|
Name |
Accession |
Description |
Interval |
E-value |
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
23-139 |
7.54e-43 |
|
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: 143.87 E-value: 7.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 23 VFLVACGGSLVDMYPAKYFLDSEAtKLHVGMYTANEFVYATPKTLGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTITL 102
Cdd:cd05710 2 VFFVGCGGSLADMYPAKYFLKKES-KLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 488976053 103 THNAQAQLIEYASHNILYAWGndTNVVDNPMAIILNL 139
Cdd:cd05710 81 TDDEDSPLAKLADYVIVYGFE--IDAVEEKYLLLYML 115
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
4-318 |
3.94e-38 |
|
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: 138.11 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 4 KEIINAVAKEIEDKGGiRQVFLVACGGSLVDMYPAKYFLdSEATKLHVGMYTANEFVYATPKTLGENSLVIVCSHGGNTP 83
Cdd:COG2222 19 AAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 84 ESVAAAKLAQQHQAHTITLTHNAQAQLIEYASHNILYAWGNDTNVV-----DNPMAIILNLcvdtlqqvegFNNYADFQQ 158
Cdd:COG2222 97 EVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAatksfTTMLLALLAL----------LAAWGGDDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 159 GMTQINGVIAHGRQQVADRCQRFAQ-KYQDEKLFYILSSGASYGHAYGFAICsLMEMQWLHAAPIHSGEYFHGPFEVTNK 237
Cdd:COG2222 167 LLAALDALPAALEAALAADWPAAALaALADAERVVFLGRGPLYGLAREAALK-LKELSAGHAEAYSAAEFRHGPKSLVDP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 238 ETPFILLMNEGRTRAMDERALAFLTKYAEKVEVVDAKELGIGVLP--PSVVEFFNPVL----FYSIMceYRSALAdiRQH 311
Cdd:COG2222 246 GTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPaiPDLHDALDPLLllvvAQRLA--LALALA--RGL 321
|
....*..
gi 488976053 312 PLDTRRY 318
Cdd:COG2222 322 DPDTPRH 328
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
176-318 |
3.28e-30 |
|
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: 111.97 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 176 DRCQRFAQKYQDEKLFYILSSGASYGHAYGFAICsLMEMQWLHAAPIHSGEYFHGPFEVTNKETPFILLMNEGRTRAMDE 255
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALK-LKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976053 256 RALAFLTKYAEKVEVVDAKELGIG-----VLPPSVVEFFNPVL----FYsIMCEYrsaLADIRQHPLDTRRY 318
Cdd:cd05009 80 SLIKEVKARGAKVIVITDDGDAKDladvvIRVPATVEELSPLLyivpLQ-LLAYH---LAVARGIDPDKPRN 147
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
7-324 |
2.73e-27 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 109.32 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 7 INAVAKEIEDKGgIRQVFLVACGGSLVDMYPAKYFLDsEATKLHVGMYTANEFVYATPKTLGENSLVIVCSHGGNTPESV 86
Cdd:PRK11382 32 VHAIVEEMVKRD-IDRIYFVACGSPLNAAQTAKHLAD-RFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 87 AAAKLAQQHQAHTITLTHNAQAQLIEYASHNILYAwgndtnvVDNPMAIILNLCVDT-LQQVEGFNNYADF---QQGMTQ 162
Cdd:PRK11382 110 KALELGRACGALTAAFTKRADSPITSAAEFSIDYQ-------ADCIWEIHLLLCYSVvLEMITRLAPNAEIgkiKNDLKQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 163 INGVIAHGRQQVADRCQRFAQKYQDEKLFYILSSGASYGHAYGFAICSLMEMQWLHAAPIHSGEYFHGPFEVTNKETPFI 242
Cdd:PRK11382 183 LPNALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 243 LLMNEGRTRAMDERALAFLTKYAEKVEVVDAKELGIGVLPpsvveFFNPVLFYSIM---CEYRSALADirQHPLDTRRYM 319
