|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
63-493 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 640.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 63 EEKEVEYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKK-------SLDDPHA--REITTLKMEIQQIMKGNY 133
Cdd:PLN02981 235 RDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENekgrgggGLSRPASveRALSTLEMEVEQIMKGNY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 134 DYFMQKEIFEQPDSVVNTMRGRVRFDGNA----IVLGGIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVM 209
Cdd:PLN02981 315 DHYMQKEIHEQPESLTTTMRGRLIRGGSGkakrVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 210 VELASDFLDRNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKA 289
Cdd:PLN02981 395 MELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKA 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 290 YTSQFISLVMFALVMSEDRLSLQQRRLEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGAL 369
Cdd:PLN02981 475 YTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGAL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 370 KVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETK--AFSSRHL 447
Cdd:PLN02981 555 KVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVcpSGGCRVI 634
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 320546259 448 EIPRTVDCLQGILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:PLN02981 635 EVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
68-493 |
0e+00 |
|
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: 574.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 68 EYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKkslDDPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDS 147
Cdd:COG0449 188 ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLD---GEPVEREVKTVDWDAEAAEKGGYPHFMLKEIHEQPEA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 148 VVNTMRGRVRFDGNaIVLGGIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDD 227
Cdd:COG0449 265 IRDTLRGRLDEDGR-VVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVVDPGT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 228 VCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMSED 307
Cdd:COG0449 344 LVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLARA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 308 RLSL-QQRRLEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGE 386
Cdd:COG0449 424 RGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEISYIHAEGYAAGE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 387 LKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETKAFSSRHLEIPRTVDCLQGILTVIPMQ 466
Cdd:COG0449 504 LKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEVDELLAPILAVVPLQ 583
|
410 420
....*....|....*....|....*..
gi 320546259 467 LLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:COG0449 584 LLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
68-493 |
9.40e-157 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 458.64 E-value: 9.40e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 68 EYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKKSlddPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDS 147
Cdd:TIGR01135 187 ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGA---PVQREVRVIDWDLDAAEKGGYRHFMLKEIYEQPRA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 148 VVNTMRGRVRFDGNAIVLGGIKDyipEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDD 227
Cdd:TIGR01135 264 LRDTLEGRIEENGGVFEELGAEE---LLKNIDRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 228 VCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMSED 307
Cdd:TIGR01135 341 LVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKA 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 308 R--LSLQQRRlEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAG 385
Cdd:TIGR01135 421 RgtLSAEEEA-ELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEGYPAG 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 386 ELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETKAFSSRHLEIPRTVDCLQGILTVIPM 465
Cdd:TIGR01135 500 ELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEVEELLAPIVYTIPL 579
|
410 420
....*....|....*....|....*...
gi 320546259 466 QLLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:TIGR01135 580 QLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
338-491 |
1.25e-67 |
|
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: 213.66 E-value: 1.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 338 KVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNA 417
Cdd:cd05009 2 DIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320546259 418 LQQVTSRKGCPIIICEEGDEETKAFssRHLEIPRTVDCLQGILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVT 491
Cdd:cd05009 82 IKEVKARGAKVIVITDDGDAKDLAD--VVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
174-302 |
1.00e-40 |
|
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: 142.44 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 174 EIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDR-NTPIFRDDVCFFISQSGETADTLMALRYCKQRG 252
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 320546259 253 ALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFAL 302
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAV 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
63-493 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 640.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 63 EEKEVEYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKK-------SLDDPHA--REITTLKMEIQQIMKGNY 133
Cdd:PLN02981 235 RDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENekgrgggGLSRPASveRALSTLEMEVEQIMKGNY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 134 DYFMQKEIFEQPDSVVNTMRGRVRFDGNA----IVLGGIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVM 209
Cdd:PLN02981 315 DHYMQKEIHEQPESLTTTMRGRLIRGGSGkakrVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 210 VELASDFLDRNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKA 289
Cdd:PLN02981 395 MELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKA 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 290 YTSQFISLVMFALVMSEDRLSLQQRRLEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGAL 369
Cdd:PLN02981 475 YTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGAL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 370 KVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETK--AFSSRHL 447
Cdd:PLN02981 555 KVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDASSVcpSGGCRVI 634
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 320546259 448 EIPRTVDCLQGILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:PLN02981 635 EVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
68-493 |
0e+00 |
|
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: 574.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 68 EYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKkslDDPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDS 147
Cdd:COG0449 188 ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLD---GEPVEREVKTVDWDAEAAEKGGYPHFMLKEIHEQPEA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 148 VVNTMRGRVRFDGNaIVLGGIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDD 227
Cdd:COG0449 265 IRDTLRGRLDEDGR-VVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVVDPGT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 228 VCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMSED 307
Cdd:COG0449 344 LVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLARA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 308 RLSL-QQRRLEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGE 386
Cdd:COG0449 424 RGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEISYIHAEGYAAGE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 387 LKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETKAFSSRHLEIPRTVDCLQGILTVIPMQ 466
Cdd:COG0449 504 LKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEVDELLAPILAVVPLQ 583
|
410 420
....*....|....*....|....*..
