|
Name |
Accession |
Description |
Interval |
E-value |
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
6-339 |
1.50e-112 |
|
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: 330.32 E-value: 1.50e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 6 RREIDEIPEAAARLLDRSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVASLGPSLASIYGAELK 85
Cdd:COG2222 1 AREIAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 86 LGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGE 165
Cdd:COG2222 81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 166 WTGDAGLKRAVADLPNQFAKAVKLNWQDFA-ADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPV 244
Cdd:COG2222 161 WGGDDALLAALDALPAALEAALAADWPAAAlAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 245 ALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATSARAQKAKRLPFVETGHPITDALALILPFYGFVEAWSRSRG 324
Cdd:COG2222 241 SLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALALARG 320
|
330
....*....|....*
gi 1240630904 325 LNPDAPASLKKVTET 339
Cdd:COG2222 321 LDPDTPRHLNKVVKT 335
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
191-338 |
2.54e-41 |
|
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: 141.63 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 191 WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEASVTEIA 270
Cdd:cd05009 3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1240630904 271 DGMSAKGAVVHATSARAQkAKRLPFVETGHPITD----ALALILPFYGFVEAWSRSRGLNPDAPASLKKVTE 338
Cdd:cd05009 83 KEVKARGAKVIVITDDGD-AKDLADVVIRVPATVeelsPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
5-261 |
1.68e-36 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 138.64 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 5 MRREIDEIPEAAARLLD-RSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVAslgPSLASIYG-A 82
Cdd:PRK00331 254 MLKEIYEQPEAIRDTLEgRLDELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVE---VEIASEFRyR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 83 ELKLG-GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVA--G 159
Cdd:PRK00331 331 DPVLSpKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVlyL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 160 LAV-LGEWTG------DAGLKRAVADLPNQFAKAVKLN--WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMH 230
Cdd:PRK00331 411 LALaLAKARGtlsaeeEADLVHELRELPALIEQVLDLKeqIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIH 490
|
250 260 270
....*....|....*....|....*....|.
gi 1240630904 231 AEAYSAAEVLHGPVALVGARFPVLVLAARDA 261
Cdd:PRK00331 491 AEGYAAGELKHGPIALIDEGMPVVAIAPNDE 521
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
5-337 |
5.88e-36 |
|
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: 137.00 E-value: 5.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 5 MRREIDEIPEAAARLLdrsATALAAAGAALRAKDPAFLVT-------IARGSSDHAALFLKYAIELQAGRPVAslgPSLA 77
Cdd:TIGR01135 253 MLKEIYEQPRALRDTL---EGRIEENGGVFEELGAEELLKnidriqiVACGTSYHAGLVAKYLIERLAGIPVE---VEIA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 78 SiygaELKLGGAA------AIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKS 151
Cdd:TIGR01135 327 S----EFRYRKPVvdkdtlVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 152 YVNSIVAgLAVLGEWTGDA----------GLKRAVADLPNQFAKAVKLNWQ--DFAADLGEVESLYVLGRGPALAIASEA 219
Cdd:TIGR01135 403 FTTQLTV-LYLLALALAKArgtlsaeeeaELVDALRRLPDLVEQVLLADESiaELAERYADKRNFLFLGRGLGYPIALEG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 220 ALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATS------ARAQKAKRL 293
Cdd:TIGR01135 482 ALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFApeddetIASVADDVI 561
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1240630904 294 PFVETGHPITDALALIlPFYGFVEAWSRSRGLNPDAPASL-KKVT 337
Cdd:TIGR01135 562 KLPEVEELLAPIVYTI-PLQLLAYHIALAKGTDVDKPRNLaKSVT 605
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
42-163 |
1.11e-12 |
|
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: 64.24 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 42 LVTIARGSSDHAALFLKYAIELQAGRPVASlgpslasIYGAELKLGGAA-------AIAISQSGKSPDIVAMAEAATRAG 114
Cdd:pfam01380 8 IFVIGRGTSYAIALELALKFEEIGYKVVEV-------ELASELRHGVLAlvdeddlVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1240630904 115 AVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVL 163
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALA 129