Cdd:PRK11382 263 FLLGNDESRHTTERAINFVKQRTDNVIVIDYAEISQGLHP-----WLAPFLMFVPMewlCYYLSIYKD--HNPDERRYYG 335
|
....*
gi 488976053 320 GLVEY 324
Cdd:PRK11382 336 GLVEY 340
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
21-144 |
3.29e-10 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 57.31 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 21 RQVFLVACGGS-LVDMYPAKYFLdsEATKLHVGMYTANEFVYATPKTLGENSLVIVCSHGGNTPESVAAAKLAQQHQAHT 99
Cdd:pfam01380 6 KRIFVIGRGTSyAIALELALKFE--EIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKI 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488976053 100 ITLTHNAQAQLIEYASHNIlyawgnDTNVVDNPMAIILNLCVDTL 144
Cdd:pfam01380 84 IAITDSPGSPLAREADHVL------YINAGPETGVASTKSITAQL 122
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
20-245 |
1.80e-08 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 55.80 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 20 IRQVFLVACGGSLVDMYPAKYFLDSEATKLHVGMYTANEF-VYATPKtlgENSLVIVCSHGGNTPESVAAAKLAQQHQAH 98
Cdd:PTZ00295 322 IKNLILVGCGTSYYAALFAASIMQKLKCFNTVQVIDASELtLYRLPD---EDAGVIFISQSGETLDVVRALNLADELNLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 99 TITLThNAQAQLIEYASHNILYAWGNDTNVVDNPMAIILNLCVDTLQQVEGFNNY---------ADFQQGMTQINGVIAH 169
Cdd:PTZ00295 399 KISVV-NTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeyscsnykcSSLINSLHRLPTYIGM 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976053 170 GRQQVADRCQRFAQKYQDEKLFYILSSGASYGHAYGFAIcSLMEMQWLHAAPIHSGEYFHGPFEVTNKE--TPFILLM 245
Cdd:PTZ00295 478 TLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGAL-KIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILII 554
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
23-139 |
7.54e-43 |
|
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: 143.87 E-value: 7.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 23 VFLVACGGSLVDMYPAKYFLDSEAtKLHVGMYTANEFVYATPKTLGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTITL 102
Cdd:cd05710 2 VFFVGCGGSLADMYPAKYFLKKES-KLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 488976053 103 THNAQAQLIEYASHNILYAWGndTNVVDNPMAIILNL 139
Cdd:cd05710 81 TDDEDSPLAKLADYVIVYGFE--IDAVEEKYLLLYML 115
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
4-318 |
3.94e-38 |
|
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: 138.11 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 4 KEIINAVAKEIEDKGGiRQVFLVACGGSLVDMYPAKYFLdSEATKLHVGMYTANEFVYATPKTLGENSLVIVCSHGGNTP 83
Cdd:COG2222 19 AAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 84 ESVAAAKLAQQHQAHTITLTHNAQAQLIEYASHNILYAWGNDTNVV-----DNPMAIILNLcvdtlqqvegFNNYADFQQ 158
Cdd:COG2222 97 EVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAatksfTTMLLALLAL----------LAAWGGDDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 159 GMTQINGVIAHGRQQVADRCQRFAQ-KYQDEKLFYILSSGASYGHAYGFAICsLMEMQWLHAAPIHSGEYFHGPFEVTNK 237
Cdd:COG2222 167 LLAALDALPAALEAALAADWPAAALaALADAERVVFLGRGPLYGLAREAALK-LKELSAGHAEAYSAAEFRHGPKSLVDP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 238 ETPFILLMNEGRTRAMDERALAFLTKYAEKVEVVDAKELGIGVLP--PSVVEFFNPVL----FYSIMceYRSALAdiRQH 311
Cdd:COG2222 246 GTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPaiPDLHDALDPLLllvvAQRLA--LALALA--RGL 321
|
....*..
