ALEGALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDA-IISND 315
Cdd:PLN02981 549 ALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDAsSVCPS 628
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
2POC_B 316 KVHTTLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:PLN02981 629 GGCRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
2-367 |
5.72e-164 |
|
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: 471.80 E-value: 5.72e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 2 KGPYKHFMQKEIFEQPDSAFNTMRGRIDFENcVVTLGGLKSWLSTIRRCRRIIMIACGTSYHSCLATRSIFEELTEIPVS 81
Cdd:COG0449 247 KGGYPHFMLKEIHEQPEAIRDTLRGRLDEDG-RVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 82 VELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVASTKA 161
Cdd:COG0449 326 VEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 162 YTSQYIALVMFALSLS--NDSISRKgRHEEIIKGLQKIPEQIKQVLKLENKIKDLCNsSLNDQKSLLLLGRGYQFATALE 239
Cdd:COG0449 406 FTTQLAALYLLALYLAraRGTLSAE-EEAELLEELRKLPEKIEEVLDLEEQIEELAE-KYADARNALFLGRGINYPVALE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 240 GALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDAIISNDKVHt 319
Cdd:COG0449 484 GALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADD- 562
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
2POC_B 320 TLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:COG0449 563 VIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
2-367 |
1.07e-150 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 437.94 E-value: 1.07e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 2 KGPYKHFMQKEIFEQPDSAFNTMRGRIDFencvvtLGGLKSWLSTIRRCRRIIMIACGTSYHSCLATRSIFEELTEIPVS 81
Cdd:PRK00331 247 KGGYRHFMLKEIYEQPEAIRDTLEGRLDE------LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 82 VELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVASTKA 161
Cdd:PRK00331 321 VEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 162 YTSQYIALVMFALSL--SNDSISrKGRHEEIIKGLQKIPEQIKQVLKLENKIKDLCnSSLNDQKSLLLLGRGYQFATALE 239
Cdd:PRK00331 401 FTAQLAVLYLLALALakARGTLS-AEEEADLVHELRELPALIEQVLDLKEQIEELA-EDFADARNALFLGRGVDYPVALE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 240 GALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDAIIsnDKVHT 319
Cdd:PRK00331 479 GALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVA--EEADD 556
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
2POC_B 320 TLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:PRK00331 557 VIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
2-367 |
3.67e-149 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 436.23 E-value: 3.67e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 2 KGPYKHFMQKEIFEQPDSAFNTMRGRIDFENCVVTLGGL-KSWLSTIRRCRRIIMIACGTSYHSCLATRSIFEELTEIPV 80
Cdd:PTZ00394 305 KGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFtQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 81 SVELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVASTK 160
Cdd:PTZ00394 385 SVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 161 AYTSQYIALVMFALSLSNDSISRKGRHEEIIKGLQKIPEQIKQVLKLENKIKDLCNSSLNDQKSLLLLGRGYQFATALEG 240
Cdd:PTZ00394 465 AYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATAMEA 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 241 ALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDAIISNdKVHTT 320
Cdd:PTZ00394 545 ALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKA-AASEI 623
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
2POC_B 321 LEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:PTZ00394 624 VLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-367 |
1.92e-133 |
|
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: 393.93 E-value: 1.92e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 2 KGPYKHFMQKEIFEQPDSAFNTMRGRIDFENCVVTLGGLKSWLSTIRRCRRIimiACGTSYHSCLATRSIFEELTEIPVS 81
Cdd:TIGR01135 246 KGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNIDRIQIV---ACGTSYHAGLVAKYLIERLAGIPVE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 82 VELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVASTKA 161
Cdd:TIGR01135 323 VEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 162 YTSQYIALVMFALSLSNDSISRKGRHE-EIIKGLQKIPEQIKQVLKLENKIKDLCNsSLNDQKSLLLLGRGYQFATALEG 240
Cdd:TIGR01135 403 FTTQLTVLYLLALALAKARGTLSAEEEaELVDALRRLPDLVEQVLLADESIAELAE-RYADKRNFLFLGRGLGYPIALEG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 241 ALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDAIISNDKVHtT 320
Cdd:TIGR01135 482 ALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADD-V 560
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
2POC_B 321 LEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:TIGR01135 561 IKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
