|
Name |
Accession |
Description |
Interval |
E-value |
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
11-295 |
2.92e-77 |
|
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: 238.64 E-value: 2.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 11 AEEVASQPDMWELAVSLAK-------KFDIARPGARMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEYL-----WE 78
Cdd:COG2222 1 AREIAQQPEAWRRALAALAaaiaallARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVvypayLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 79 RNYDVVVALTRSGTTTEILDTTERLK-GTTKLIGIVGDPNTPFVNMVDELVSLDFADEQSVVQTRFATSALALLRTGLGE 157
Cdd:COG2222 81 LEGTLVVAISRSGNSPEVVAALELAKaRGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 158 ---------DLTDVIAQARDALTSELPEAVI----NAEQYSFLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPM 224
Cdd:COG2222 161 wggddallaALDALPAALEAALAADWPAAALaalaDAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 225 SIAQPGRVTWQFGS------LLPELARDVKETGAHF------------------EHGYTDPMVELIRVHRATLETALERG 280
Cdd:COG2222 241 SLVDPGTLVVVLASedptreLDLDLAAELRALGARVvaigaeddaaitlpaipdLHDALDPLLLLVVAQRLALALALARG 320
|
330
....*....|....*
gi 2676403739 281 LNPDTPRNLTRSVIL 295
Cdd:COG2222 321 LDPDTPRHLNKVVKT 335
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
172-293 |
3.91e-25 |
|
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: 98.10 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 172 SELPEAVINAEQYSFLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPMSIAQPG-RVTW--QFGSLLP---ELAR 245
Cdd:cd05009 4 KELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGtPVIFlaPEDRLEEkleSLIK 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2676403739 246 DVKETGAH---------------------FEHGYTDPMVELIRVHRATLETALERGLNPDTPRNLTRSV 293
Cdd:cd05009 84 EVKARGAKvivitddgdakdladvvirvpATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSV 152
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
40-293 |
2.34e-18 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 85.07 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 40 MAVIGCGTSFYVAQAFAQLRERL-GFGQTDAFAASE---YLWERNYDVVVALTRSGtttEILDTTERLKGTTKL----IG 111
Cdd:PTZ00295 325 LILVGCGTSYYAALFAASIMQKLkCFNTVQVIDASEltlYRLPDEDAGVIFISQSG---ETLDVVRALNLADELnlpkIS 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 112 IVGDPNTPFVNMVDELVSLDFADEQSVVQTR-FATSALALLRTGLgedltdVIAQARDALTSE------------LPEAV 178
Cdd:PTZ00295 402 VVNTVGSLIARSTDCGVYLNAGREVAVASTKaFTSQVTVLSLIAL------WFAQNKEYSCSNykcsslinslhrLPTYI 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 179 -----INAEQYS-------------FLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPMSIAQPGRVTWQFGSLL 240
Cdd:PTZ00295 476 gmtlkSCEEQCKriaeklknaksmfILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEKNTPVILIIL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 241 PE--------LARDVKETGAHF---------------------EHGYTDPMVELIRVHRATLETALERGLNPDTPRNLTR 291
Cdd:PTZ00295 556 DDehkelminAAEQVKARGAYIivitddedlvkdfadeiilipSNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAK 635
|
..
gi 2676403739 292 SV 293
Cdd:PTZ00295 636 TV 637
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
39-126 |
2.46e-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: 43.06 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 39 RMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEYLWE-----RNYDVVVALTRSGTTTEILDTTERLKG-TTKLIGI 112
Cdd:pfam01380 7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvlalvDEDDLVIAISYSGETKDLLAAAELAKArGAKIIAI 86
|
90
....*....|....
