|
Name |
Accession |
Description |
Interval |
E-value |
| agaS_fam |
TIGR02815 |
putative sugar isomerase, AgaS family; Some members of this protein family are found in ... |
16-377 |
2.56e-152 |
|
putative sugar isomerase, AgaS family; Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases.
Pssm-ID: 131862 [Multi-domain] Cd Length: 372 Bit Score: 434.61 E-value: 2.56e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 16 SGKWTATEIAQQPTLWRELQADFKHREAQLSAFLNPLLAKDNLRIILTGAGTSAYIGEALAAFLQRQLRLpgqRVEALSS 95
Cdd:TIGR02815 1 NATHTAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGL---NVSAVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 96 TDIVSHPRLHLNPLQPTLIVSYGRSGNSPESLAVLALADELLTDVSHLLLTCNPEGALASYAAEHSHKACLwLMPQESHD 175
Cdd:TIGR02815 78 TDLVSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFAL-LMPAESND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 176 RSFAMTSSFSCMYLATLLLFAE---EDKSLSRVLTLTEQLLETRL--DGVQQTAGHCCKRIVFLGAGPLKAAAQEAALKY 250
Cdd:TIGR02815 157 RSFAMTSSFSCMTLATLAVLGPetiESQTEERFADAALCILESGQwdFSEGVLGYAPWERIVYLGSGGLQGLARESALKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 251 LELTAGIVISSFESPLGFRHGPKSLVNEDTQIVLLGSSEPYARAYDLDLLAELRADKRALDICYLSEEALAQDGQA---- 326
Cdd:TIGR02815 237 LELTAGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGdhfi 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717501609 327 -----SLEEAWLTLPFIVYCQLLAFYKALELGVSPDNPCPSGQVNRVVQGVKLHSL 377
Cdd:TIGR02815 317 lppsrHFIDVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
21-372 |
1.68e-95 |
|
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: 288.72 E-value: 1.68e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 21 ATEIAQQPTLWRELqadFKHREAQLSAFLNPLLAKDNLRIILTGAGTSAYIGEALAAFLQRQLRLPgqrVEALSSTDIVS 100
Cdd:COG2222 1 AREIAQQPEAWRRA---LAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIP---VAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 101 HPRlHLnPLQPTLIVSYGRSGNSPESLAVLALADELltDVSHLLLTCNPEGALASYAAEhshkacLWLMPqESHDRSFAM 180
Cdd:COG2222 75 YPA-YL-KLEGTLVVAISRSGNSPEVVAALELAKAR--GARTLAITNNPDSPLAEAADR------VLPLP-AGPEKSVAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 181 TSSFSCMYLATLLLFAE--EDKSLSRVLT----LTEQLLETRLDGVQQTAGHCCKRIVFLGAGPLKAAAQEAALKYLELT 254
Cdd:COG2222 144 TKSFTTMLLALLALLAAwgGDDALLAALDalpaALEAALAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 255 AGivISSFESPLGFRHGPKSLVNEDTQIVLLGSSEPyARAYDLDLLAELRAD-KRALDICYLSEEALAQDGQASLEEAWL 333
Cdd:COG2222 224 AG--HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRALgARVVAIGAEDDAAITLPAIPDLHDALD 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 1717501609 334 TLPFIVYCQLLAFYKALELGVSPDNPCPsgqVNRVVQGV 372
Cdd:COG2222 301 PLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
231-372 |
1.12e-71 |
|
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: 220.96 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 231 IVFLGAGPLKAAAQEAALKYLELTAGIVISSFESPLGFRHGPKSLVNEDTQIVLLGSSEPYARAYDLDLLAELRADKRAL 310
Cdd:cd05010 1 VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717501609 311 DICYLSEEALA---------QDGQASLEEAWLTLPFIVYCQLLAFYKALELGVSPDNPCPSGQVNRVVQGV 372
Cdd:cd05010 81 RVIAISPESDAgiednshyyLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
226-303 |
1.10e-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. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 50.38 E-value: 1.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717501609 226 HCCKRIVFLGAGPLKAAAQEAALKYLELTAGIVisSFESPLGFRHGPKSLVNEDTQIVLLGSSEpyaRAYDLDLLAEL 303
Cdd:pfam01380 3 AKAKRIFVIGRGTSYAIALELALKFEEIGYKVV--EVELASELRHGVLALVDEDDLVIAISYSG---ETKDLLAAAEL 75
