|
Name |
Accession |
Description |
Interval |
E-value |
| agaS_fam |
TIGR02815 |
putative sugar isomerase, AgaS family; Some members of this protein family are found in ... |
14-379 |
0e+00 |
|
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: 608.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 14 EKEIRQQPASWLRSLNNIDNLRASIDSFLTPLLRKPDLRIVLTGAGTSAFIGDIIAPWLASHTGKNITAIPTTDLVTNPM 93
Cdd:TIGR02815 6 AREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGLNVSAVPTTDLVSNPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 94 DYFSPSHPLLLVSFARSGNSPESVAAVELANQFVPECYHLSITCNEAGSLYQNAVDSDNACALLMPAETHDRGFAMTSSI 173
Cdd:TIGR02815 86 QYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRSFAMTSSF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 174 TTMMASCLAVFAPETINSKTFRDVSDRCQAILTS-LGDFSPGVFGNEPWKRIVYLGSGGLQGAARESALKVLELTAGKLA 252
Cdd:TIGR02815 166 SCMTLATLAVLGPETIESQTEERFADAALCILESgQWDFSEGVLGYAPWERIVYLGSGGLQGLARESALKVLELTAGKVM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 253 AFYDSPTGFRHGPKSLVDNETLVVVFVSSHPYTRQYDRDLLAELRRDRQAMRVVAIAAETDPVIEAGPHILLPPSRSFND 332
Cdd:TIGR02815 246 AFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPSRHFID 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 505384858 333 MEQAFCFLMYAQVFALTQSLHVGNTPDTPSASGTVNRVVQGVVIHPW 379
Cdd:TIGR02815 326 VELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
14-374 |
2.29e-113 |
|
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: 333.79 E-value: 2.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 14 EKEIRQQPASWLRSLnniDNLRASIDSFLTPLLRKPDLRIVLTGAGTSAFIGDIIAPWLASHTGKNITAIPTTDLVTNPm 93
Cdd:COG2222 1 AREIAQQPEAWRRAL---AALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 94 DYFSPShPLLLVSFARSGNSPESVAAVELANQFvpECYHLSITCNEAGSLYQNAvdsdnACALLMPAeTHDRGFAMTSSI 173
Cdd:COG2222 77 AYLKLE-GTLVVAISRSGNSPEVVAALELAKAR--GARTLAITNNPDSPLAEAA-----DRVLPLPA-GPEKSVAATKSF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 174 TTMMASCLAVFAPETINS---KTFRDVSDRCQAILTSLGDFSPGVfGNEPWKRIVYLGSGGLQGAARESALKVLELTAGK 250
Cdd:COG2222 148 TTMLLALLALLAAWGGDDallAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAGH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 251 laAFYDSPTGFRHGPKSLVDNETLVVVFVSSHPyTRQYDRDLLAELRRDrqAMRVVAIAAETDPVIEagphilLPPSRSF 330
Cdd:COG2222 227 --AEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRAL--GARVVAIGAEDDAAIT------LPAIPDL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 505384858 331 NDMEQAFCFLMYAQVFALTQSLHVGNTPDTPSAsgtVNRVVQGV 374
Cdd:COG2222 296 HDALDPLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
224-374 |
1.30e-93 |
|
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: 276.82 E-value: 1.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 224 IVYLGSGGLQGAARESALKVLELTAGKLAAFYDSPTGFRHGPKSLVDNETLVVVFVSSHPYTRQYDRDLLAELRRDRQAM 303
Cdd:cd05010 1 VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505384858 304 RVVAIAAETDPVIEAGPHILLPPSRSFNDMEQAFCFLMYAQVFALTQSLHVGNTPDTPSASGTVNRVVQGV 374
Cdd:cd05010 81 RVIAISPESDAGIEDNSHYYLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
45-184 |
9.84e-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: 78.88 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 45 LLRKPDlRIVLTGAGTSAFIGDIIAPWLASHTGKNITAIPTTDLVTNPMDYFSPSHPLLLVSFarSGNSPESVAAVELAN 124
Cdd:pfam01380 1 LLAKAK-RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISY--SGETKDLLAAAELAK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 125 QFVPECyhLSITCNEAGSLYQNAvdsdnACALLMPAETHDrGFAMTSSITTMMASCLAVF 184