4-366 |
1.87e-100 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 310.41 E-value: 1.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 4 PYKHFMQKEIFEQPDSAFNTM--RGRI-DFENCVVtLGGLKSWLSTIRRCRRIIMIACGTSYHSCLATRSIFEELTEI-P 79
Cdd:PTZ00295 274 PYPHWTLKEIFEQPIALSRALnnGGRLsGYNNRVK-LGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 80 VSVELASDFLDRRSPvFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVAST 159
Cdd:PTZ00295 353 VQVIDASELTLYRLP-DEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVAST 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 160 KAYTSQYIALVMFALSLSN--DSISRKGRHEEIIKGLQKIPEQIKQVLKlenKIKDLCNS---SLNDQKSLLLLGRGYQF 234
Cdd:PTZ00295 432 KAFTSQVTVLSLIALWFAQnkEYSCSNYKCSSLINSLHRLPTYIGMTLK---SCEEQCKRiaeKLKNAKSMFILGKGLGY 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 235 ATALEGALKIKEISYMHSEGVLAGELKHGILALVDED--LPIIAFATRDSLFPKVMSAIEQVTARDGRPIVICNEGDaiI 312
Cdd:PTZ00295 509 PIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKARGAYIIVITDDED--L 586
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
2POC_B 313 SNDKVHTTLEVPETvDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTV 366
Cdd:PTZ00295 587 VKDFADEIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
219-365 |
1.10e-69 |
|
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: 215.20 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 219 LNDQKSLLLLGRGYQFATALEGALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVTARD 298
Cdd:cd05009 10 LKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLIKEVKARG 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2POC_B 299 GRPIVICNEGDAIISNDKVhttLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVT 365
Cdd:cd05009 90 AKVIVITDDGDAKDLADVV---IRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
57-367 |
1.54e-65 |
|
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: 210.91 E-value: 1.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 57 ACGTSYHSCLATRSIFEELTEIPVSVELASDFLDRRSPVFRDDT-CVFVSQSGETADSILALQYCLERGALTVGIVNSVG 135
Cdd:COG2222 41 GAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLKLEGTlVVAISRSGNSPEVVAALELAKARGARTLAITNNPD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 136 SSMSRQTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSNDsisrkgrhEEIIKGLQKIPEQIKQVLKLENKIKDLC 215
Cdd:COG2222 121 SPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAAWGGD--------DALLAALDALPAALEAALAADWPAAALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 216 nsSLNDQKSLLLLGRGYQFATALEGALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMSAIEQVT 295
Cdd:COG2222 193 --ALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELR 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2POC_B 296 ARDGRPIVICNEGDAIIsndkvhtTLEVPETV-DCLQGLLNVIPLQLISYWLAVNRGIDVDFPRNLAKSVTVE 367
Cdd:COG2222 271 ALGARVVAIGAEDDAAI-------TLPAIPDLhDALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
57-177 |
8.04e-58 |
|
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: 183.85 E-value: 8.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 57 ACGTSYHSCLATRSIFEELTEIPVSVELASDFLDRRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGS 136
Cdd:cd05008 6 GCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGS 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
2POC_B 137 SMSRQTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLS 177
Cdd:cd05008 86 TLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
57-175 |
3.69e-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: 127.80 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 57 ACGTSYHSCLATRSIFEELTEIPVSVELASDFLDR-RSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVG 135
Cdd:pfam01380 12 GRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPG 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
2POC_B 136 SSMSRQTHCGVHINAGPEIGVASTKAYTSQYIALVMFALS 175
Cdd:pfam01380 92 SPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
218-350 |
3.16e-33 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 120.10 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 218 SLNDQKSLLLLGRGYQFATALEGALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSLFPKVMsAIEQVTAR 297
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
2POC_B 298 DGRPIVICNEGDAIISN--DKVHTTLEVPETvdcLQGLLNVIPLQLISYWLAVNR 350
Cdd:pfam01380 80 GAKIIAITDSPGSPLAReaDHVLYINAGPET---GVASTKSITAQLAALDALAVA 131
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
57-136 |
1.84e-11 |
|
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: 60.67 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 57 ACGTSYHSCLATRSIFEELTEIPVSVELASDFLDRRSPVFRDDT-CVFVSQSGETADSILALQYCLERGALTVGIVNSVG 135
Cdd:cd05710 6 GCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKSvVILASHSGNTKETVAAAKFAKEKGATVIGLTDDED 85
|
.
