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Conserved domains on  [gi|16131028|ref|NP_417605|]
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putative galactosamine-6-phosphate deaminase/isomerase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

AgaS family sugar isomerase( domain architecture ID 11495506)

AgaS family sugar isomerase similar to Shewanella sp. D-galactosamine-6-phosphate (GalN-6-P) deaminase AgaS, which catalyzes the conversion GalN-6-P to D-tagatofuranose 6-phosphate (Tag-6-P), and can also catalyze the conversion of Tag-6-P to GalN-6-P

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
agaS_fam TIGR02815
putative sugar isomerase, AgaS family; Some members of this protein family are found in ...
 12-382 0e+00

putative sugar isomerase, AgaS family; Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases.


:

Pssm-ID: 131862 [Multi-domain]  Cd Length: 372  Bit Score: 659.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028    12 TGTWTEEEIRHQPRAWIRSLTNIDALRSALNNFLEPLLRKENLRIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTDL 91
Cdd:TIGR02815   1 NATHTAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGLNVSAVPTTDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028    92 VTNPMDYLNPAHPLLLISFGRSGNSPESVAAVELANQFVPECYHLPITCNEAGALYQNAINSDNAFALLMPAETHDRGFA 171
Cdd:TIGR02815  81 VSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRSFA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   172 MTSSITTMMASCLAVFAPETINSQTFRDVADRCQAILTS-LGDFSEGVFGYAPWKRIVYLGSGGLQGAARESALKVLELT 250
Cdd:TIGR02815 161 MTSSFSCMTLATLAVLGPETIESQTEERFADAALCILESgQWDFSEGVLGYAPWERIVYLGSGGLQGLARESALKVLELT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   251 AGKLAAFYDSPTGFRHGPKSLVDDETLVVVFVSSHPYTRQYDLDLLAELRRDNQAMRVIAIAAESSDIVAAGPHIILPPS 330
Cdd:TIGR02815 241 AGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPS 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16131028   331 RHFIDVEQAFCFLMYAQTFALMQSLHMGNTPDTPSASGTVNRVVQGVIIHPW 382
Cdd:TIGR02815 321 RHFIDVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
 
Name Accession Description Interval E-value
agaS_fam TIGR02815
putative sugar isomerase, AgaS family; Some members of this protein family are found in ...
 12-382 0e+00

putative sugar isomerase, AgaS family; Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases.


Pssm-ID: 131862 [Multi-domain]  Cd Length: 372  Bit Score: 659.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028    12 TGTWTEEEIRHQPRAWIRSLTNIDALRSALNNFLEPLLRKENLRIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTDL 91
Cdd:TIGR02815   1 NATHTAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGLNVSAVPTTDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028    92 VTNPMDYLNPAHPLLLISFGRSGNSPESVAAVELANQFVPECYHLPITCNEAGALYQNAINSDNAFALLMPAETHDRGFA 171
Cdd:TIGR02815  81 VSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRSFA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   172 MTSSITTMMASCLAVFAPETINSQTFRDVADRCQAILTS-LGDFSEGVFGYAPWKRIVYLGSGGLQGAARESALKVLELT 250
Cdd:TIGR02815 161 MTSSFSCMTLATLAVLGPETIESQTEERFADAALCILESgQWDFSEGVLGYAPWERIVYLGSGGLQGLARESALKVLELT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   251 AGKLAAFYDSPTGFRHGPKSLVDDETLVVVFVSSHPYTRQYDLDLLAELRRDNQAMRVIAIAAESSDIVAAGPHIILPPS 330
Cdd:TIGR02815 241 AGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPS 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16131028   331 RHFIDVEQAFCFLMYAQTFALMQSLHMGNTPDTPSASGTVNRVVQGVIIHPW 382
Cdd:TIGR02815 321 RHFIDVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 17-377 5.24e-109