gi 488976053 312 PLDTRRY 318
Cdd:COG2222 322 DPDTPRH 328
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
176-318 |
3.28e-30 |
|
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: 111.97 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 176 DRCQRFAQKYQDEKLFYILSSGASYGHAYGFAICsLMEMQWLHAAPIHSGEYFHGPFEVTNKETPFILLMNEGRTRAMDE 255
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALK-LKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976053 256 RALAFLTKYAEKVEVVDAKELGIG-----VLPPSVVEFFNPVL----FYsIMCEYrsaLADIRQHPLDTRRY 318
Cdd:cd05009 80 SLIKEVKARGAKVIVITDDGDAKDladvvIRVPATVEELSPLLyivpLQ-LLAYH---LAVARGIDPDKPRN 147
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
7-324 |
2.73e-27 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 109.32 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 7 INAVAKEIEDKGgIRQVFLVACGGSLVDMYPAKYFLDsEATKLHVGMYTANEFVYATPKTLGENSLVIVCSHGGNTPESV 86
Cdd:PRK11382 32 VHAIVEEMVKRD-IDRIYFVACGSPLNAAQTAKHLAD-RFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 87 AAAKLAQQHQAHTITLTHNAQAQLIEYASHNILYAwgndtnvVDNPMAIILNLCVDT-LQQVEGFNNYADF---QQGMTQ 162
Cdd:PRK11382 110 KALELGRACGALTAAFTKRADSPITSAAEFSIDYQ-------ADCIWEIHLLLCYSVvLEMITRLAPNAEIgkiKNDLKQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 163 INGVIAHGRQQVADRCQRFAQKYQDEKLFYILSSGASYGHAYGFAICSLMEMQWLHAAPIHSGEYFHGPFEVTNKETPFI 242
Cdd:PRK11382 183 LPNALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 243 LLMNEGRTRAMDERALAFLTKYAEKVEVVDAKELGIGVLPpsvveFFNPVLFYSIM---CEYRSALADirQHPLDTRRYM 319
Cdd:PRK11382 263 FLLGNDESRHTTERAINFVKQRTDNVIVIDYAEISQGLHP-----WLAPFLMFVPMewlCYYLSIYKD--HNPDERRYYG 335
|
....*
gi 488976053 320 GLVEY 324
Cdd:PRK11382 336 GLVEY 340
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
23-119 |
3.44e-14 |
|
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: 68.29 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 23 VFLVACGGSLVDMYPAKYFLdSEATKLHVGMYTANEFVYATPkTLGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTITL 102
Cdd:cd05008 2 ILIVGCGTSYHAALVAKYLL-ERLAGIPVEVEAASEFRYRRP-LLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAI 79
|
90
....*....|....*..
gi 488976053 103 THNAQAQLIEYASHNIL 119
Cdd:cd05008 80 TNVVGSTLAREADYVLY 96
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
5-121 |
5.59e-12 |
|
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: 62.25 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 5 EIINAVAKEIEDKggiRQVFLVACGGSlvdMYPAKYFldseATKL-----HVGMYTANEFVYATPKTLGENSLVIVCSHG 79
Cdd:cd05013 1 EALEKAVDLLAKA---RRIYIFGVGSS---GLVAEYL----AYKLlrlgkPVVLLSDPHLQLMSAANLTPGDVVIAISFS 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488976053 80 GNTPESVAAAKLAQQHQAHTITLTHNAQAQLIEYASHNILYA 121
Cdd:cd05013 71 GETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVS 112
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
21-144 |
3.29e-10 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 57.31 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 21 RQVFLVACGGS-LVDMYPAKYFLdsEATKLHVGMYTANEFVYATPKTLGENSLVIVCSHGGNTPESVAAAKLAQQHQAHT 99
Cdd:pfam01380 6 KRIFVIGRGTSyAIALELALKFE--EIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKI 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488976053 100 ITLTHNAQAQLIEYASHNIlyawgnDTNVVDNPMAIILNLCVDTL 144
Cdd:pfam01380 84 IAITDSPGSPLAREADHVL------YINAGPETGVASTKSITAQL 122
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
20-245 |
1.80e-08 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 55.80 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 20 IRQVFLVACGGSLVDMYPAKYFLDSEATKLHVGMYTANEF-VYATPKtlgENSLVIVCSHGGNTPESVAAAKLAQQHQAH 98
Cdd:PTZ00295 322 IKNLILVGCGTSYYAALFAASIMQKLKCFNTVQVIDASELtLYRLPD---EDAGVIFISQSGETLDVVRALNLADELNLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 99 TITLThNAQAQLIEYASHNILYAWGNDTNVVDNPMAIILNLCVDTLQQVEGFNNY---------ADFQQGMTQINGVIAH 169
