|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-428 |
1.13e-154 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 453.44 E-value: 1.13e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 1 MEFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHI------HCSKIGSEDFSF---RTVQKLELELSKIKKGPYDNFM 71
Cdd:PLN02981 239 KEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIykfeneKGRGGGGLSRPAsveRALSTLEMEVEQIMKGNYDHYM 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 72 QKEIYEQCETTKNVMRGRV----DAFTNRVVLGGLENWLTELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELA 147
Cdd:PLN02981 319 QKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 148 LDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQ 227
Cdd:PLN02981 399 SDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 228 YIALVMIALWMSEDLVSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCdKKLKQHDTFLLLGRGYQFASALEGASKMK 307
Cdd:PLN02981 479 IVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELA-ELLIDEQSLLVFGRGYNYATALEGALKVK 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 308 EISYVHSESILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKiwEQDKQKGNVVTLE 387
Cdd:PLN02981 558 EVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDA--SSVCPSGGCRVIE 635
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 6323731 388 VPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMS 428
Cdd:PLN02981 636 VPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKS 676
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
2-423 |
3.17e-116 |
|
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: 352.39 E-value: 3.17e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 2 EFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHcskigseDFSF----RTVQKLELELSKIKKGPYDNFMQKEIYE 77
Cdd:COG0449 188 ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIY-------DLDGepveREVKTVDWDAEAAEKGGYPHFMLKEIHE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 78 QCETTKNVMRGRVDAfTNRVVLGGLENWLTELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCI 157
Cdd:COG0449 261 QPEAIRDTLRGRLDE-DGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 158 FRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALW 237
Cdd:COG0449 340 DPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALY 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 238 MSEDL-VSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCdKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSES 316
Cdd:COG0449 420 LARARgTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELA-EKYADARNALFLGRGINYPVALEGALKLKEISYIHAEG 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 317 ILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKiweqDKQKGNVVTLEVPQTVDCLQ 396
Cdd:COG0449 499 YAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDE----EVEELADDVIEVPEVDELLA 574
|
410 420
....*....|....*....|....*..
gi 6323731 397 GILNVIPLQLISYWLAIKKDIGVDLPR 423
Cdd:COG0449 575 PILAVVPLQLLAYHVAVLRGTDVDQPR 601
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-428 |
2.06e-98 |
|
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: 306.49 E-value: 2.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 2 EFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHcskigseDFSFRTVQK----LELELSKIKKGPYDNFMQKEIYE 77
Cdd:TIGR01135 187 ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIY-------NFEGAPVQRevrvIDWDLDAAEKGGYRHFMLKEIYE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 78 QCETTKNVMRGRVDAFTNRVVLGGLENwltELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCI 157
Cdd:TIGR01135 260 QPRALRDTLEGRIEENGGVFEELGAEE---LLKNIDRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVV 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 158 FRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALW 237
Cdd:TIGR01135 337 DKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALA 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 238 MSEDL-VSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCdKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSES 316
Cdd:TIGR01135 417 LAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELA-ERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEG 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 317 ILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKIWEQDkqkgNVVTLEVPQTVDCLQ 396
Cdd:TIGR01135 496 YPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV----ADDVIKLPEVEELLA 571
|
410 420 430
....*....|....*....|....*....|..