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: 323.00  E-value: 5.24e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  17 EEEIRHQPRAWIRSLtniDALRSALNNFLEPLLRKENLRIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTDLVTNPm 96
Cdd:COG2222   1 AREIAQQPEAWRRAL---AALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYP- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  97 DYLNPAhPLLLISFGRSGNSPESVAAVELANQFvpECYHLPITCNEAGALYQNAinsdnAFALLMPAeTHDRGFAMTSSI 176
Cdd:COG2222  77 AYLKLE-GTLVVAISRSGNSPEVVAALELAKAR--GARTLAITNNPDSPLAEAA-----DRVLPLPA-GPEKSVAATKSF 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028 177 TTMMASCLAVFAPETINSQ---TFRDVADRCQAILTSLGDFSEGVfGYAPWKRIVYLGSGGLQGAARESALKVLELTAGK 253
Cdd:COG2222 148 TTMLLALLALLAAWGGDDAllaALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAGH 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028 254 laAFYDSPTGFRHGPKSLVDDETLVVVFVSSHPyTRQYDLDLLAELRRDnqAMRVIAIAAEssdivaAGPHIILPPSRHF 333
Cdd:COG2222 227 --AEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRAL--GARVVAIGAE------DDAAITLPAIPDL 295

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 16131028 334 IDVEQAFCFLMYAQTFALMQSLHMGNTPDTPSAsgtVNRVVQGV 377
Cdd:COG2222 296 HDALDPLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
SIS_AgaS_like cd05010
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ...
 227-377 2.19e-95

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: 281.44  E-value: 2.19e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028 227 IVYLGSGGLQGAARESALKVLELTAGKLAAFYDSPTGFRHGPKSLVDDETLVVVFVSSHPYTRQYDLDLLAELRRDNQAM 306
Cdd:cd05010   1 VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131028 307 RVIAIAAESSDIVAAGPHIILPPSRHFIDVEQAFCFLMYAQTFALMQSLHMGNTPDTPSASGTVNRVVQGV 377
Cdd:cd05010  81 RVIAISPESDAGIEDNSHYYLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 48-187 1.82e-19

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: 83.50  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028    48 LLRKENlRIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTDLVTNPMDYLNPAHPLLLISFgrSGNSPESVAAVELAN 127
Cdd:pfam01380   1 LLAKAK-RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISY--SGETKDLLAAAELAK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   128 QFVPECyhLPITCNEAGALYQNAinsDNAFALLMPAEThdrGFAMTSSITTMMASCLAVF 187
Cdd:pfam01380  78 ARGAKI--IAITDSPGSPLAREA---DHVLYINAGPET---GVASTKSITAQLAALDALA 129
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 225-364 8.97e-05

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 44.48  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  225 KRIVYLGSGGLQGAARESALKVLELT--------AGKLaafydsptgfRHGPKSLVDDETLVVVFVsshPYTRQYDLDLL 296
Cdd:PTZ00394 527 SSILVLGRGYDLATAMEAALKVKELSyvhtegihSGEL----------KHGPLALIDETSPVLAMC---THDKHFGLSKS 593

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131028  297 AELRRDNQAMRVIAIAAES-SDIVAAGPHIILPPSrhFIDVEQAFCFLMYAQTFALMQSLHMGNTPDTP 364
Cdd:PTZ00394 594 AVQQVKARGGAVVVFATEVdAELKAAASEIVLVPK--TVDCLQCVVNVIPFQLLAYYMALLRGNNVDCP 660
 
Name Accession Description Interval E-value
agaS_fam TIGR02815
putative sugar isomerase, AgaS family; Some members of this protein family are found in ...
 12-382 0e+00

putative sugar isomerase, AgaS family; Some members of this protein family are found in regions associated with N-acetyl-galactosamine and galactosamine untilization and are suggested to be isomerases.