gi 320546259 467 LLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:COG0449 584 LLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
68-493 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 520.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 68 EYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKkslDDPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDS 147
Cdd:PRK00331 188 ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFD---GNPVEREVYTVDWDASAAEKGGYRHFMLKEIYEQPEA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 148 VVNTMRGRVRFDGNaivlggIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDD 227
Cdd:PRK00331 265 IRDTLEGRLDELGE------GELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEFRYRDPVLSPKT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 228 VCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMSED 307
Cdd:PRK00331 339 LVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALALAKA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 308 RLSLQQRRL-EILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGE 386
Cdd:PRK00331 419 RGTLSAEEEaDLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIHAEGYAAGE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 387 LKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETkAFSSRHLEIPRTVDCLQGILTVIPMQ 466
Cdd:PRK00331 499 LKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVA-EEADDVIEVPEVHELLAPLLYVVPLQ 577
|
410 420
....*....|....*....|....*..
gi 320546259 467 LLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:PRK00331 578 LLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
60-493 |
1.31e-171 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 499.02 E-value: 1.31e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 60 MPLEEKEVEYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKKSLDDPHAREITTLKMEIQQIMKGNYDYFMQK 139
Cdd:PTZ00394 235 LTDLSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 140 EIFEQPDSVVNTMRGRVRFDGNAIVLGGIKD-YIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLD 218
Cdd:PTZ00394 315 EIYEQPESVISSMHGRIDFSSGTVQLSGFTQqSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLD 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 219 RNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLV 298
Cdd:PTZ00394 395 RRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLT 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 299 MFALVMSEDRLSLQQRRLEILQALSKLADQIRDVLQLDSK-VKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYM 377
Cdd:PTZ00394 475 LVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKITHDpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 378 HSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETKAFSSRHLEIPRTVDCLQ 457
Cdd:PTZ00394 555 HTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQ 634
|
410 420 430
....*....|....*....|....*....|....*.
gi 320546259 458 GILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:PTZ00394 635 CVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
68-493 |
9.40e-157 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 458.64 E-value: 9.40e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 68 EYFFASDASAVIEHTNRVIYLEDDDVAAVRDGTLSIHRLKKSlddPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDS 147
Cdd:TIGR01135 187 ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGA---PVQREVRVIDWDLDAAEKGGYRHFMLKEIYEQPRA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 148 VVNTMRGRVRFDGNAIVLGGIKDyipEIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDD 227
Cdd:TIGR01135 264 LRDTLEGRIEENGGVFEELGAEE---LLKNIDRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 228 VCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMSED 307
Cdd:TIGR01135 341 LVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKA 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 308 R--LSLQQRRlEILQALSKLADQIRDVLQLDSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAG 385
Cdd:TIGR01135 421 RgtLSAEEEA-ELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEGYPAG 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 386 ELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETKAFSSRHLEIPRTVDCLQGILTVIPM 465
Cdd:TIGR01135 500 ELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEVEELLAPIVYTIPL 579
|
410 420
....*....|....*....|....*...