Cdd:pfam01380 78 ARGAKI--IAITDSPGSPLAREA-----DHVLYINAGPET-GVASTKSITAQLAALDALA 129
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
14-361 |
1.83e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 50.02 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 14 EKEIRQQPASWLRSLNNIDNLR--------ASIDSFLTPLLRKPDLriVLTGAGTSAFIGDIIAPWLAS-HTGKNITAIP 84
Cdd:PTZ00295 280 LKEIFEQPIALSRALNNGGRLSgynnrvklGGLDQYLEELLNIKNL--ILVGCGTSYYAALFAASIMQKlKCFNTVQVID 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 85 TTDLvtNPMDYFSPSHPLLLVSfaRSGNSPESVAAVELANQFvpECYHLSITcNEAGSLYQNAVDsdnaCALLMPAeTHD 164
Cdd:PTZ00295 358 ASEL--TLYRLPDEDAGVIFIS--QSGETLDVVRALNLADEL--NLPKISVV-NTVGSLIARSTD----CGVYLNA-GRE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 165 RGFAMTSSITTMMaSCLAVFAPETINSKTFRDVSDRCQAILTSLGDFsPGVFG------NEPWKRI---------VY-LG 228
Cdd:PTZ00295 426 VAVASTKAFTSQV-TVLSLIALWFAQNKEYSCSNYKCSSLINSLHRL-PTYIGmtlkscEEQCKRIaeklknaksMFiLG 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 229 SGGLQGAARESALKVLELTagklaafYDSPTGF-----RHGPKSLVDNE--TLVVVFVSSHPYtrQYDRDLLAELRRDRQ 301
Cdd:PTZ00295 504 KGLGYPIALEGALKIKEIT-------YIHAEGFsggalKHGPFALIDKEknTPVILIILDDEH--KELMINAAEQVKARG 574
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 302 AmRVVAIAAETDPVIEAGPHILLPPSrsfNDMEQAFCFLMYAQVFALTQSLHVGNTPDTP 361
Cdd:PTZ00295 575 A-YIIVITDDEDLVKDFADEIILIPS---NGPLTALLAVIPLQLLAYEIAILRGINPDKP 630
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| agaS_fam |
TIGR02815 |
putative sugar isomerase, AgaS family; Some members of this protein family are found in ... |
14-379 |
0e+00 |
|
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: 608.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 14 EKEIRQQPASWLRSLNNIDNLRASIDSFLTPLLRKPDLRIVLTGAGTSAFIGDIIAPWLASHTGKNITAIPTTDLVTNPM 93
Cdd:TIGR02815 6 AREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGLNVSAVPTTDLVSNPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 94 DYFSPSHPLLLVSFARSGNSPESVAAVELANQFVPECYHLSITCNEAGSLYQNAVDSDNACALLMPAETHDRGFAMTSSI 173
Cdd:TIGR02815 86 QYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRSFAMTSSF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 174 TTMMASCLAVFAPETINSKTFRDVSDRCQAILTS-LGDFSPGVFGNEPWKRIVYLGSGGLQGAARESALKVLELTAGKLA 252
Cdd:TIGR02815 166 SCMTLATLAVLGPETIESQTEERFADAALCILESgQWDFSEGVLGYAPWERIVYLGSGGLQGLARESALKVLELTAGKVM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 253 AFYDSPTGFRHGPKSLVDNETLVVVFVSSHPYTRQYDRDLLAELRRDRQAMRVVAIAAETDPVIEAGPHILLPPSRSFND 332
Cdd:TIGR02815 246 AFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPSRHFID 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 505384858 333 MEQAFCFLMYAQVFALTQSLHVGNTPDTPSASGTVNRVVQGVVIHPW 379
Cdd:TIGR02815 326 VELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
14-374 |
2.29e-113 |
|
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: 333.79 E-value: 2.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 14 EKEIRQQPASWLRSLnniDNLRASIDSFLTPLLRKPDLRIVLTGAGTSAFIGDIIAPWLASHTGKNITAIPTTDLVTNPm 93
Cdd:COG2222 1 AREIAQQPEAWRRAL---AALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 94 DYFSPShPLLLVSFARSGNSPESVAAVELANQFvpECYHLSITCNEAGSLYQNAvdsdnACALLMPAeTHDRGFAMTSSI 173
Cdd:COG2222 77 AYLKLE-GTLVVAISRSGNSPEVVAALELAKAR--GARTLAITNNPDSPLAEAA-----DRVLPLPA-GPEKSVAATKSF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 174 TTMMASCLAVFAPETINS---KTFRDVSDRCQAILTSLGDFSPGVfGNEPWKRIVYLGSGGLQGAARESALKVLELTAGK 250
Cdd:COG2222 148 TTMLLALLALLAAWGGDDallAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAGH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 251 laAFYDSPTGFRHGPKSLVDNETLVVVFVSSHPyTRQYDRDLLAELRRDrqAMRVVAIAAETDPVIEagphilLPPSRSF 330