gi 2676403739 113 VGDPNTPFVNMVDE 126
Cdd:pfam01380 87 TDSPGSPLAREADH 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
11-295 |
2.92e-77 |
|
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: 238.64 E-value: 2.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 11 AEEVASQPDMWELAVSLAK-------KFDIARPGARMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEYL-----WE 78
Cdd:COG2222 1 AREIAQQPEAWRRALAALAaaiaallARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVvypayLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 79 RNYDVVVALTRSGTTTEILDTTERLK-GTTKLIGIVGDPNTPFVNMVDELVSLDFADEQSVVQTRFATSALALLRTGLGE 157
Cdd:COG2222 81 LEGTLVVAISRSGNSPEVVAALELAKaRGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 158 ---------DLTDVIAQARDALTSELPEAVI----NAEQYSFLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPM 224
Cdd:COG2222 161 wggddallaALDALPAALEAALAADWPAAALaalaDAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 225 SIAQPGRVTWQFGS------LLPELARDVKETGAHF------------------EHGYTDPMVELIRVHRATLETALERG 280
Cdd:COG2222 241 SLVDPGTLVVVLASedptreLDLDLAAELRALGARVvaigaeddaaitlpaipdLHDALDPLLLLVVAQRLALALALARG 320
|
330
....*....|....*
gi 2676403739 281 LNPDTPRNLTRSVIL 295
Cdd:COG2222 321 LDPDTPRHLNKVVKT 335
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
172-293 |
3.91e-25 |
|
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: 98.10 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 172 SELPEAVINAEQYSFLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPMSIAQPG-RVTW--QFGSLLP---ELAR 245
Cdd:cd05009 4 KELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGtPVIFlaPEDRLEEkleSLIK 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2676403739 246 DVKETGAH---------------------FEHGYTDPMVELIRVHRATLETALERGLNPDTPRNLTRSV 293
Cdd:cd05009 84 EVKARGAKvivitddgdakdladvvirvpATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSV 152
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
39-155 |
2.33e-21 |
|
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: 87.17 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 39 RMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEYLWERN----YDVVVALTRSGTTTEILDTTERLKGT-TKLIGIV 113
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPlldeDTLVIAISQSGETADTLAALRLAKEKgAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2676403739 114 GDPNTPFVNMVDELVSLDFADEQSVVQT-RFATSALALLRTGL 155
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATkAFTSQLLALLLLAL 123
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
40-293 |
2.34e-18 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 85.07 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 40 MAVIGCGTSFYVAQAFAQLRERL-GFGQTDAFAASE---YLWERNYDVVVALTRSGtttEILDTTERLKGTTKL----IG 111
Cdd:PTZ00295 325 LILVGCGTSYYAALFAASIMQKLkCFNTVQVIDASEltlYRLPDEDAGVIFISQSG---ETLDVVRALNLADELnlpkIS 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 112 IVGDPNTPFVNMVDELVSLDFADEQSVVQTR-FATSALALLRTGLgedltdVIAQARDALTSE------------LPEAV 178
Cdd:PTZ00295 402 VVNTVGSLIARSTDCGVYLNAGREVAVASTKaFTSQVTVLSLIAL------WFAQNKEYSCSNykcsslinslhrLPTYI 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 179 -----INAEQYS-------------FLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPMSIAQPGRVTWQFGSLL 240
Cdd:PTZ00295 476 gmtlkSCEEQCKriaeklknaksmfILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEKNTPVILIIL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 241 PE--------LARDVKETGAHF---------------------EHGYTDPMVELIRVHRATLETALERGLNPDTPRNLTR 291
Cdd:PTZ00295 556 DDehkelminAAEQVKARGAYIivitddedlvkdfadeiilipSNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAK 635
|
..
