|
Name |
Accession |
Description |
Interval |
E-value |
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
18-331 |
4.75e-34 |
|
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: 128.48 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 18 LERSSELVAQLVDIFQSGSFDALRIVASGSSRHAADCTRDFLQDTLQMQVSVVTP-EAFVDFEHTYPQHALNIAVSQSGY 96
Cdd:COG2222 15 LAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPsELVVYPAYLKLEGTLVVAISRSGN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 97 STNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVE-SV----DFVTLgvevLVEYLVLFGIYGGQArgtvd 171
Cdd:COG2222 95 SPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEkSVaatkSFTTM----LLALLALLAAWGGDD----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 172 akGVAQRLDGLREAIQAnavMCKTAEAYVQDHMLELSEHMpaMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHG 251
Cdd:COG2222 166 --ALLAALDALPAALEA---ALAADWPAAALAALADAERV--VFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 252 PeMQIV-PGYLVFIVDDPQGSERL-ANIADALSNVTTKTVLLTAHPRGKAHEVAVPQVVPLLSAIPNLVFFQTIAAMIAE 329
Cdd:COG2222 239 P-KSLVdPGTLVVVLASEDPTRELdLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALAL 317
|
..
gi 1469906302 330 RL 331
Cdd:COG2222 318 AR 319
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
213-331 |
1.79e-16 |
|
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: 75.76 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 213 AMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHGPeMQIV-PGYLVFIVDDPQGSERLA-NIADALSNVTTKTVL 290
Cdd:cd05009 16 FYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGP-IALVdEGTPVIFLAPEDRLEEKLeSLIKEVKARGAKVIV 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1469906302 291 LTAHPRGKA---HEVAVPQVVPLLSAIPNLVFFQTIAAMIAERL 331
Cdd:cd05009 95 ITDDGDAKDladVVIRVPATVEELSPLLYIVPLQLLAYHLAVAR 138
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
41-324 |
7.59e-11 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 63.62 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 41 RIV--ASGSSRHAADCTRDFLQDTLQMQVSVVTPEAFVDFEHTYPQHALNIAVSQSGYSTNTIAALDYMRAHDMAAVALT 118
Cdd:PLN02981 365 RIVfiGCGTSYNAALAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGIT 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 119 ANVEAPI--KEHADIVLDYG--VGVESVDFVTLGVEVLVEYLVLFG--IYGGQARGTVDAKGVAQRLDGLREAIQANAVM 192
Cdd:PLN02981 445 NTVGSAIsrGTHCGVHINAGaeIGVASTKAYTSQIVAMTMLALALGedSISSRSRREAIIDGLFDLPNKVREVLKLDQEM 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 193 CKTAEAYVQDHMLelsehmpaMVVGNGPNYGVAEEAALKLSEtikIPAMHHEG---EEFVHGPeMQIVPGYLVFIV---D 266
Cdd:PLN02981 525 KELAELLIDEQSL--------LVFGRGYNYATALEGALKVKE---VALMHSEGilaGEMKHGP-LALVDETLPIIViatR 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469906302 267 DPQGSERLANIADALSNVTTKTVLLT------AHPRGKAHEVAVPQVVPLLSAIPNLVFFQTIA 324
Cdd:PLN02981 593 DACFSKQQSVIQQLRARKGRLIVICSkgdassVCPSGGCRVIEVPQVEDCLQPVINIVPLQLLA 656
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
42-134 |
8.54e-05 |
|
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: 41.90 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 42 IVASGSSRHAADCTRDFLQDTLQMQVSVVTPEAFVDfehtypQHALN-------IAVSQSGYSTNTIAALDYMRAHDMAA 114
Cdd:pfam01380 10 VIGRGTSYAIALELALKFEEIGYKVVEVELASELRH------GVLALvdeddlvIAISYSGETKDLLAAAELAKARGAKI 83
|
90 100
....*....|....*....|
gi 1469906302 115 VALTANVEAPIKEHADIVLD 134
Cdd:pfam01380 84 IAITDSPGSPLAREADHVLY 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
18-331 |
4.75e-34 |
|
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: 128.48 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 18 LERSSELVAQLVDIFQSGSFDALRIVASGSSRHAADCTRDFLQDTLQMQVSVVTP-EAFVDFEHTYPQHALNIAVSQSGY 96
Cdd:COG2222 15 LAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPsELVVYPAYLKLEGTLVVAISRSGN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 97 STNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVE-SV----DFVTLgvevLVEYLVLFGIYGGQArgtvd 171
Cdd:COG2222 95 SPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEkSVaatkSFTTM----LLALLALLAAWGGDD----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 172 akGVAQRLDGLREAIQAnavMCKTAEAYVQDHMLELSEHMpaMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHG 251
Cdd:COG2222 166 --ALLAALDALPAALEA---ALAADWPAAALAALADAERV--VFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 252 PeMQIV-PGYLVFIVDDPQGSERL-ANIADALSNVTTKTVLLTAHPRGKAHEVAVPQVVPLLSAIPNLVFFQTIAAMIAE 329
Cdd:COG2222 239 P-KSLVdPGTLVVVLASEDPTRELdLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALAL 317
|
..