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
6-339 |
1.50e-112 |
|
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: 330.32 E-value: 1.50e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 6 RREIDEIPEAAARLLDRSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVASLGPSLASIYGAELK 85
Cdd:COG2222 1 AREIAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 86 LGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGE 165
Cdd:COG2222 81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 166 WTGDAGLKRAVADLPNQFAKAVKLNWQDFA-ADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPV 244
Cdd:COG2222 161 WGGDDALLAALDALPAALEAALAADWPAAAlAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYSAAEFRHGPK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 245 ALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATSARAQKAKRLPFVETGHPITDALALILPFYGFVEAWSRSRG 324
Cdd:COG2222 241 SLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPAIPDLHDALDPLLLLVVAQRLALALALARG 320
|
330
....*....|....*
gi 1240630904 325 LNPDAPASLKKVTET 339
Cdd:COG2222 321 LDPDTPRHLNKVVKT 335
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
191-338 |
2.54e-41 |
|
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: 141.63 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 191 WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEASVTEIA 270
Cdd:cd05009 3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1240630904 271 DGMSAKGAVVHATSARAQkAKRLPFVETGHPITD----ALALILPFYGFVEAWSRSRGLNPDAPASLKKVTE 338
Cdd:cd05009 83 KEVKARGAKVIVITDDGD-AKDLADVVIRVPATVeelsPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
5-261 |
3.15e-40 |
|
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: 149.01 E-value: 3.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 5 MRREIDEIPEAAARLLDRSATALAAAGAALRAKDPAFLVTIAR------GSSDHAALFLKYAIELQAGRPVAslgPSLAS 78
Cdd:COG0449 254 MLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRiyivacGTSYHAGLVGKYLIEELARIPVE---VEIAS 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 79 --IYGAELKLGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSI 156
Cdd:COG0449 331 efRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 157 VAgLAVLGEWTG----------DAGLKRAVADLPNQFAKAVKLNWQ--DFAADLGEVESLYVLGRGPALAIASEAALKFK 224
Cdd:COG0449 411 AA-LYLLALYLArargtlsaeeEAELLEELRKLPEKIEEVLDLEEQieELAEKYADARNALFLGRGINYPVALEGALKLK 489
|
250 260 270
....*....|....*....|....*....|....*..
gi 1240630904 225 ETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDA 261
Cdd:COG0449 490 EISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDE 526
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
5-261 |
1.68e-36 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 138.64 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 5 MRREIDEIPEAAARLLD-RSATALAAAGAALRAKDPAFLVTIARGSSDHAALFLKYAIELQAGRPVAslgPSLASIYG-A 82
Cdd:PRK00331 254 MLKEIYEQPEAIRDTLEgRLDELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVE---VEIASEFRyR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 83 ELKLG-GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVA--G 159
Cdd:PRK00331 331 DPVLSpKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVlyL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 160 LAV-LGEWTG------DAGLKRAVADLPNQFAKAVKLN--WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMH 230
Cdd:PRK00331 411 LALaLAKARGtlsaeeEADLVHELRELPALIEQVLDLKeqIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIH 490
|
250 260 270
....*....|....*....|....*....|.
gi 1240630904 231 AEAYSAAEVLHGPVALVGARFPVLVLAARDA 261
Cdd:PRK00331 491 AEGYAAGELKHGPIALIDEGMPVVAIAPNDE 521
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
5-337 |
5.88e-36 |
|
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: 137.00 E-value: 5.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 5 MRREIDEIPEAAARLLdrsATALAAAGAALRAKDPAFLVT-------IARGSSDHAALFLKYAIELQAGRPVAslgPSLA 77
Cdd:TIGR01135 253 MLKEIYEQPRALRDTL---EGRIEENGGVFEELGAEELLKnidriqiVACGTSYHAGLVAKYLIERLAGIPVE---VEIA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 78 SiygaELKLGGAA------AIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKS 151
Cdd:TIGR01135 327 S----EFRYRKPVvdkdtlVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 152 YVNSIVAgLAVLGEWTGDA----------GLKRAVADLPNQFAKAVKLNWQ--DFAADLGEVESLYVLGRGPALAIASEA 219
