|
Name |
Accession |
Description |
Interval |
E-value |
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
18-331 |
2.22e-35 |
|
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: 131.94 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 18 LERSSELVAQLVDIFQSGSFDALRIVASGSSRHAADCARDYLQDALQMQVSVVTP-EAFVDFEHTYPQHVLNIAVSQSGY 96
Cdd:COG2222 15 LAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPsELVVYPAYLKLEGTLVVAISRSGN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 97 STNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVE-SV----DFVTLgvevLVEYLVLFGIYGGQArgtid 171
Cdd:COG2222 95 SPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEkSVaatkSFTTM----LLALLALLAAWGGDD----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 172 akGVAQRLDDLREAIHAnavMCKTAEAYVQDHMLELSEHtpAMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHG 251
Cdd:COG2222 166 --ALLAALDALPAALEA---ALAADWPAAALAALADAER--VVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 252 PEMQITPGYLVFIVDDPQGSERL-ANIADALSNVTTKTVLLTAHPKGRAHEVAVPQVAPLLSAIPNLVFFQTIAAMIAER 330
Cdd:COG2222 239 PKSLVDPGTLVVVLASEDPTRELdLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALALA 318
|
.
gi 2438385571 331 L 331
Cdd:COG2222 319 R 319
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
42-143 |
3.48e-17 |
|
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: 76.77 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 42 IVASGSSRHAADCARDYLQDALQMQVSVVTPEAFVDFEHTYPQHVLNIAVSQSGYSTNTIAALDYMRAHDMAAVALTANV 121
Cdd:cd05008 4 IVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVV 83
|
90 100
....*....|....*....|...
gi 2438385571 122 EAPIKEHADIVLDYGVGVE-SVD 143
Cdd:cd05008 84 GSTLAREADYVLYLRAGPEiSVA 106
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
40-328 |
4.56e-10 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 61.19 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 40 LRIVASGSSRHAADCARDYLQdALQM--QVSVVTPEAFvdFEHTYP-QHVLNIAVSQSGYSTNTIAALDYMRAHDMAAVA 116
Cdd:PTZ00295 325 LILVGCGTSYYAALFAASIMQ-KLKCfnTVQVIDASEL--TLYRLPdEDAGVIFISQSGETLDVVRALNLADELNLPKIS 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 117 LTANVEAPIKEHAD--IVLDYG--VGVESVDFVTlgVEVLVeyLVLFGIYGGQAR-GTIDAKGVAQRLDDLREAIHANAV 191
Cdd:PTZ00295 402 VVNTVGSLIARSTDcgVYLNAGreVAVASTKAFT--SQVTV--LSLIALWFAQNKeYSCSNYKCSSLINSLHRLPTYIGM 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 192 MCKTAEAYVQDHMLELSEHTPAMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHGP-----EMQITPGYLVfIVD 266
Cdd:PTZ00295 478 TLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPfalidKEKNTPVILI-ILD 556
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2438385571 267 DpQGSERLANIADALSNVTTKTVLLTAHP---KGRAHE-VAVPQ---VAPLLSAIPnlvfFQTIAAMIA 328
Cdd:PTZ00295 557 D-EHKELMINAAEQVKARGAYIIVITDDEdlvKDFADEiILIPSngpLTALLAVIP----LQLLAYEIA 620
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
42-134 |
2.11e-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: 43.83 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 42 IVASGSSRHAADCARDYLQDALQMQVSVVTPEAFVD--FEHTYPQHVLnIAVSQSGYSTNTIAALDYMRAHDMAAVALTA 119
Cdd:pfam01380 10 VIGRGTSYAIALELALKFEEIGYKVVEVELASELRHgvLALVDEDDLV-IAISYSGETKDLLAAAELAKARGAKIIAITD 88
|
90
....*....|....*
gi 2438385571 120 NVEAPIKEHADIVLD 134
Cdd:pfam01380 89 SPGSPLAREADHVLY 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
18-331 |
2.22e-35 |
|
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: 131.94 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 18 LERSSELVAQLVDIFQSGSFDALRIVASGSSRHAADCARDYLQDALQMQVSVVTP-EAFVDFEHTYPQHVLNIAVSQSGY 96
Cdd:COG2222 15 LAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPsELVVYPAYLKLEGTLVVAISRSGN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 97 STNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVE-SV----DFVTLgvevLVEYLVLFGIYGGQArgtid 171
Cdd:COG2222 95 SPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEkSVaatkSFTTM----LLALLALLAAWGGDD----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 172 akGVAQRLDDLREAIHAnavMCKTAEAYVQDHMLELSEHtpAMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHG 251
Cdd:COG2222 166 --ALLAALDALPAALEA---ALAADWPAAALAALADAER--VVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 252 PEMQITPGYLVFIVDDPQGSERL-ANIADALSNVTTKTVLLTAHPKGRAHEVAVPQVAPLLSAIPNLVFFQTIAAMIAER 330
Cdd:COG2222 239 PKSLVDPGTLVVVLASEDPTRELdLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALALA 318
|
.