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
19-359 |
3.11e-07 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 52.33 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 19 WTATEIAQQP-TLWREL-------QADFKHREAQLSAFLNPLLAKDNLriILTGAGTSAYIGEALAAFLQRqLRLPGQrV 90
Cdd:PTZ00295 278 WTLKEIFEQPiALSRALnnggrlsGYNNRVKLGGLDQYLEELLNIKNL--ILVGCGTSYYAALFAASIMQK-LKCFNT-V 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 91 EALSSTDIvshpRLHLNPLQPTLIVSYGRSGNSPESLAVLALADEL-------LTDVSHLL---------LTCNPEGALA 154
Cdd:PTZ00295 354 QVIDASEL----TLYRLPDEDAGVIFISQSGETLDVVRALNLADELnlpkisvVNTVGSLIarstdcgvyLNAGREVAVA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 155 SYAAEHSHKACLWLMP------QESHDRSFAMTSsfscmylatlLLfaeedKSLSRVLTLTEQLLETRLDGVQQTAGHCC 228
Cdd:PTZ00295 430 STKAFTSQVTVLSLIAlwfaqnKEYSCSNYKCSS----------LI-----NSLHRLPTYIGMTLKSCEEQCKRIAEKLK 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 229 --KRIVFLGAGPLKAAAQEAALKYLELTAgIVISSFESPlGFRHGPKSLVNED--TQIVLLGSSEPYARAYdLDLLAELR 304
Cdd:PTZ00295 495 naKSMFILGKGLGYPIALEGALKIKEITY-IHAEGFSGG-ALKHGPFALIDKEknTPVILIILDDEHKELM-INAAEQVK 571
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 305 AdKRALDICYLSEEALAQDGQASL----EEAWLT-LPFIVYCQLLAFYKALELGVSPDNP 359
Cdd:PTZ00295 572 A-RGAYIIVITDDEDLVKDFADEIilipSNGPLTaLLAVIPLQLLAYEIAILRGINPDKP 630
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| agaS_fam |
TIGR02815 |
putative sugar isomerase, AgaS family; Some members of this protein family are found in ... |
16-377 |
2.56e-152 |
|
putative sugar isomerase, AgaS family; Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases.
Pssm-ID: 131862 [Multi-domain] Cd Length: 372 Bit Score: 434.61 E-value: 2.56e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 16 SGKWTATEIAQQPTLWRELQADFKHREAQLSAFLNPLLAKDNLRIILTGAGTSAYIGEALAAFLQRQLRLpgqRVEALSS 95
Cdd:TIGR02815 1 NATHTAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGL---NVSAVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 96 TDIVSHPRLHLNPLQPTLIVSYGRSGNSPESLAVLALADELLTDVSHLLLTCNPEGALASYAAEHSHKACLwLMPQESHD 175
Cdd:TIGR02815 78 TDLVSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFAL-LMPAESND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 176 RSFAMTSSFSCMYLATLLLFAE---EDKSLSRVLTLTEQLLETRL--DGVQQTAGHCCKRIVFLGAGPLKAAAQEAALKY 250
Cdd:TIGR02815 157 RSFAMTSSFSCMTLATLAVLGPetiESQTEERFADAALCILESGQwdFSEGVLGYAPWERIVYLGSGGLQGLARESALKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 251 LELTAGIVISSFESPLGFRHGPKSLVNEDTQIVLLGSSEPYARAYDLDLLAELRADKRALDICYLSEEALAQDGQA---- 326
Cdd:TIGR02815 237 LELTAGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGdhfi 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717501609 327 -----SLEEAWLTLPFIVYCQLLAFYKALELGVSPDNPCPSGQVNRVVQGVKLHSL 377
Cdd:TIGR02815 317 lppsrHFIDVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
21-372 |
1.68e-95 |
|
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: 288.72 E-value: 1.68e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 21 ATEIAQQPTLWRELqadFKHREAQLSAFLNPLLAKDNLRIILTGAGTSAYIGEALAAFLQRQLRLPgqrVEALSSTDIVS 100
Cdd:COG2222 1 AREIAQQPEAWRRA---LAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIP---VAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 101 HPRlHLnPLQPTLIVSYGRSGNSPESLAVLALADELltDVSHLLLTCNPEGALASYAAEhshkacLWLMPqESHDRSFAM 180
Cdd:COG2222 75 YPA-YL-KLEGTLVVAISRSGNSPEVVAALELAKAR--GARTLAITNNPDSPLAEAADR------VLPLP-AGPEKSVAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 181 TSSFSCMYLATLLLFAE--EDKSLSRVLT----LTEQLLETRLDGVQQTAGHCCKRIVFLGAGPLKAAAQEAALKYLELT 254