Cdd:TIGR01135 403 FTTQLTV-LYLLALALAKArgtlsaeeeaELVDALRRLPDLVEQVLLADESiaELAERYADKRNFLFLGRGLGYPIALEG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 220 ALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEASVTEIADGMSAKGAVVHATS------ARAQKAKRL 293
Cdd:TIGR01135 482 ALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFApeddetIASVADDVI 561
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1240630904 294 PFVETGHPITDALALIlPFYGFVEAWSRSRGLNPDAPASL-KKVT 337
Cdd:TIGR01135 562 KLPEVEELLAPIVYTI-PLQLLAYHIALAKGTDVDKPRNLaKSVT 605
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
41-166 |
2.01e-35 |
|
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: 125.30 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 41 FLVTIARGSSDHAALFLKYAIELQAGRPVASLGPSlASIYGAELKLGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIAL 120
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAAS-EFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1240630904 121 TNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGEW 166
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALAL 125
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
5-337 |
2.76e-31 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 124.09 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 5 MRREIDEIPEAA-----ARLLdRSATALAAAGAALRAKDpaFLVTIAR---------GSSDHAALFLKYAIELQAGRPVA 70
Cdd:PLN02981 318 MQKEIHEQPESLtttmrGRLI-RGGSGKAKRVLLGGLKD--HLKTIRRsrrivfigcGTSYNAALAARPILEELSGVPVT 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 71 SlgpSLAS--------IYGAElklggaAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGP 142
Cdd:PLN02981 395 M---ELASdlldrqgpIYRED------TAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 143 ELAVAATKSYVNSIVA----GLAvLGEWTGDAGLKR-----AVADLPNQFAKAVKLNWQ--DFAADLGEVESLYVLGRGP 211
Cdd:PLN02981 466 EIGVASTKAYTSQIVAmtmlALA-LGEDSISSRSRReaiidGLFDLPNKVREVLKLDQEmkELAELLIDEQSLLVFGRGY 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 212 ALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARDAA---EASVTE--IADG-----MSAKGAVVH 281
Cdd:PLN02981 545 NYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACfskQQSVIQqlRARKgrlivICSKGDASS 624
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1240630904 282 ATSARAQKAKRLPFVETG-HPITDALALILPFYGFveawSRSRGLNPDAPASL-KKVT 337
Cdd:PLN02981 625 VCPSGGCRVIEVPQVEDClQPVINIVPLQLLAYHL----TVLRGHNVDQPRNLaKSVT 678
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
42-337 |
1.08e-29 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 119.36 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 42 LVTIARGSSDHAALFLKYAIE-LQAGRPVASLGPSLASIYGAELKLGGAaaIAISQSGKSPDIVAMAEAATRAGAVSIAL 120
Cdd:PTZ00295 325 LILVGCGTSYYAALFAASIMQkLKCFNTVQVIDASELTLYRLPDEDAGV--IFISQSGETLDVVRALNLADELNLPKISV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 121 TNTLPSPIAEACSHPLDILAGPELAVAATKSYvNSIVAGLAVLGEW-----------TGDAGLKRAVADLPNQFAKAVKL 189
Cdd:PTZ00295 403 VNTVGSLIARSTDCGVYLNAGREVAVASTKAF-TSQVTVLSLIALWfaqnkeyscsnYKCSSLINSLHRLPTYIGMTLKS 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 190 N---WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGAR--FPVLVLAARDAAEA 264
Cdd:PTZ00295 482 CeeqCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKE 561
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1240630904 265 SVTEIADGMSAKGAVVHATSARAQKAK----RLPFVETGHPITDALALIlPFYGFVEAWSRSRGLNPDAPASLKK-VT 337
Cdd:PTZ00295 562 LMINAAEQVKARGAYIIVITDDEDLVKdfadEIILIPSNGPLTALLAVI-PLQLLAYEIAILRGINPDKPRGLAKtVT 638
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
92-335 |
9.44e-22 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 96.10 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVLGEWTGD-- 169
Cdd:PTZ00394 406 FFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDsv 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 170 ------AGLKRAVADLPNQFAKAVKLN---WQDFAADLGEVESLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVL 240
Cdd:PTZ00394 486 rlqerrNEIIRGLAELPAAISECLKIThdpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELK 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 241 HGPVALVGARFPVLVLAARDAA-EASVTEIADGMSAKGAVV-HATSARAQ-KAKRLPFVETGHpITDALALI---LPFYG 314
Cdd:PTZ00394 566 HGPLALIDETSPVLAMCTHDKHfGLSKSAVQQVKARGGAVVvFATEVDAElKAAASEIVLVPK-TVDCLQCVvnvIPFQL 644
|
250 260
....*....|....*....|.