gi 2438385571 331 L 331
Cdd:COG2222 319 R 319
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
42-143 |
3.48e-17 |
|
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: 76.77 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 42 IVASGSSRHAADCARDYLQDALQMQVSVVTPEAFVDFEHTYPQHVLNIAVSQSGYSTNTIAALDYMRAHDMAAVALTANV 121
Cdd:cd05008 4 IVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVV 83
|
90 100
....*....|....*....|...
gi 2438385571 122 EAPIKEHADIVLDYGVGVE-SVD 143
Cdd:cd05008 84 GSTLAREADYVLYLRAGPEiSVA 106
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
206-331 |
4.92e-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: 77.30 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 206 ELSEHTPAMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHGPEMQITPGYLVFIVDDPQGSERLA-NIADALSNV 284
Cdd:cd05009 9 KLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLeSLIKEVKAR 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2438385571 285 TTKTVLLTA---HPKGRAHEVAVPQVAPLLSAIPNLVFFQTIAAMIAERL 331
Cdd:cd05009 89 GAKVIVITDdgdAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVAR 138
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
36-315 |
1.79e-11 |
|
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: 65.42 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 36 SFDALRIVASGSSRHAADCARDYLQDALQMQVSVVtpeafVDFEHTYPQHVLN-----IAVSQSGYSTNTIAALDYMRAH 110
Cdd:COG0449 293 NIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVE-----IASEFRYRDPVVDpgtlvIAISQSGETADTLAALREAKEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 111 DMAAVALTANVEAPIKEHADIVLDYGVGVE-SV----DFVTlgvEVLVeyLVLFGIYGGQARGTIDAKGVAQRLDDLR-- 183
Cdd:COG0449 368 GAKVLAICNVVGSTIARESDAVLYTHAGPEiGVastkAFTT---QLAA--LYLLALYLARARGTLSAEEEAELLEELRkl 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 184 -----EAIHANAVMCKTAEayvqdhmlELSEHTPAMVVGNGPNYGVAEEAALKLSEtikIPAMHHEG---EEFVHGPEMQ 255
Cdd:COG0449 443 pekieEVLDLEEQIEELAE--------KYADARNALFLGRGINYPVALEGALKLKE---ISYIHAEGyaaGELKHGPIAL 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2438385571 256 ITPGYLVFIVdDPQGS--ERLaniadaLSNVT------TKTVLLTAHPKGRAHEVA-----VPQV----APLLSAIP 315
Cdd:COG0449 512 IDEGMPVVAI-APQDElyEKT------LSNIQevkargGKVIAIADEGDEEVEELAddvieVPEVdellAPILAVVP 581
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
40-328 |
4.56e-10 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 61.19 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 40 LRIVASGSSRHAADCARDYLQdALQM--QVSVVTPEAFvdFEHTYP-QHVLNIAVSQSGYSTNTIAALDYMRAHDMAAVA 116
Cdd:PTZ00295 325 LILVGCGTSYYAALFAASIMQ-KLKCfnTVQVIDASEL--TLYRLPdEDAGVIFISQSGETLDVVRALNLADELNLPKIS 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 117 LTANVEAPIKEHAD--IVLDYG--VGVESVDFVTlgVEVLVeyLVLFGIYGGQAR-GTIDAKGVAQRLDDLREAIHANAV 191
Cdd:PTZ00295 402 VVNTVGSLIARSTDcgVYLNAGreVAVASTKAFT--SQVTV--LSLIALWFAQNKeYSCSNYKCSSLINSLHRLPTYIGM 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 192 MCKTAEAYVQDHMLELSEHTPAMVVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHGP-----EMQITPGYLVfIVD 266
Cdd:PTZ00295 478 TLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPfalidKEKNTPVILI-ILD 556
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2438385571 267 DpQGSERLANIADALSNVTTKTVLLTAHP---KGRAHE-VAVPQ---VAPLLSAIPnlvfFQTIAAMIA 328