gi 6323731 397 GILNVIPLQLISYWLAIKKDIGVDLPRDSAMS 428
Cdd:TIGR01135 572 PIVYTIPLQLLAYHIALAKGTDVDKPRNLAKS 603
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
279-428 |
1.99e-46 |
|
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: 157.04 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 279 KKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIE 358
Cdd:cd05009 8 EKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLIKEVKA 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 359 RKGNPIIICNKGhkiweqDKQKGNVVTLEVPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMS 428
Cdd:cd05009 88 RGAKVIVITDDG------DAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKS 151
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
108-236 |
6.98e-28 |
|
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: 107.00 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 108 ELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCC-IFRNDVCIFVSRSGETTDTINALNYCIKKE 186
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLAlVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 6323731 187 AVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIAL 236
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAV 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-428 |
1.13e-154 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 453.44 E-value: 1.13e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 1 MEFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHI------HCSKIGSEDFSF---RTVQKLELELSKIKKGPYDNFM 71
Cdd:PLN02981 239 KEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIykfeneKGRGGGGLSRPAsveRALSTLEMEVEQIMKGNYDHYM 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 72 QKEIYEQCETTKNVMRGRV----DAFTNRVVLGGLENWLTELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELA 147
Cdd:PLN02981 319 QKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 148 LDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQ 227
Cdd:PLN02981 399 SDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 228 YIALVMIALWMSEDLVSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCdKKLKQHDTFLLLGRGYQFASALEGASKMK 307
Cdd:PLN02981 479 IVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELA-ELLIDEQSLLVFGRGYNYATALEGALKVK 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 308 EISYVHSESILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKiwEQDKQKGNVVTLE 387
Cdd:PLN02981 558 EVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDA--SSVCPSGGCRVIE 635
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 6323731 388 VPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMS 428
Cdd:PLN02981 636 VPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKS 676
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-428 |
1.72e-128 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 386.16 E-value: 1.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 1 MEFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHCSKIGSEDFSFRTVQKLELELSKIKKGPYDNFMQKEIYEQCE 80
Cdd:PTZ00394 242 LEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQPE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 81 TTKNVMRGRVDAFTNRVVLGGL-ENWLTELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCIFR 159
Cdd:PTZ00394 322 SVISSMHGRIDFSSGTVQLSGFtQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 160 NDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALWMS 239
Cdd:PTZ00394 402 DDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLS 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 240 EDLVSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCDKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILT 319
Cdd:PTZ00394 482 SDSVRLQERRNEIIRGLAELPAAISECLKITHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHS 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 320 NELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNkghkiwEQDKQKGNVVTL--EVPQTVDCLQG 397
Cdd:PTZ00394 562 GELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFAT------EVDAELKAAASEivLVPKTVDCLQC 635
|
410 420 430
....*....|....*....|....*....|.
gi 6323731 398 ILNVIPLQLISYWLAIKKDIGVDLPRDSAMS 428
Cdd:PTZ00394 636 VVNVIPFQLLAYYMALLRGNNVDCPRNLAKS 666
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
2-423 |
3.17e-116 |
|
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: 352.39 E-value: 3.17e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 2 EFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHcskigseDFSF----RTVQKLELELSKIKKGPYDNFMQKEIYE 77
Cdd:COG0449 188 ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIY-------DLDGepveREVKTVDWDAEAAEKGGYPHFMLKEIHE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 78 QCETTKNVMRGRVDAfTNRVVLGGLENWLTELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCI 157
Cdd:COG0449 261 QPEAIRDTLRGRLDE-DGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 158 FRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALW 237
Cdd:COG0449 340 DPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALY 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 238 MSEDL-VSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCdKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSES 316
Cdd:COG0449 420 LARARgTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELA-EKYADARNALFLGRGINYPVALEGALKLKEISYIHAEG 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 317 ILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKiweqDKQKGNVVTLEVPQTVDCLQ 396
Cdd:COG0449 499 YAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDE----EVEELADDVIEVPEVDELLA 574
|
410 420
....*....|....*....|....*..
gi 6323731 397 GILNVIPLQLISYWLAIKKDIGVDLPR 423
Cdd:COG0449 575 PILAVVPLQLLAYHVAVLRGTDVDQPR 601
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
2-423 |
2.77e-103 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 318.91 E-value: 2.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 2 EFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIhcskigsEDFS----FRTVQKLELELSKIKKGPYDNFMQKEIYE 77
Cdd:PRK00331 188 ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEI-------FDFDgnpvEREVYTVDWDASAAEKGGYRHFMLKEIYE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 78 QCETTKNVMRGRVDAftnrvvLGGLENWLTELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCI 157
Cdd:PRK00331 261 QPEAIRDTLEGRLDE------LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEFRYRDPVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 158 FRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALW 237
Cdd:PRK00331 335 SPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 238 MSEDLVSK-IERRKEIIQALTIVPSQIKEVLELEPLIIELCdKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSES 316
Cdd:PRK00331 415 LAKARGTLsAEEEADLVHELRELPALIEQVLDLKEQIEELA-EDFADARNALFLGRGVDYPVALEGALKLKEISYIHAEG 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 317 ILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKIWEQDkqkgnVVTLEVPQTVDCLQ 396
Cdd:PRK00331 494 YAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEA-----DDVIEVPEVHELLA 568
|
410 420
....*....|....*....|....*..