Cdd:COG2222 144 TKSFTTMLLALLALLAAwgGDDALLAALDalpaALEAALAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 255 AGivISSFESPLGFRHGPKSLVNEDTQIVLLGSSEPyARAYDLDLLAELRAD-KRALDICYLSEEALAQDGQASLEEAWL 333
Cdd:COG2222 224 AG--HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRALgARVVAIGAEDDAAITLPAIPDLHDALD 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 1717501609 334 TLPFIVYCQLLAFYKALELGVSPDNPCPsgqVNRVVQGV 372
Cdd:COG2222 301 PLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
231-372 |
1.12e-71 |
|
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: 220.96 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 231 IVFLGAGPLKAAAQEAALKYLELTAGIVISSFESPLGFRHGPKSLVNEDTQIVLLGSSEPYARAYDLDLLAELRADKRAL 310
Cdd:cd05010 1 VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717501609 311 DICYLSEEALA---------QDGQASLEEAWLTLPFIVYCQLLAFYKALELGVSPDNPCPSGQVNRVVQGV 372
Cdd:cd05010 81 RVIAISPESDAgiednshyyLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
59-195 |
3.64e-25 |
|
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: 99.11 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 59 RIILTGAGTSAYIGEALAAFLQRQLRLPgqrVEAlsstdIVSHPRLHLNPL--QPTLIVSYGRSGNSPESLAVLALADEL 136
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIP---VEV-----EAASEFRYRRPLldEDTLVIAISQSGETADTLAALRLAKEK 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717501609 137 ltdVSHLLLTCNPEGALASYAAEHShkACLWLMPQESHDRSFAMTSSFSCMYLATLLLF 195
Cdd:cd05008 73 ---GAKTVAITNVVGSTLAREADYV--LYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
228-359 |
4.67e-17 |
|
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: 77.69 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 228 CKRIVFLGAGPLKAAAQEAALKYLElTAGI---VISSFEsplgFRHGPKSLVNEDTQIVLLGSSEPYARAYDlDLLAELR 304
Cdd:cd05009 13 AKSFYVLGRGPNYGTALEGALKLKE-TSYIhaeAYSAGE----FKHGPIALVDEGTPVIFLAPEDRLEEKLE-SLIKEVK 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717501609 305 AdkRALDICYLSEEALAQDGQ------ASLEEAWLTLPFIVYCQLLAFYKALELGVSPDNP 359
Cdd:cd05009 87 A--RGAKVIVITDDGDAKDLAdvvirvPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKP 145
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
226-303 |
1.10e-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. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 50.38 E-value: 1.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717501609 226 HCCKRIVFLGAGPLKAAAQEAALKYLELTAGIVisSFESPLGFRHGPKSLVNEDTQIVLLGSSEpyaRAYDLDLLAEL 303
Cdd:pfam01380 3 AKAKRIFVIGRGTSYAIALELALKFEEIGYKVV--EVELASELRHGVLALVDEDDLVIAISYSG---ETKDLLAAAEL 75
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
19-359 |
3.11e-07 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 52.33 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 19 WTATEIAQQP-TLWREL-------QADFKHREAQLSAFLNPLLAKDNLriILTGAGTSAYIGEALAAFLQRqLRLPGQrV 90
Cdd:PTZ00295 278 WTLKEIFEQPiALSRALnnggrlsGYNNRVKLGGLDQYLEELLNIKNL--ILVGCGTSYYAALFAASIMQK-LKCFNT-V 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 91 EALSSTDIvshpRLHLNPLQPTLIVSYGRSGNSPESLAVLALADEL-------LTDVSHLL---------LTCNPEGALA 154
Cdd:PTZ00295 354 QVIDASEL----TLYRLPDEDAGVIFISQSGETLDVVRALNLADELnlpkisvVNTVGSLIarstdcgvyLNAGREVAVA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 155 SYAAEHSHKACLWLMP------QESHDRSFAMTSsfscmylatlLLfaeedKSLSRVLTLTEQLLETRLDGVQQTAGHCC 228
Cdd:PTZ00295 430 STKAFTSQVTVLSLIAlwfaqnKEYSCSNYKCSS----------LI-----NSLHRLPTYIGMTLKSCEEQCKRIAEKLK 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 229 --KRIVFLGAGPLKAAAQEAALKYLELTAgIVISSFESPlGFRHGPKSLVNED--TQIVLLGSSEPYARAYdLDLLAELR 304