Cdd:COG2222 227 --AEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRAL--GARVVAIGAEDDAAIT------LPAIPDL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 505384858 331 NDMEQAFCFLMYAQVFALTQSLHVGNTPDTPSAsgtVNRVVQGV 374
Cdd:COG2222 296 HDALDPLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
224-374 |
1.30e-93 |
|
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: 276.82 E-value: 1.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 224 IVYLGSGGLQGAARESALKVLELTAGKLAAFYDSPTGFRHGPKSLVDNETLVVVFVSSHPYTRQYDRDLLAELRRDRQAM 303
Cdd:cd05010 1 VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505384858 304 RVVAIAAETDPVIEAGPHILLPPSRSFNDMEQAFCFLMYAQVFALTQSLHVGNTPDTPSASGTVNRVVQGV 374
Cdd:cd05010 81 RVIAISPESDAGIEDNSHYYLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
52-184 |
2.82e-23 |
|
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: 93.72 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 52 RIVLTGAGTSAFIGDIIAPWLASHTGKNITAIPTTdlvtnPMDYFSP--SHPLLLVSFARSGNSPESVAAVELANQfvpE 129
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAAS-----EFRYRRPllDEDTLVIAISQSGETADTLAALRLAKE---K 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 505384858 130 CYHLSITCNEAGSLYQNAVDsDNACALLMPAETHDRGFAMTSSITTMMASCLAVF 184
Cdd:cd05008 73 GAKTVAITNVVGSTLAREAD-YVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
219-361 |
3.51e-18 |
|
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: 80.77 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 219 EPWKRIVYLGSGGLQGAARESALKVLElTAGKLAAFYdsPTG-FRHGPKSLVDNETLVVVFVSSHPyTRQYDRDLLAELr 297
Cdd:cd05009 11 KEAKSFYVLGRGPNYGTALEGALKLKE-TSYIHAEAY--SAGeFKHGPIALVDEGTPVIFLAPEDR-LEEKLESLIKEV- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505384858 298 RDRQAmRVVAIAAETDPVIEAGPHILLPPSrsfNDMEQAFCFLMYAQVFALTQSLHVGNTPDTP 361
Cdd:cd05009 86 KARGA-KVIVITDDGDAKDLADVVIRVPAT---VEELSPLLYIVPLQLLAYHLAVARGIDPDKP 145
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
45-184 |
9.84e-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: 78.88 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 45 LLRKPDlRIVLTGAGTSAFIGDIIAPWLASHTGKNITAIPTTDLVTNPMDYFSPSHPLLLVSFarSGNSPESVAAVELAN 124
Cdd:pfam01380 1 LLAKAK-RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISY--SGETKDLLAAAELAK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 125 QFVPECyhLSITCNEAGSLYQNAvdsdnACALLMPAETHDrGFAMTSSITTMMASCLAVF 184
Cdd:pfam01380 78 ARGAKI--IAITDSPGSPLAREA-----DHVLYINAGPET-GVASTKSITAQLAALDALA 129
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
221-330 |
2.70e-13 |
|
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: 66.17 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 221 WKRIVYLGSGGLQGAARESALKvLELTAGKLAAFYDSPTgFRHGPKSLVDNETLVVVFvSSHPYTRQYDRdlLAELRRDR 300
Cdd:pfam01380 5 AKRIFVIGRGTSYAIALELALK-FEEIGYKVVEVELASE-LRHGVLALVDEDDLVIAI-SYSGETKDLLA--AAELAKAR 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 505384858 301 QAMRVV-------AIAAETDPVIE--AGPHILLPPSRSF 330
Cdd:pfam01380 80 GAKIIAitdspgsPLAREADHVLYinAGPETGVASTKSI 118
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
224-310 |
5.59e-11 |
|
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: 58.54 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 224 IVYLGSGGLQGAARESALKVLELTagKLAAFYDSPTGFRHGPKSLVDNETLVVVFVSSHPYTRqYDRDLLAELRrdRQAM 303
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELT--GIEVVALIATELEHASLLSLLRKGDVVIALSYSGRTE-ELLAALEIAK--ELGI 75
|
....*..