gi 6323731 397 GILNVIPLQLISYWLAIKKDIGVDLPR 423
Cdd:PRK00331 569 PLLYVVPLQLLAYHVALARGTDVDKPR 595
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-428 |
2.06e-98 |
|
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: 306.49 E-value: 2.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 2 EFYLSSDCASLARYVSKVVYLEDNDIAHIYDGELHIHcskigseDFSFRTVQK----LELELSKIKKGPYDNFMQKEIYE 77
Cdd:TIGR01135 187 ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIY-------NFEGAPVQRevrvIDWDLDAAEKGGYRHFMLKEIYE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 78 QCETTKNVMRGRVDAFTNRVVLGGLENwltELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCI 157
Cdd:TIGR01135 260 QPRALRDTLEGRIEENGGVFEELGAEE---LLKNIDRIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVV 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 158 FRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALW 237
Cdd:TIGR01135 337 DKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALA 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 238 MSEDL-VSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCdKKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSES 316
Cdd:TIGR01135 417 LAKARgTLSAEEEAELVDALRRLPDLVEQVLLADESIAELA-ERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEG 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 317 ILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGHKIWEQDkqkgNVVTLEVPQTVDCLQ 396
Cdd:TIGR01135 496 YPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV----ADDVIKLPEVEELLA 571
|
410 420 430
....*....|....*....|....*....|..
gi 6323731 397 GILNVIPLQLISYWLAIKKDIGVDLPRDSAMS 428
Cdd:TIGR01135 572 PIVYTIPLQLLAYHIALAKGTDVDKPRNLAKS 603
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
4-426 |
1.02e-71 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 237.61 E-value: 1.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 4 YLSSDCASLARYVSKVVYLEDNDIAHI-YDGElhihcskigSEDFSFRTVQKLELELSKIKKGPYDNFMQKEIYEQCETT 82
Cdd:PTZ00295 220 YVASEPSAFAKYTNEYISLKDGEIAELsLENV---------NDLYTQRRVEKIPEEVIEKSPEPYPHWTLKEIFEQPIAL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 83 KNVM--RGRVDAFTNRVVLGGLENWLTELRRAKRIIMIASKASFHSCLAARPIFE-----ELMEVPVNVELALDfvdrnc 155
Cdd:PTZ00295 291 SRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQklkcfNTVQVIDASELTLY------ 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 156 CIFRNDV-CIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMI 234
Cdd:PTZ00295 365 RLPDEDAgVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLI 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 235 ALWMSE--DLVSKIERRKEIIQALTIVPSQIKEVLELEPLIIELCDKKLKQHDTFLLLGRGYQFASALEGASKMKEISYV 312
Cdd:PTZ00295 445 ALWFAQnkEYSCSNYKCSSLINSLHRLPTYIGMTLKSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 313 HSESILTNELGHRVLAV--ASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKghkiwEQDKQKGNVVTLEVPQ 390
Cdd:PTZ00295 525 HAEGFSGGALKHGPFALidKEKNTPVILIILDDEHKELMINAAEQVKARGAYIIVITDD-----EDLVKDFADEIILIPS 599
|
410 420 430
....*....|....*....|....*....|....*.
gi 6323731 391 TvDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSA 426
Cdd:PTZ00295 600 N-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLA 634
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
279-428 |
1.99e-46 |
|
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: 157.04 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 279 KKLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIE 358
Cdd:cd05009 8 EKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLIKEVKA 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 359 RKGNPIIICNKGhkiweqDKQKGNVVTLEVPQTVDCLQGILNVIPLQLISYWLAIKKDIGVDLPRDSAMS 428
Cdd:cd05009 88 RGAKVIVITDDG------DAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKS 151
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
114-239 |
9.79e-46 |
|
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: 154.19 E-value: 9.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 114 RIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVV 193
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6323731 194 NCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIALWMS 239
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
73-423 |
9.67e-41 |
|
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: 147.74 E-value: 9.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 73 KEIYEQCETTKNvmrgrvdafTNRVVLGGLENWLTELRRAK--RIIMIASKASFHSCLAARPIFEELMEVPVNVELALDF 150
Cdd:COG2222 2 REIAQQPEAWRR---------ALAALAAAIAALLARLRAKPprRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 151 VDRNCCIF-RNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYI 229
Cdd:COG2222 73 VVYPAYLKlEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 230 ALVMI-ALWMSEDlvskierrkEIIQALTIVPSQIKEVLELEPLIIELCDkkLKQHDTFLLLGRGYQFASALEGASKMKE 308
Cdd:COG2222 153 ALLALlAAWGGDD---------ALLAALDALPAALEAALAADWPAAALAA--LADAERVVFLGRGPLYGLAREAALKLKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 309 ISYVHSESILTNELGHRVLAVASDNPPIIAFATKDAFSPKIASCIDQIIERKGNPIIICNKGhkiweqdkqkGNVVTLEV 388
Cdd:COG2222 222 LSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAED----------DAAITLPA 291
|
330 340 350
....*....|....*....|....*....|....*.