Cdd:PTZ00295 557 D-EHKELMINAAEQVKARGAYIIVITDDEdlvKDFADEiILIPSngpLTALLAVIP----LQLLAYEIA 620
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
20-252 |
7.99e-10 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 60.44 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 20 RSSELVAQLVDIFQSGSFDALRIVASGSSRHAADCARdYLqdaLQMQVSVVTpEAFVDFEHTYPQHVLN-----IAVSQS 94
Cdd:PRK00331 272 RLDELGEGELADEDLKKIDRIYIVACGTSYHAGLVAK-YL---IESLAGIPV-EVEIASEFRYRDPVLSpktlvIAISQS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 95 GYSTNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVEsvdfvtLGV--------EVLVEYLvlFGIYGGQA 166
Cdd:PRK00331 347 GETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPE------IGVastkaftaQLAVLYL--LALALAKA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 167 RGTIDAKGVAQRLDDLREAIHANAVMCKTAEAyvqdhMLELSEH----TPAMVVGNGPNYGVAEEAALKLSEtikIPAMH 242
Cdd:PRK00331 419 RGTLSAEEEADLVHELRELPALIEQVLDLKEQ-----IEELAEDfadaRNALFLGRGVDYPVALEGALKLKE---ISYIH 490
|
250
....*....|...
gi 2438385571 243 HEG---EEFVHGP 252
Cdd:PRK00331 491 AEGyaaGELKHGP 503
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
41-252 |
2.12e-09 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 58.99 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 41 RIV--ASGSSRHAADCARDYLQDALQMQVSVVTPEAFVDFEHTYPQHVLNIAVSQSGYSTNTIAALDYMRAHDMAAVALT 118
Cdd:PLN02981 365 RIVfiGCGTSYNAALAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGIT 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 119 ANVEAPI--KEHADIVLDYG--VGVESVDFVTLGVEVLVEYLVLFG---IYGGQARGTIdAKGVAQRLDDLREAIHANAV 191
Cdd:PLN02981 445 NTVGSAIsrGTHCGVHINAGaeIGVASTKAYTSQIVAMTMLALALGedsISSRSRREAI-IDGLFDLPNKVREVLKLDQE 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2438385571 192 MCKTAEayvqdhmlELSEHTPAMVVGNGPNYGVAEEAALKLSEtikIPAMHHEG---EEFVHGP 252
Cdd:PLN02981 524 MKELAE--------LLIDEQSLLVFGRGYNYATALEGALKVKE---VALMHSEGilaGEMKHGP 576
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
40-330 |
2.51e-08 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 55.65 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 40 LRIVASGSSRHAADCARDYLQDALQMQVSVVTPEAFVDFEHTYPQHVLNIAVSQSGYSTNTIAALDYMRAHDMAAVALTA 119
Cdd:PTZ00394 357 ILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 120 NVEAPIKEHAD--IVLDYGV--GVESVDFVTLGVEVLVeyLVLFGIYGGQARgtiDAKGVAQRLDDLREAIHANAVMCKT 195
Cdd:PTZ00394 437 VVGSSISRLTHyaIHLNAGVevGVASTKAYTSQVVVLT--LVALLLSSDSVR---LQERRNEIIRGLAELPAAISECLKI 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 196 AEAYVQDHMLELSEHTPAMVVGNGPNYGVAEEAALKLSEtikIPAMHHEG---EEFVHGPEMQI--TPGYLVFIVDDP-- 268
Cdd:PTZ00394 512 THDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKE---LSYVHTEGihsGELKHGPLALIdeTSPVLAMCTHDKhf 588
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2438385571 269 -QGSERLANIADALSNVTTKTVLLTAHPKGRAHE-VAVPQVAPLLSAIPNLVFFQTIAAMIAER 330
Cdd:PTZ00394 589 gLSKSAVQQVKARGGAVVVFATEVDAELKAAASEiVLVPKTVDCLQCVVNVIPFQLLAYYMALL 652
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
42-133 |
3.33e-06 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 48.00 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 42 IVASGSSRHAADcardYLQDALQM---QVSVVTPEAFVDFEHTY---PQHVLnIAVSQSGYSTNTIAALDYMRAHDMAAV 115
Cdd:COG1737 139 IFGVGASAPVAE----DLAYKLLRlgkNVVLLDGDGHLQAESAAllgPGDVV-IAISFSGYTRETLEAARLAKERGAKVI 213
|
90
....*....|....*...