gi 505384858 304 RVVAIAA 310
Cdd:cd04795 76 PVIAITD 82
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
52-183 |
6.11e-09 |
|
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: 53.70 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 52 RIVLTGAGTSAFIGDIIAPWLAShtgkniTAIPTTDLvtNPMDYF-------SPSHPLLLVSfaRSGNSPESVAAVELAN 124
Cdd:cd05014 2 KVVVTGVGKSGHIARKIAATLSS------TGTPAFFL--HPTEALhgdlgmvTPGDVVIAIS--NSGETDELLNLLPHLK 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505384858 125 QFvpECYHLSITCNEAGSLYQNavdSDNACALLMPAETHDRGFAMTSSITTMMAS--CLAV 183
Cdd:cd05014 72 RR--GAPIIAITGNPNSTLAKL---SDVVLDLPVEEEACPLGLAPTTSTTAMLALgdALAV 127
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
14-361 |
1.83e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 50.02 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 14 EKEIRQQPASWLRSLNNIDNLR--------ASIDSFLTPLLRKPDLriVLTGAGTSAFIGDIIAPWLAS-HTGKNITAIP 84
Cdd:PTZ00295 280 LKEIFEQPIALSRALNNGGRLSgynnrvklGGLDQYLEELLNIKNL--ILVGCGTSYYAALFAASIMQKlKCFNTVQVID 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 85 TTDLvtNPMDYFSPSHPLLLVSfaRSGNSPESVAAVELANQFvpECYHLSITcNEAGSLYQNAVDsdnaCALLMPAeTHD 164
Cdd:PTZ00295 358 ASEL--TLYRLPDEDAGVIFIS--QSGETLDVVRALNLADEL--NLPKISVV-NTVGSLIARSTD----CGVYLNA-GRE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 165 RGFAMTSSITTMMaSCLAVFAPETINSKTFRDVSDRCQAILTSLGDFsPGVFG------NEPWKRI---------VY-LG 228
Cdd:PTZ00295 426 VAVASTKAFTSQV-TVLSLIALWFAQNKEYSCSNYKCSSLINSLHRL-PTYIGmtlkscEEQCKRIaeklknaksMFiLG 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 229 SGGLQGAARESALKVLELTagklaafYDSPTGF-----RHGPKSLVDNE--TLVVVFVSSHPYtrQYDRDLLAELRRDRQ 301
Cdd:PTZ00295 504 KGLGYPIALEGALKIKEIT-------YIHAEGFsggalKHGPFALIDKEknTPVILIILDDEH--KELMINAAEQVKARG 574
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 302 AmRVVAIAAETDPVIEAGPHILLPPSrsfNDMEQAFCFLMYAQVFALTQSLHVGNTPDTP 361
Cdd:PTZ00295 575 A-YIIVITDDEDLVKDFADEIILIPS---NGPLTALLAVIPLQLLAYEIAILRGINPDKP 630
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
222-361 |
1.36e-03 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 40.63 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384858 222 KRIVYLGSGGLQGAARESALKVLELT--------AGKLaafydsptgfRHGPKSLVDNETLVVVFVsshPYTRQYDRDLL 293
Cdd:PTZ00394 527 SSILVLGRGYDLATAMEAALKVKELSyvhtegihSGEL----------KHGPLALIDETSPVLAMC---THDKHFGLSKS 593
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505384858 294 AELRRDRQAMRVVAIAAETDPVIE-AGPHILLPPSRSfnDMEQAFCFLMYAQVFALTQSLHVGNTPDTP 361
Cdd:PTZ00394 594 AVQQVKARGGAVVVFATEVDAELKaAASEIVLVPKTV--DCLQCVVNVIPFQLLAYYMALLRGNNVDCP 660
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
52-123 |
6.71e-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: 36.09 E-value: 6.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505384858 52 RIVLTGAGTSAFIGDIIAPWLASHTGKNITAIpttdlvtnpMDYFSP---SHPLLLVSFARSGNSPESVAAVELA 123
Cdd:cd05017 1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYVV---------KDYTLPafvDRKTLVIAVSYSGNTEETLSAVEQA 66
|
|
| |