gi 6323731 389 PQTV-DCLQGILNVIPLQLISYWLAIKKDIGVDLPR 423
Cdd:COG2222 292 IPDLhDALDPLLLLVVAQRLALALALARGLDPDTPR 327
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
108-236 |
6.98e-28 |
|
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: 107.00 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 108 ELRRAKRIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFVDRNCC-IFRNDVCIFVSRSGETTDTINALNYCIKKE 186
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLAlVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 6323731 187 AVTIGVVNCSGSSISRFTHCGVHTNTGPEKGIATTKSYTSQYIALVMIAL 236
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAV 130
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
280-413 |
2.87e-17 |
|
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: 77.72 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 280 KLKQHDTFLLLGRGYQFASALEGASKMKEISYVHSESILTNELGHRVLAVASDNPPIIAFATKDAFSPKIAScIDQIIER 359
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAA-AELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6323731 360 KGNPIIICNKGHKIWEQDKqKGNVVTLEVPQTvdcLQGILNVIPLQLISYWLAI 413
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREA-DHVLYINAGPET---GVASTKSITAQLAALDALA 129
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-30 |
8.80e-07 |
|
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: 49.37 E-value: 8.80e-07
10 20
....*....|....*....|....*....
gi 6323731 2 EFYLSSDCASLARYVSKVVYLEDNDIAHI 30
Cdd:cd00714 187 ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
147-268 |
3.16e-06 |
|
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: 48.29 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 147 ALDFVDRNCCifRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPE--KGIATTKSY 224
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEvvAGSTRLKAG 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323731 225 TSQYIAL------VMIAL------WMSeDLVSK----IERRKEIIQALT-IVPSQIKEVLE 268
Cdd:cd05007 186 TAQKLALnmlstaVMIRLgkvygnLMV-DVRATneklRERAIRIVMEATgVSRDEAEAALE 245
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
109-256 |
1.03e-05 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 46.84 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 109 LRRAKRIIMIASKASFhscLAARPIFEELMEVPVNVEL----ALDFVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIK 184
Cdd:COG1737 131 LAKARRIYIFGVGASA---PVAEDLAYKLLRLGKNVVLldgdGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKE 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323731 185 KEAVTIGVVNCSGSSISRFTHC--GVHTNTGPEKGIATTkSYTSQYIAL----VMIALWMSEDLVSKIERRKEIIQAL 256
Cdd:COG1737 208 RGAKVIAITDSPLSPLAKLADVvlYVPSEEPTLRSSAFS-SRVAQLALIdalaAAVAQRDGDKARERLERTEALLSEL 284
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
160-282 |
2.14e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 45.93 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 160 NDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTHCGVHTNTGPEkgIAT--T--KSYTSQYIAL---- 231
Cdd:PRK05441 132 KDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPE--VLTgsTrmKAGTAQKLVLnmis 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323731 232 --VMIAL------WMSeDLV---SK-IERRKEIIQALTIVPSQIKEVLelepliIELCDKKLK 282
Cdd:PRK05441 210 tgVMIRLgkvygnLMV-DVKatnEKlVDRAVRIVMEATGVSREEAEAA------LEAADGSVK 265
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
109-236 |
9.65e-05 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 42.22 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 109 LRRAKRIIMIASKASFhscLAARPIFEELMEVPVNVELALD---FVDRNCCIFRNDVCIFVSRSGETTDTINALNYCIKK 185
Cdd:cd05013 10 LAKARRIYIFGVGSSG---LVAEYLAYKLLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 6323731 186 EAVTIGVVNCSGSSISRFTHC--GVHTNTGPEKGIATTkSYTSQYIALVMIAL 236
Cdd:cd05013 87 GAKVIAITDSANSPLAKLADIvlLVSSEEGDFRSSAFS-SRIAQLALIDALFL 138
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
156-233 |
4.33e-04 |
|
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: 40.22 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 156 CIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRFTH----CGVHTNTGPEkGIATTKSYTSQYI-- 229
Cdd:cd05014 44 MVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACPL-GLAPTTSTTAMLAlg 122
|
....*
gi 6323731 230 -ALVM 233
Cdd:cd05014 123 dALAV 127
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
114-205 |
9.69e-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: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 114 RIIMIASKASFHSCLAARPIFEELMEVPVNVELALDFV-DRNCCIFRNDVCIFVSRSGETTDTINALNYCIKKEAVTIGV 192
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLhTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90
....*....|...
gi 6323731 193 VNCSGSSISRFTH 205
Cdd:cd05710 81 TDDEDSPLAKLAD 93
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
159-233 |
5.88e-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: 38.42 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323731 159 RNDVCIFVSRSGETTDTINALNYCIKKEAVTIGVVNCSGSSISRftHCGVHTNTGPEK-----GIATTKSYTSQyiaLVM 233
Cdd:COG0794 91 PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLAR--AADVVLDLPVEReacplNLAPTTSTTAT---LAL 165
|
|
| |