gi 1469906302 330 RL 331
Cdd:COG2222 318 AR 319
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
213-331 |
1.79e-16 |
|
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: 75.76 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 213 AMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHGPeMQIV-PGYLVFIVDDPQGSERLA-NIADALSNVTTKTVL 290
Cdd:cd05009 16 FYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGP-IALVdEGTPVIFLAPEDRLEEKLeSLIKEVKARGAKVIV 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1469906302 291 LTAHPRGKA---HEVAVPQVVPLLSAIPNLVFFQTIAAMIAERL 331
Cdd:cd05009 95 ITDDGDAKDladVVIRVPATVEELSPLLYIVPLQLLAYHLAVAR 138
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
42-143 |
4.79e-16 |
|
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: 73.69 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 42 IVASGSSRHAADCTRDFLQDTLQMQVSVVTPEAFVDFEHTYPQHALNIAVSQSGYSTNTIAALDYMRAHDMAAVALTANV 121
Cdd:cd05008 4 IVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVV 83
|
90 100
....*....|....*....|...
gi 1469906302 122 EAPIKEHADIVLDYGVGVE-SVD 143
Cdd:cd05008 84 GSTLAREADYVLYLRAGPEiSVA 106
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
41-324 |
7.59e-11 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 63.62 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 41 RIV--ASGSSRHAADCTRDFLQDTLQMQVSVVTPEAFVDFEHTYPQHALNIAVSQSGYSTNTIAALDYMRAHDMAAVALT 118
Cdd:PLN02981 365 RIVfiGCGTSYNAALAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGIT 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 119 ANVEAPI--KEHADIVLDYG--VGVESVDFVTLGVEVLVEYLVLFG--IYGGQARGTVDAKGVAQRLDGLREAIQANAVM 192
Cdd:PLN02981 445 NTVGSAIsrGTHCGVHINAGaeIGVASTKAYTSQIVAMTMLALALGedSISSRSRREAIIDGLFDLPNKVREVLKLDQEM 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 193 CKTAEAYVQDHMLelsehmpaMVVGNGPNYGVAEEAALKLSEtikIPAMHHEG---EEFVHGPeMQIVPGYLVFIV---D 266
Cdd:PLN02981 525 KELAELLIDEQSL--------LVFGRGYNYATALEGALKVKE---VALMHSEGilaGEMKHGP-LALVDETLPIIViatR 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469906302 267 DPQGSERLANIADALSNVTTKTVLLT------AHPRGKAHEVAVPQVVPLLSAIPNLVFFQTIA 324
Cdd:PLN02981 593 DACFSKQQSVIQQLRARKGRLIVICSkgdassVCPSGGCRVIEVPQVEDCLQPVINIVPLQLLA 656
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
89-252 |
7.71e-10 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 60.44 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 89 IAVSQSGYSTNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVEsvdfvtLGV--------EVLVEYLvlFG 160
Cdd:PRK00331 341 IAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPE------IGVastkaftaQLAVLYL--LA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 161 IYGGQARGTVDAKGVAQRLDGLREAIQANAVMCKTAEAyvqdhMLELSEHMP----AMVVGNGPNYGVAEEAALKLSEti 236
Cdd:PRK00331 413 LALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQ-----IEELAEDFAdarnALFLGRGVDYPVALEGALKLKE-- 485
|
170
....*....|....*....
gi 1469906302 237 kIPAMHHEG---EEFVHGP 252
Cdd:PRK00331 486 -ISYIHAEGyaaGELKHGP 503
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
40-330 |
3.99e-09 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 58.35 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 40 LRIVASGSSRHAADCTRDFLQDTLQMQVSVVTPEAFVDFEHTYPQHALNIAVSQSGYSTNTIAALDYMRAHDMAAVALTA 119
Cdd:PTZ00394 357 ILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 120 NVEAPIKEHAD--IVLDYG--VGVESVDFVTLGVEVLVeyLVLFGIYGGQARgtvDAKGVAQRLDGLREAIQANAVMCKT 195
Cdd:PTZ00394 437 VVGSSISRLTHyaIHLNAGveVGVASTKAYTSQVVVLT--LVALLLSSDSVR---LQERRNEIIRGLAELPAAISECLKI 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 196 AEAYVQDHMLELSEHMPAMVVGNGPNYGVAEEAALKLSEtikIPAMHHEG---EEFVHGPeMQIVPGYLVFIVDDPQGS- 271
Cdd:PTZ00394 512 THDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKE---LSYVHTEGihsGELKHGP-LALIDETSPVLAMCTHDKh 587
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469906302 272 -ERLANIADALSNVTTKTVLLTAHPRGKAHE-----VAVPQVVPLLSAIPNLVFFQTIAAMIAER 330
Cdd:PTZ00394 588 fGLSKSAVQQVKARGGAVVVFATEVDAELKAaaseiVLVPKTVDCLQCVVNVIPFQLLAYYMALL 652
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
40-328 |
5.98e-09 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 57.72 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 40 LRIVASGSSRHAADCTRDFLQdTLQM--QVSVVTPEAFvdFEHTYP-QHALNIAVSQSGYSTNTIAALDYMRAHDMAAVA 116
Cdd:PTZ00295 325 LILVGCGTSYYAALFAASIMQ-KLKCfnTVQVIDASEL--TLYRLPdEDAGVIFISQSGETLDVVRALNLADELNLPKIS 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 117 LTANVEAPIKEHAD--IVLDYG--VGVESVDFVTlgVEVLVeyLVLFGIYGGQAR-GTVDAKGVAQRLDGLREAIQANAV 191