gi 1240630904 315 FVEAWSRSRGLNPDAPASLKK 335
Cdd:PTZ00394 645 LAYYMALLRGNNVDCPRNLAK 665
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
42-163 |
1.11e-12 |
|
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: 64.24 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 42 LVTIARGSSDHAALFLKYAIELQAGRPVASlgpslasIYGAELKLGGAA-------AIAISQSGKSPDIVAMAEAATRAG 114
Cdd:pfam01380 8 IFVIGRGTSYAIALELALKFEEIGYKVVEV-------ELASELRHGVLAlvdeddlVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1240630904 115 AVSIALTNTLPSPIAEACSHPLDILAGPELAVAATKSYVNSIVAGLAVL 163
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALA 129
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
90-262 |
2.90e-08 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 54.62 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 90 AAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGP--ELAVAATKSYVNSIVAGLAVLGEWt 167
Cdd:PRK11382 95 AVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNAEI- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 168 gdAGLKRAVADLPNQFAKAVKlNWQDFAADLGEVES----LYVLGRGPALAIA-SEAALKFKETSGMHAEAYSAAEVLHG 242
Cdd:PRK11382 174 --GKIKNDLKQLPNALGHLVR-TWEEKGRQLGELASqwpmIYTVAAGPLRPLGyKEGIVTLMEFTWTHGCVIESGEFRHG 250
|
170 180
....*....|....*....|
gi 1240630904 243 PVALVGARFPVLVLAARDAA 262
Cdd:PRK11382 251 PLEIVEPGVPFLFLLGNDES 270
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
45-163 |
3.60e-08 |
|
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: 51.85 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 45 IARGSSDHAALFLKYAIeLQAGRPV-ASLGPSLASIYGAELKlGGAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNT 123
Cdd:cd05013 19 FGVGSSGLVAEYLAYKL-LRLGKPVvLLSDPHLQLMSAANLT-PGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDS 96
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1240630904 124 LPSPIAEACSHPLDILAGPELavaATKSYVNSIVAGLAVL 163
Cdd:cd05013 97 ANSPLAKLADIVLLVSSEEGD---FRSSAFSSRIAQLALI 133
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
45-163 |
1.35e-07 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 52.24 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 45 IARGSSDHAALFLKYAIeLQAGRPVASLGPSLASIYGAELKLG-GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNT 123
Cdd:COG1737 140 FGVGASAPVAEDLAYKL-LRLGKNVVLLDGDGHLQAESAALLGpGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDS 218
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1240630904 124 LPSPIAEACSHPLDIlagPELAVAATKSYVNSIVAGLAVL 163
Cdd:COG1737 219 PLSPLAKLADVVLYV---PSEEPTLRSSAFSSRVAQLALI 255
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
203-260 |
2.71e-07 |
|
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: 48.83 E-value: 2.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1240630904 203 SLYVLGRGPALAIASEAALKFKETSGMHAEAYSAAEVLHGPVALVGARFPVLVLAARD 260
Cdd:pfam01380 7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSG 64
|
|
| PRK15482 |
PRK15482 |
HTH-type transcriptional regulator MurR; |
88-141 |
2.11e-05 |
|
HTH-type transcriptional regulator MurR;
Pssm-ID: 185379 [Multi-domain] Cd Length: 285 Bit Score: 45.46 E-value: 2.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1240630904 88 GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAG 141
Cdd:PRK15482 183 GDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSG 236
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
92-144 |
2.39e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 42.46 E-value: 2.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1240630904 92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPEL 144
Cdd:PRK05441 136 VGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEV 188
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
88-130 |
2.77e-04 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 42.05 E-value: 2.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1240630904 88 GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAE 130
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAK 230
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
92-162 |
3.01e-04 |
|
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: 41.74 E-value: 3.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1240630904 92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPEL--------AVAATKSYVNSIVAGLAV 162
Cdd:cd05007 123 IGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVvagstrlkAGTAQKLALNMLSTAVMI 201
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
91-134 |
4.37e-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: 39.48 E-value: 4.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1240630904 91 AIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSH 134
Cdd:cd05710 51 VILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADY 94
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
207-330 |
2.19e-03 |
|
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: 37.99 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 207 LGRGPALAIASEAALKFKE-TSG-MHAEAYSAAEVLHGPVALVGARFPVLVLAARDAAEAS-----VTEI-ADGMSAKGA 278
Cdd:cd05010 4 LGSGPLAGLAREAALKVLElTAGkVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQydldlLKELrRDGIAARVI 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1240630904 279 VVHATSARAQKAKRLPFVETGHPITDAlALILPFYGFVE----AWSRSRGLNPDAP 330
Cdd:cd05010 84 AISPESDAGIEDNSHYYLPGSRDLDDV-YLAFPYILYAQlfalFNSIALGLTPDNP 138
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
92-170 |
2.47e-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: 39.19 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240630904 92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDILAGPE---LAVAATksyvNSIVAGLAVlgewtG 168
Cdd:COG0794 96 IAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREacpLNLAPT----TSTTATLAL-----G 166
|
..
gi 1240630904 169 DA 170
Cdd:COG0794 167 DA 168
|
|
| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
88-138 |
3.40e-03 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 37.91 E-value: 3.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1240630904 88 GAAAIAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAEACSHPLDI 138
Cdd:PRK13937 107 GDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLIV 157
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
92-130 |
6.25e-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: 37.17 E-value: 6.25e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1240630904 92 IAISQSGKSPDIVAMAEAATRAGAVSIALTNTLPSPIAE 130
Cdd:cd05005 80 IAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAK 118
|
|
|