2POC_B 136 S 136
Cdd:cd05710 86 S 86
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
98-172 |
5.88e-09 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 56.72 E-value: 5.88e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2POC_B 98 DDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVAST--KAYTSQYIALVMF 172
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMI 208
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
98-172 |
1.09e-07 |
|
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: 52.52 E-value: 1.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2POC_B 98 DDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVAST--KAYTSQYIALVMF 172
Cdd:cd05007 119 RDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQKLALNML 195
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
81-172 |
6.17e-07 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 50.48 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 81 SVELASDF-------LDRRSPVfRDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPE 153
Cdd:COG2103 110 AVEGAEDDeeagaadLKALGLG-PGDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPE 188
|
90 100
....*....|....*....|..
2POC_B 154 IgVA-ST--KAYTSQYIALVMF 172
Cdd:COG2103 189 V-ITgSTrlKAGTAQKLVLNML 209
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
57-131 |
1.54e-06 |
|
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: 45.83 E-value: 1.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2POC_B 57 ACGTSYHSCLATRSIFEELTEIPVSVELASDFLD--RRSPVFRDDTCVFVSQSGETADSILALQYCLERGALTVGIV 131
Cdd:cd04795 5 GIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAIT 81
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
57-304 |
1.00e-04 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 43.84 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 57 ACGTSYHSCLATRSIFEELTEIPVSVELASDFLDRrSPVFRDDTC--VFVSQSGETADSILALQYCLERGALTVGIVNSV 134
Cdd:PRK11382 51 ACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDN-TPYRLDDRCavIGVSDYGKTEEVIKALELGRACGALTAAFTKRA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 135 GSSmsrqthcgvhINAGPEIGVASTKAYTSQYIALVMFALSLsnDSISRKGRHEEIIK---GLQKIPEQIKQVLKL-ENK 210
Cdd:PRK11382 130 DSP----------ITSAAEFSIDYQADCIWEIHLLLCYSVVL--EMITRLAPNAEIGKiknDLKQLPNALGHLVRTwEEK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 211 IKDLcnSSLNDQKSLL-------LLGRGYQfatalEGALKIKEISYMHSEGVLAGELKHGILALVDEDLPIIAFATRDSL 283
Cdd:PRK11382 198 GRQL--GELASQWPMIytvaagpLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDES 270
|
250 260
....*....|....*....|.
2POC_B 284 FPKVMSAIEQVTARDGRPIVI 304
Cdd:PRK11382 271 RHTTERAINFVKQRTDNVIVI 291
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
97-194 |
1.17e-04 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 43.38 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 97 RDDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRqtHCGVHINAGPEIGVASTKAYTSQYIALVMF---- 172
Cdd:COG1737 182 PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAK--LADVVLYVPSEEPTLRSSAFSSRVAQLALIdala 259
|
90 100
....*....|....*....|....*
2POC_B 173 ---ALSLSNDSISRKGRHEEIIKGL 194
Cdd:COG1737 260 aavAQRDGDKARERLERTEALLSEL 284
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
228-357 |
3.79e-04 |
|
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: 40.30 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 228 LGRGYQFATALEGALKIKEIsymhSEGVLAGE------LKHGILALVDEDLPIIAFATRDSLFPKV-MSAIEQVtARDG- 299
Cdd:cd05010 4 LGSGPLAGLAREAALKVLEL----TAGKVATVydsplgFRHGPKSLVDDDTLVVVFVSNDPYTRQYdLDLLKEL-RRDGi 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 300 --RPIVICNEGDAIISNDKVHTTLEVPETVDCLQGLLNVIPLQLISYWLAVNRGIDVDFP 357
Cdd:cd05010 79 aaRVIAISPESDAGIEDNSHYYLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNP 138
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
98-186 |
1.85e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 39.67 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2POC_B 98 DDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHCGVHINAGPEIGVAST--KAYTSQYIALVMfals 175
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNM---- 203
|
90
....*....|.
2POC_B 176 LSNDSISRKGR 186
Cdd:PRK12570 204 LSTASMIRLGK 214
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
98-171 |
1.99e-03 |
|
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: 37.98 E-value: 1.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2POC_B 98 DDTCVFVSQSGETADSILALQYCLERGALTVGIVNSVGSSMSRQTHcgVHINAGPEIGVASTKAYTSQYIALVM 171
Cdd:cd05013 61 GDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| |