Cdd:PTZ00295 399 KISVV-NTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeyscsnykcSSLINSLHRLPTYIGM 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976053 170 GRQQVADRCQRFAQKYQDEKLFYILSSGASYGHAYGFAIcSLMEMQWLHAAPIHSGEYFHGPFEVTNKE--TPFILLM 245
Cdd:PTZ00295 478 TLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGAL-KIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILII 554
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
21-242 |
4.75e-07 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 51.42 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 21 RQVFLVACGGSLVDMYPAKYFLDsEATKLHVGMYTANEFVYATPKtLGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTI 100
Cdd:PTZ00394 355 RRILFIACGTSLNSCLAVRPLFE-ELVPLPISVENASDFLDRRPR-IQRDDVCFFVSQSGETADTLMALQLCKEAGAMCV 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 101 TLTHNAQAQLIEYASHNILYAWGNDTNVVDN----PMAIILNLCVDTLQ--QVEGFNNYADFQQGMTQINGVIAHGRQQV 174
Cdd:PTZ00394 433 GITNVVGSSISRLTHYAIHLNAGVEVGVASTkaytSQVVVLTLVALLLSsdSVRLQERRNEIIRGLAELPAAISECLKIT 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976053 175 ADRCQRFAQKYQDEKLFYILSSGASYGHAYGFAIcSLMEMQWLHAAPIHSGEYFHGPFEVTNKETPFI 242
Cdd:PTZ00394 513 HDPVKALAARLKESSSILVLGRGYDLATAMEAAL-KVKELSYVHTEGIHSGELKHGPLALIDETSPVL 579
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
60-121 |
3.08e-05 |
|
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: 42.64 E-value: 3.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976053 60 VYATPKTLGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTITLTHNaqAQLIEYA-SHNILYA 121
Cdd:cd05017 34 DYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAITSG--GKLLEMArEHGVPVI 94
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
67-114 |
5.72e-05 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 43.98 E-value: 5.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488976053 67 LGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTITLTHNAQAQLIEYA 114
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLA 232
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
5-114 |
1.40e-04 |
|
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: 41.79 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 5 EIINAVAKEIEDK---------GGIRQVFLVACGGS-LVdmypAKYFldseATKL-HVGM--YTANEFVyaTPkTLGENS 71
Cdd:cd05005 9 EEIENVADKIDEEeldklisaiLNAKRIFVYGAGRSgLV----AKAF----AMRLmHLGLnvYVVGETT--TP-AIGPGD 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488976053 72 LVIVCSHGGNTPESVAAAKLAQQHQAHTITLTHNAQAQLIEYA 114
Cdd:cd05005 78 LLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLA 120
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
67-119 |
2.57e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 39.00 E-value: 2.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488976053 67 LGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTITLTHNAQAQLIEYASHNIL 119
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIE 181
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
67-119 |
3.01e-03 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 37.14 E-value: 3.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488976053 67 LGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTITLTHNAQAQLIEYASHNIL 119
Cdd:cd05014 45 VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLD 97
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
23-104 |
5.37e-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: 35.43 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976053 23 VFLVACGGSLvdmYPAKYF--LDSEATKLHVGMYTANEFVYATPKTLG-ENSLVIVCSHGGNTPESVAAAKLAQQHQAHT 99
Cdd:cd04795 1 IFVIGIGGSG---AIAAYFalELLELTGIEVVALIATELEHASLLSLLrKGDVVIALSYSGRTEELLAALEIAKELGIPV 77
|
....*
gi 488976053 100 ITLTH 104
Cdd:cd04795 78 IAITD 82
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
61-103 |
6.42e-03 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 38.04 E-value: 6.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488976053 61 YATPKTLGENSLVIVCSHGGNTPESVAAAKLAQQHQAHTITLT 103
Cdd:PRK08674 70 YTLPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAIT 112
|
|
| |