Cdd:PTZ00295 495 naKSMFILGKGLGYPIALEGALKIKEITY-IHAEGFSGG-ALKHGPFALIDKEknTPVILIILDDEHKELM-INAAEQVK 571
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 305 AdKRALDICYLSEEALAQDGQASL----EEAWLT-LPFIVYCQLLAFYKALELGVSPDNP 359
Cdd:PTZ00295 572 A-RGAYIIVITDDEDLVKDFADEIilipSNGPLTaLLAVIPLQLLAYEIAILRGINPDKP 630
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
52-196 |
1.02e-05 |
|
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: 44.91 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 52 LLAKDNlRIILTGAGTSAYIgealAAFLQRQLRLPGQRVEALSSTDIvshPRLHLNPLQPT---LIVSYgrSGNSPESLA 128
Cdd:cd05013 9 LLAKAR-RIYIFGVGSSGLV----AEYLAYKLLRLGKPVVLLSDPHL---QLMSAANLTPGdvvIAISF--SGETKETVE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717501609 129 VLALADELLTDVshLLLTCNPEGALASYAaehshKACLWLMPQESHDRSFAMTSSFSCMYLATLLLFA 196
Cdd:cd05013 79 AAEIAKERGAKV--IAITDSANSPLAKLA-----DIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
59-216 |
3.53e-05 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 44.92 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 59 RIILTGAGTSAyigeALAAFLQRQLRLPGQRVEALSSTdiVSHPRLHLNPLQP---TLIVSYgrSGNSPESLAVLALADE 135
Cdd:COG1737 136 RIYIFGVGASA----PVAEDLAYKLLRLGKNVVLLDGD--GHLQAESAALLGPgdvVIAISF--SGYTRETLEAARLAKE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 136 LltDVSHLLLTCNPEGALASYAAEhshkaCLWLMPQESHDRSFAMTSSFSCMY----LATLLLFAEEDKSLSRvLTLTEQ 211
Cdd:COG1737 208 R--GAKVIAITDSPLSPLAKLADV-----VLYVPSEEPTLRSSAFSSRVAQLAlidaLAAAVAQRDGDKARER-LERTEA 279
|
....*
gi 1717501609 212 LLETR 216
Cdd:COG1737 280 LLSEL 284
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
59-187 |
9.24e-05 |
|
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: 41.76 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 59 RIILTGAGTSAYIGEALAAflqrqlrlpgqrveALSSTDIVS---HPR--LH--LNPLQP--TLI-VSYgrSGNSPESLA 128
Cdd:cd05014 2 KVVVTGVGKSGHIARKIAA--------------TLSSTGTPAfflHPTeaLHgdLGMVTPgdVVIaISN--SGETDELLN 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717501609 129 VLALADELLTDVshLLLTCNPEGALASYA-----AEHSHKACLW-LMPqeshdrsfamTSSFSCM 187
Cdd:cd05014 66 LLPHLKRRGAPI--IAITGNPNSTLAKLSdvvldLPVEEEACPLgLAP----------TTSTTAM 118
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
59-195 |
3.18e-04 |
|
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: 40.36 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 59 RIILTGAGTSAYIGEALAAFLQRQLRLPgqrVEALSSTDIVSHPRLHLNPLQPTLIVSYgrSGNSPESLAVLALADELlt 138
Cdd:pfam01380 7 RIFVIGRGTSYAIALELALKFEEIGYKV---VEVELASELRHGVLALVDEDDLVIAISY--SGETKDLLAAAELAKAR-- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717501609 139 DVSHLLLTCNPEGALASYAAehshkacLWLMPQESHDRSFAMTSSFSCMYLATLLLF 195
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREAD-------HVLYINAGPETGVASTKSITAQLAALDALA 129
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
179-359 |
9.69e-03 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 37.93 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 179 AMTSSFSCMYLATLLLF----------AEEDKSLSRVLTLTEQLLETRLDGVQQTAGHCC--KRIVFLGAGPLKAAAQEA 246
Cdd:PTZ00394 465 AYTSQVVVLTLVALLLSsdsvrlqerrNEIIRGLAELPAAISECLKITHDPVKALAARLKesSSILVLGRGYDLATAMEA 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717501609 247 ALKYLEL----TAGivISSFEsplgFRHGPKSLVNEDTQIVLLGSSEpyaRAYDLDLLAELRADKRALDICYLSEEALAQ 322
Cdd:PTZ00394 545 ALKVKELsyvhTEG--IHSGE----LKHGPLALIDETSPVLAMCTHD---KHFGLSKSAVQQVKARGGAVVVFATEVDAE 615
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1717501609 323 DGQASLEeaWLTLPFIVYC----------QLLAFYKALELGVSPDNP 359
Cdd:PTZ00394 616 LKAAASE--IVLVPKTVDClqcvvnvipfQLLAYYMALLRGNNVDCP 660
|
|
| |