gi 2676403739 292 SV 293
Cdd:PTZ00295 636 TV 637
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
39-226 |
1.88e-11 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 64.39 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 39 RMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEyLWERN-----YDVVVALTRSGTTTEILDTTERLKGTTKL-IGI 112
Cdd:PLN02981 365 RIVFIGCGTSYNAALAARPILEELSGVPVTMELASD-LLDRQgpiyrEDTAVFVSQSGETADTLRALEYAKENGALcVGI 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 113 VGDPNTPFVNMVDELVSLDFADEQSVVQTRFATS---ALALLRTGLGED--------------LTDVIAQARDAL----- 170
Cdd:PLN02981 444 TNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSqivAMTMLALALGEDsissrsrreaiidgLFDLPNKVREVLkldqe 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2676403739 171 TSELPEAVINAEQYSFLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPMSI 226
Cdd:PLN02981 524 MKELAELLIDEQSLLVFGRGYNYATALEGALKVKEVALMHSEGILAGEMKHGPLAL 579
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
39-293 |
3.34e-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: 63.49 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 39 RMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEYlweRNYD-------VVVALTRSGTTteiLDTTE-----RLKGT 106
Cdd:COG0449 296 RIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEF---RYRDpvvdpgtLVIAISQSGET---ADTLAalreaKEKGA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 107 tKLIGIVgdpNTPFVNMVDElvsldfADeqSVVQTR------------FAT--SALALLrtGLgedltdVIAQARDALTS 172
Cdd:COG0449 370 -KVLAIC---NVVGSTIARE------SD--AVLYTHagpeigvastkaFTTqlAALYLL--AL------YLARARGTLSA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 173 E-----------LP---EAVIN--------AEQYS------FLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPM 224
Cdd:COG0449 430 EeeaelleelrkLPekiEEVLDleeqieelAEKYAdarnalFLGRGINYPVALEGALKLKEISYIHAEGYAAGELKHGPI 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 225 S----------IAQPGRVtwqFGSLLPEL----ARD-----VKETGAHFEHGYTDPMVELIRVHR------ATL------ 273
Cdd:COG0449 510 AlidegmpvvaIAPQDEL---YEKTLSNIqevkARGgkviaIADEGDEEVEELADDVIEVPEVDEllapilAVVplqlla 586
|
330 340
....*....|....*....|.
gi 2676403739 274 -ETALERGLNPDTPRNLTRSV 293
Cdd:COG0449 587 yHVAVLRGTDVDQPRNLAKSV 607
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
39-293 |
4.59e-10 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 60.06 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 39 RMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEYlweRNYD-------VVVALTRSGTTteiLDTTERLKGTTKL-- 109
Cdd:PRK00331 291 RIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEF---RYRDpvlspktLVIAISQSGET---ADTLAALRLAKELga 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 110 --IGIVgdpNTPFVNMVDElvsldfADeqSVVQTR------------FAT--SALALLRTGLGEDLT----DVIAQARDA 169
Cdd:PRK00331 365 ktLAIC---NVPGSTIARE------SD--AVLYTHagpeigvastkaFTAqlAVLYLLALALAKARGtlsaEEEADLVHE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 170 LtSELP---EAVIN--------AEQYS------FLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPMS------- 225
Cdd:PRK00331 434 L-RELPaliEQVLDlkeqieelAEDFAdarnalFLGRGVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIAlidegmp 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 226 ---IAQPGRVtwqFGSLL-----------------PELARDVKETGAHFE----HGYTDPMVELIRVHRATLETALERGL 281
Cdd:PRK00331 513 vvaIAPNDEL---YEKTKsniqevkargarviviaDEGDEVAEEADDVIEvpevHELLAPLLYVVPLQLLAYHVALARGT 589
|
330
....*....|..
gi 2676403739 282 NPDTPRNLTRSV 293
Cdd:PRK00331 590 DVDKPRNLAKSV 601
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
186-286 |
6.97e-09 |
|
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: 53.79 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 186 FLGVGWGVGIAQEAALKMRE--AAQVWTEAYSAHEYRHGPMSIAQPGRVTWQFGS-----------LLPELARDVK---- 248
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLEltAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSndpytrqydldLLKELRRDGIaarv 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2676403739 249 -----ETGAHFEHG---YTDPMVELIRVHRA----------TLETALERGLNPDTP 286
Cdd:cd05010 83 iaispESDAGIEDNshyYLPGSRDLDDVYLAfpyilyaqlfALFNSIALGLTPDNP 138
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
39-293 |
1.98e-07 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 52.19 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 39 RMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEYLWER----NYDVVVALTRSGTTTeilDTTERLKGTTK----LI 110
Cdd:PTZ00394 356 RILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRpriqRDDVCFFVSQSGETA---DTLMALQLCKEagamCV 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 111 GIVGDPNTPFVNMVDELVSLDFADEQSVVQTRFATSA------LALLRT---------------GLGE---DLTDVIAQA 166
Cdd:PTZ00394 433 GITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQvvvltlVALLLSsdsvrlqerrneiirGLAElpaAISECLKIT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 167 RDALTSeLPEAVINAEQYSFLGVGWGVGIAQEAALKMREAAQVWTEAYSAHEYRHGPMS-IAQPGRVTW-----QFGSLL 240
Cdd:PTZ00394 513 HDPVKA-LAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPLAlIDETSPVLAmcthdKHFGLS 591
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2676403739 241 PELARDVKETGAHFEHGYTDPMVELIRVHRATLET-----------------------ALERGLNPDTPRNLTRSV 293
Cdd:PTZ00394 592 KSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVpktvdclqcvvnvipfqllayymALLRGNNVDCPRNLAKSV 667
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
42-151 |
1.90e-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: 46.45 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 42 VIGCGTSFYVAQAFAQLRERLGFgqtDAFAASEYLWERNY-------DVVVALTRSGTTTEILDTTERLKGT-TKLIGIV 113
Cdd:cd05013 18 IFGVGSSGLVAEYLAYKLLRLGK---PVVLLSDPHLQLMSaanltpgDVVIAISFSGETKETVEAAEIAKERgAKVIAIT 94
|
90 100 110
....*....|....*....|....*....|....*...