gi 320546259 466 QLLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:TIGR01135 580 QLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
70-492 |
3.46e-100 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 314.27 E-value: 3.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 70 FFASDASAVIEHTNRVIYLEDDDVAAVRdgtlsihrLKKSLDDPHAREITTLKMEIQQIMKGNYDYFMQKEIFEQPDSVV 149
Cdd:PTZ00295 220 YVASEPSAFAKYTNEYISLKDGEIAELS--------LENVNDLYTQRRVEKIPEEVIEKSPEPYPHWTLKEIFEQPIALS 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 150 NTMRGRVRFDG--NAIVLGGIKDYIPEIKRCRRLMLIGCGTSYHSAVATRQLLEELTEL-PVMVELASDF-LDRNTpifR 225
Cdd:PTZ00295 292 RALNNGGRLSGynNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVIDASELtLYRLP---D 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 226 DDVCF-FISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVM 304
Cdd:PTZ00295 369 EDAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWF 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 305 SE--DRLSLQQRRLEILQALSKLADQIRDVLQL-DSKVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEG 381
Cdd:PTZ00295 449 AQnkEYSCSNYKCSSLINSLHRLPTYIGMTLKScEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEG 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 382 IMAGELKHGPLALVD--DSMPVLMIVLRDPVYVKCMNALQQVTSRkGCPIIICEEGDEETKAFSSRHLEIPrTVDCLQGI 459
Cdd:PTZ00295 529 FSGGALKHGPFALIDkeKNTPVILIILDDEHKELMINAAEQVKAR-GAYIIVITDDEDLVKDFADEIILIP-SNGPLTAL 606
|
410 420 430
....*....|....*....|....*....|...
gi 320546259 460 LTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTV 492
Cdd:PTZ00295 607 LAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
139-493 |
3.65e-70 |
|
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: 227.09 E-value: 3.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 139 KEIFEQPDSVVNTmrgrvrFDGNAIVLGGIKDYIPEIKRcRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLD 218
Cdd:COG2222 2 REIAQQPEAWRRA------LAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 219 RNTPIFRD-DVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISL 297
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 298 VMFALVMSEDRlslqqrrlEILQALSKLADQIRDVLQLDSKVKELAkDLYQHKSLLIMGRGYNFATCLEGALKVKELTYM 377
Cdd:COG2222 155 LALLAAWGGDD--------ALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 378 HSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNALQQVTSRKGCPIIICEEGDEETkafssRHLEIPRTVDCLQ 457
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAI-----TLPAIPDLHDALD 300
|
330 340 350
....*....|....*....|....*....|....*.
gi 320546259 458 GILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVTVE 493
Cdd:COG2222 301 PLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
338-491 |
1.25e-67 |
|
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: 213.66 E-value: 1.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 338 KVKELAKDLYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMNA 417
Cdd:cd05009 2 DIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320546259 418 LQQVTSRKGCPIIICEEGDEETKAFssRHLEIPRTVDCLQGILTVIPMQLLSYHIAVLRGCDVDCPRNLAKSVT 491
Cdd:cd05009 82 IKEVKARGAKVIVITDDGDAKDLAD--VVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
180-305 |
4.53e-63 |
|
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: 201.19 E-value: 4.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 180 RLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGIT 259
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 320546259 260 NTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFALVMS 305
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
174-302 |
1.00e-40 |
|
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: 142.44 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 174 EIKRCRRLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDR-NTPIFRDDVCFFISQSGETADTLMALRYCKQRG 252
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 320546259 253 ALIVGITNTVGSSICRESHCGVHINAGPEIGVASTKAYTSQFISLVMFAL 302
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAV 130
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
346-476 |
1.35e-22 |
|
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: 93.13 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 346 LYQHKSLLIMGRGYNFATCLEGALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKCMnALQQVTSRK 425
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 320546259 426 GCPIIICEEGDEETKAFSSRHLEIPRTVDCLQGILTVIPMQLLSYHIAVLR 476
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
180-271 |
1.77e-14 |
|
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: 69.91 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 180 RLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDRNTPIFRDD-VCFFISQSGETADTLMALRYCKQRGALIVGI 258
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 320546259 259 TNTVGSSICRESH 271
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
65-96 |
1.38e-11 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 64.01 E-value: 1.38e-11
10 20 30
....*....|....*....|....*....|..