gi 2438385571 116 ALTANVEAPIKEHADIVL 133
Cdd:COG1737 214 AITDSPLSPLAKLADVVL 231
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
16-137 |
5.14e-06 |
|
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: 45.68 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 16 ENLERSSELVAQLVDIFqsgsfdalrIVASGSSRHAADcardYLQDALQM---QVSVVT--PEAFVDFEHTYPQHVLnIA 90
Cdd:cd05013 1 EALEKAVDLLAKARRIY---------IFGVGSSGLVAE----YLAYKLLRlgkPVVLLSdpHLQLMSAANLTPGDVV-IA 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2438385571 91 VSQSGYSTNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGV 137
Cdd:cd05013 67 ISFSGETKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSS 113
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
42-134 |
2.11e-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: 43.83 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 42 IVASGSSRHAADCARDYLQDALQMQVSVVTPEAFVD--FEHTYPQHVLnIAVSQSGYSTNTIAALDYMRAHDMAAVALTA 119
Cdd:pfam01380 10 VIGRGTSYAIALELALKFEEIGYKVVEVELASELRHgvLALVDEDDLV-IAISYSGETKDLLAAAELAKARGAKIIAITD 88
|
90
....*....|....*
gi 2438385571 120 NVEAPIKEHADIVLD 134
Cdd:pfam01380 89 SPGSPLAREADHVLY 103
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
215-295 |
2.28e-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: 40.75 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 215 VVGNGPNYGVAEEAALKLSETIKIPAMHHEGEEFVHGPEMQITPGYLVFIVDDPQGSERLANIADALSNVTTKTVLLTAH 294
Cdd:pfam01380 10 VIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDS 89
|
.
gi 2438385571 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 |
1.15e-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: 38.33 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2438385571 77 DFEHTYPQHV----LNIAVSQSGYSTNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYGVGVESVD 143
Cdd:cd05710 36 EFLHTGPKRLteksVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIVYGFEIDAVE 106
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
18-259 |
1.27e-03 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 40.37 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 18 LERSSELVAQLVDIFQSGSFDALRIVASGSSRHAADCARDYLQDALQMQVSVVTPEAFVD-FEHTYPQHVLNIAVSQSGY 96
Cdd:PRK11382 25 LSHDVPLVHAIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDnTPYRLDDRCAVIGVSDYGK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 97 STNTIAALDYMRAHDMAAVALTANVEAPIKEHADIVLDYgvgveSVDFVtLGVEVLVEYLVLFGIYGGQARGTidakGVA 176
Cdd:PRK11382 105 TEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDY-----QADCI-WEIHLLLCYSVVLEMITRLAPNA----EIG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438385571 177 QRLDDLREAIHANAVMCKTAEAYVQdHMLELSEHTPAM-VVGNGPNYGVA-EEAALKLSETIKIPAMHHEGEEFVHGPEM 254
Cdd:PRK11382 175 KIKNDLKQLPNALGHLVRTWEEKGR-QLGELASQWPMIyTVAAGPLRPLGyKEGIVTLMEFTWTHGCVIESGEFRHGPLE 253
|
....*
gi 2438385571 255 QITPG 259
Cdd:PRK11382 254 IVEPG 258
|
|
| |