gi 2676403739 114 GDPNTPFVNMVDelVSLDFADEQSVVQTRFATSALALL 151
Cdd:cd05013 95 DSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQL 130
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
39-135 |
2.84e-06 |
|
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: 45.61 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 39 RMAVIGCGTSFYVAQAFAQLRERLGfgqTDAFaaseYLWE-----------RNYDVVVALTRSGTTTEILDTTERLK-GT 106
Cdd:cd05014 2 KVVVTGVGKSGHIARKIAATLSSTG---TPAF----FLHPtealhgdlgmvTPGDVVIAISNSGETDELLNLLPHLKrRG 74
|
90 100
....*....|....*....|....*....
gi 2676403739 107 TKLIGIVGDPNTPFVNMVDELVSLDFADE 135
Cdd:cd05014 75 APIIAITGNPNSTLAKLSDVVLDLPVEEE 103
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
39-126 |
2.46e-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: 43.06 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 39 RMAVIGCGTSFYVAQAFAQLRERLGFGQTDAFAASEYLWE-----RNYDVVVALTRSGTTTEILDTTERLKG-TTKLIGI 112
Cdd:pfam01380 7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvlalvDEDDLVIAISYSGETKDLLAAAELAKArGAKIIAI 86
|
90
....*....|....
gi 2676403739 113 VGDPNTPFVNMVDE 126
Cdd:pfam01380 87 TDSPGSPLAREADH 100
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
42-151 |
2.97e-04 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 41.45 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 42 VIGCGTSFYVAQAFAQLRERLGFG----QTDAFAASEYLWE-RNYDVVVALTRSGTTTEILDTTERLKGT-TKLIGIVGD 115
Cdd:COG1737 139 IFGVGASAPVAEDLAYKLLRLGKNvvllDGDGHLQAESAALlGPGDVVIAISFSGYTRETLEAARLAKERgAKVIAITDS 218
|
90 100 110
....*....|....*....|....*....|....*.
gi 2676403739 116 PNTPFVNMVDelVSLDFADEQSVVQTRFATSALALL 151
Cdd:COG1737 219 PLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQL 252
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
43-134 |
7.38e-04 |
|
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: 38.71 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676403739 43 IGCGTS---FYVAQAFAQLRERLgfgQTDAFAASEYLWERNYD-----VVVALTRSGTTTEILDTTERLKGT-TKLIGIV 113
Cdd:cd05710 5 VGCGGSladMYPAKYFLKKESKL---PVFVYNAAEFLHTGPKRlteksVVILASHSGNTKETVAAAKFAKEKgATVIGLT 81
|
90 100
....*....|....*....|.
gi 2676403739 114 GDPNTPFVNMVDELVSLDFAD 134
Cdd:cd05710 82 DDEDSPLAKLADYVIVYGFEI 102
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
82-119 |
2.65e-03 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 38.80 E-value: 2.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2676403739 82 DVVVALTRSGTTTEILDTTERLK--GtTKLIGIVGDPNTP 119
Cdd:COG0794 93 DVVIAISNSGETEELLALLPLLKrlG-VPLIAITGNPDST 131
|
|
| |