Cdd:PTZ00295 402 VVNTVGSLIARSTDcgVYLNAGreVAVASTKAFT--SQVTV--LSLIALWFAQNKeYSCSNYKCSSLINSLHRLPTYIGM 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 192 MCKTAEAYVQD--HMLELSEHMpaMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHGP-----EMQIVPGYLVfI 264
Cdd:PTZ00295 478 TLKSCEEQCKRiaEKLKNAKSM--FILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPfalidKEKNTPVILI-I 554
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469906302 265 VDDpQGSERLANIADALSNVTTKTVLLTAHP---RGKAHE-VAVPQ---VVPLLSAIPnlvfFQTIAAMIA 328
Cdd:PTZ00295 555 LDD-EHKELMINAAEQVKARGAYIIVITDDEdlvKDFADEiILIPSngpLTALLAVIP----LQLLAYEIA 620
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
36-252 |
6.97e-09 |
|
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: 57.33 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 36 SFDALRIVASGSSRHAADCTRDFLQDTLQMQVSV------------VTPEAFVdfehtypqhalnIAVSQSGYSTNTIAA 103
Cdd:COG0449 293 NIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVeiasefryrdpvVDPGTLV------------IAISQSGETADTLAA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 104 LDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVE-SV----DFVTlgvEVLVeyLVLFGIYGGQARGTVDAKGVAQR 178
Cdd:COG0449 361 LREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEiGVastkAFTT---QLAA--LYLLALYLARARGTLSAEEEAEL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 179 LDGLR-------EAIQANAVMCKTAEAYVQdhmlelSEHmpAMVVGNGPNYGVAEEAALKLSEtikIPAMHHEG---EEF 248
Cdd:COG0449 436 LEELRklpekieEVLDLEEQIEELAEKYAD------ARN--ALFLGRGINYPVALEGALKLKE---ISYIHAEGyaaGEL 504
|
....
gi 1469906302 249 VHGP 252
Cdd:COG0449 505 KHGP 508
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
89-137 |
3.44e-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: 43.37 E-value: 3.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1469906302 89 IAVSQSGYSTNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGV 137
Cdd:cd05013 65 IAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSS 113
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
42-133 |
4.99e-05 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 44.53 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 42 IVASGSSRHAADctrdFLQDTLQM---QVSVVTPEAfvdfeHTYPQHALN-------IAVSQSGYSTNTIAALDYMRAHD 111
Cdd:COG1737 139 IFGVGASAPVAE----DLAYKLLRlgkNVVLLDGDG-----HLQAESAALlgpgdvvIAISFSGYTRETLEAARLAKERG 209
|
90 100
....*....|....*....|..
gi 1469906302 112 MAAVALTANVEAPIKEHADIVL 133
Cdd:COG1737 210 AKVIAITDSPLSPLAKLADVVL 231
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
42-134 |
8.54e-05 |
|
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: 41.90 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 42 IVASGSSRHAADCTRDFLQDTLQMQVSVVTPEAFVDfehtypQHALN-------IAVSQSGYSTNTIAALDYMRAHDMAA 114
Cdd:pfam01380 10 VIGRGTSYAIALELALKFEEIGYKVVEVELASELRH------GVLALvdeddlvIAISYSGETKDLLAAAELAKARGAKI 83
|
90 100
....*....|....*....|
gi 1469906302 115 VALTANVEAPIKEHADIVLD 134
Cdd:pfam01380 84 IAITDSPGSPLAREADHVLY 103
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
215-295 |
1.69e-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. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 38.05 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 215 VVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHGPEMQIVPGYLVFIVDDPQGSERLANIADALSNVTTKTVLLTAH 294
Cdd:pfam01380 10 VIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDS 89
|
.
gi 1469906302 295 P 295
Cdd:pfam01380 90 P 90
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
77-143 |
2.27e-03 |
|
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: 37.56 E-value: 2.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469906302 77 DFEHTYPQH----ALNIAVSQSGYSTNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVESVD 143
Cdd:cd05710 36 EFLHTGPKRltekSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIVYGFEIDAVE 106
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
18-135 |
3.74e-03 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 38.83 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469906302 18 LERSSELVAQLVDIFQSGSFDALRIVASGSSRHAADCTRDFLQDTLQMQVSVVTPEAFVD-FEHTYPQHALNIAVSQSGY 96
Cdd:PRK11382 25 LSHDVPLVHAIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDnTPYRLDDRCAVIGVSDYGK 104
|
90 100 110
....*....|....*....|....*....|....*....
gi 1469906302 97 STNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDY 135
Cdd:PRK11382 105 TEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDY 143
|
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