gi 320546259 65 KEVEYFFASDASAVIEHTNRVIYLEDDDVAAV 96
Cdd:cd00714 184 GDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
175-299 |
1.08e-10 |
|
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: 59.55 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 175 IKRCRRLMLIGCGTSYHSAvatRQLLEELTELPVMVELASD---FLDRNTPIFRDDVCFFISQSGETADTLMALRYCKQR 251
Cdd:cd05013 10 LAKARRIYIFGVGSSGLVA---EYLAYKLLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 320546259 252 GALIVGITNTVGSSICRESHcgVHINAGPEIGVASTKAYTSQFISLVM 299
Cdd:cd05013 87 GAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
183-259 |
1.27e-10 |
|
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: 57.77 E-value: 1.27e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320546259 183 LIGCGTSYHSAVATRQLLEELTELPVMVELASDFLD--RNTPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGIT 259
Cdd:cd04795 3 VIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAIT 81
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
175-325 |
6.74e-10 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 59.94 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 175 IKRCRRLMLIGCGTSYHSAVATRQLLEEL----TELPVMVELASDFLDRNTPifrDDVCFFISQSGETADTLMALRYCKQ 250
Cdd:COG1737 131 LAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARLAKE 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320546259 251 RGALIVGITNTVGSSICRESHcgVHINAGPEIGVASTKAYTSQFISLVM----FALVMSEDRLSLQQRRLEILQALSKL 325
Cdd:COG1737 208 RGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALidalAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
179-305 |
2.30e-08 |
|
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: 52.54 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 179 RRLMLIGCGTSYHSA---VATrqlleeLTELpvmvELASDFLDrntP----------IFRDDVCFFISQSGETADTLMAL 245
Cdd:cd05014 1 GKVVVTGVGKSGHIArkiAAT------LSST----GTPAFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320546259 246 RYCKQRGALIVGITNTVGSSICRESH----CGVHINAGPeIGVASTkayTSQFISLVMF-ALVMS 305
Cdd:cd05014 68 PHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALGdALAVA 128
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
180-481 |
2.38e-08 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 55.78 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 180 RLMLIGCGTSYHSAVATRQLLEELTELPVMVELASDFLDrNTPIFRDDVCFFI--SQSGETADTLMALRYCKQRGALIVG 257
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGALTAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 258 ITNTVGSSICRESHCGVHINAGPEIGVASTKAYtsqfiSLVMFALVMSEDRLSLQQRRLEILQALSKLADQIRDVLQLDS 337
Cdd:PRK11382 125 FTKRADSPITSAAEFSIDYQADCIWEIHLLLCY-----SVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRTWEEKGR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 338 KVKELAKD---LYQHKSLLIMGRGYNfatclEGALKVKELTYMHSEGIMAGELKHGPLALVDDSMPVLMIVLRDPVYVKC 414
Cdd:PRK11382 200 QLGELASQwpmIYTVAAGPLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTT 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320546259 415 MNALQQVTSRKGCPIIIceegdeetkafssRHLEIPRTVD-CLQGILTVIPMQLLSYHIAVLRGCDVD 481
Cdd:PRK11382 275 ERAINFVKQRTDNVIVI-------------DYAEISQGLHpWLAPFLMFVPMEWLCYYLSIYKDHNPD 329
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
213-304 |
2.69e-08 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 54.84 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 213 ASDFLDRNTPifRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVAST--KAY 290
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90
....*....|....*
gi 320546259 291 TSQFISLVMFA-LVM 304
Cdd:cd05007 186 TAQKLALNMLStAVM 200
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
226-304 |
3.16e-08 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 55.17 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 226 DDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVAST--KAYTSQFISLVMFA-L 302
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIStG 211
|
..
gi 320546259 303 VM 304
Cdd:PRK05441 212 VM 213
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
213-304 |
2.45e-06 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 49.32 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 213 ASDFLDRN-TPifrDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIgVA-ST--K 288
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 320546259 289 AYTSQFISLVMFA-LVM 304
Cdd:COG2103 198 AGTAQKLVLNMLStAAM 214
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
225-315 |
5.49e-06 |
|
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: 48.43 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 225 RDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHcgVHINAGPE-----IGVASTkayTSQFISLVM 299
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVEreacpLNLAPT---TSTTATLAL 165
|
90
....*....|....*..
gi 320546259 300 F-ALVMsedrlSLQQRR 315
Cdd:COG0794 166 GdALAV-----ALLEAR 177
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
226-271 |
1.99e-04 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 43.21 E-value: 1.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 320546259 226 DDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESH 271
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLAD 233
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
226-300 |
8.95e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 41.22 E-value: 8.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320546259 226 DDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINAGPEIGVAST--KAYTSQFISLVMF 300
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
220-278 |
4.10e-03 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 38.33 E-value: 4.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 220 NTP-IFRDDVCFFISQSGETADTLMALRYCKQRGALIVGITNTVGSSICRESHCGVHINA 278
Cdd:cd05005 69 TTPaIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPA 128
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
180-259 |
4.97e-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: 36.86 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546259 180 RLMLIGCGTSYHSAVATRQLLEELTELPVMVeLASDFLDRntPIFRDDVCFFISQSGETADTLMALRYCKQRGALIVGIT 259
Cdd:cd05017 1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYV-VKDYTLPA--FVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77
|
|
| |