Pssm-ID: 131862 [Multi-domain]  Cd Length: 372  Bit Score: 659.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028    12 TGTWTEEEIRHQPRAWIRSLTNIDALRSALNNFLEPLLRKENLRIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTDL 91
Cdd:TIGR02815   1 NATHTAREIRQQPALWRRLLTIIQALRPALNAFLEPLLARENLRIVLTGAGTSAFIGDALAPWLASHTGLNVSAVPTTDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028    92 VTNPMDYLNPAHPLLLISFGRSGNSPESVAAVELANQFVPECYHLPITCNEAGALYQNAINSDNAFALLMPAETHDRGFA 171
Cdd:TIGR02815  81 VSNPRQYLDPTRPTLLVSFARSGNSPESVAAVELADQLLPECYHLVLTCNEEGALYRNAINRSNAFALLMPAESNDRSFA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   172 MTSSITTMMASCLAVFAPETINSQTFRDVADRCQAILTS-LGDFSEGVFGYAPWKRIVYLGSGGLQGAARESALKVLELT 250
Cdd:TIGR02815 161 MTSSFSCMTLATLAVLGPETIESQTEERFADAALCILESgQWDFSEGVLGYAPWERIVYLGSGGLQGLARESALKVLELT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   251 AGKLAAFYDSPTGFRHGPKSLVDDETLVVVFVSSHPYTRQYDLDLLAELRRDNQAMRVIAIAAESSDIVAAGPHIILPPS 330
Cdd:TIGR02815 241 AGKVMAFYDSSLGFRHGPKSLVDDETLVVVYVSSDPYTRQYDLDLLAELRRDNQAGRVVAISAESSDIVAAGDHFILPPS 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16131028   331 RHFIDVEQAFCFLMYAQTFALMQSLHMGNTPDTPSASGTVNRVVQGVIIHPW 382
Cdd:TIGR02815 321 RHFIDVELAFPYLIFAQTLAFEQSLALGNTPDNPCPTGEVNRVVQGVTIHPF 372
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 17-377 5.24e-109

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: 323.00  E-value: 5.24e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  17 EEEIRHQPRAWIRSLtniDALRSALNNFLEPLLRKENLRIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTDLVTNPm 96
Cdd:COG2222   1 AREIAQQPEAWRRAL---AALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYP- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  97 DYLNPAhPLLLISFGRSGNSPESVAAVELANQFvpECYHLPITCNEAGALYQNAinsdnAFALLMPAeTHDRGFAMTSSI 176
Cdd:COG2222  77 AYLKLE-GTLVVAISRSGNSPEVVAALELAKAR--GARTLAITNNPDSPLAEAA-----DRVLPLPA-GPEKSVAATKSF 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028 177 TTMMASCLAVFAPETINSQ---TFRDVADRCQAILTSLGDFSEGVfGYAPWKRIVYLGSGGLQGAARESALKVLELTAGK 253
Cdd:COG2222 148 TTMLLALLALLAAWGGDDAllaALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAGH 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028 254 laAFYDSPTGFRHGPKSLVDDETLVVVFVSSHPyTRQYDLDLLAELRRDnqAMRVIAIAAEssdivaAGPHIILPPSRHF 333
Cdd:COG2222 227 --AEAYSAAEFRHGPKSLVDPGTLVVVLASEDP-TRELDLDLAAELRAL--GARVVAIGAE------DDAAITLPAIPDL 295

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 16131028 334 IDVEQAFCFLMYAQTFALMQSLHMGNTPDTPSAsgtVNRVVQGV 377
Cdd:COG2222 296 HDALDPLLLLVVAQRLALALALARGLDPDTPRH---LNKVVKTV 336
SIS_AgaS_like cd05010
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ...
 227-377 2.19e-95

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: 281.44  E-value: 2.19e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028 227 IVYLGSGGLQGAARESALKVLELTAGKLAAFYDSPTGFRHGPKSLVDDETLVVVFVSSHPYTRQYDLDLLAELRRDNQAM 306
Cdd:cd05010   1 VVYLGSGPLAGLAREAALKVLELTAGKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLLKELRRDGIAA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131028 307 RVIAIAAESSDIVAAGPHIILPPSRHFIDVEQAFCFLMYAQTFALMQSLHMGNTPDTPSASGTVNRVVQGV 377
Cdd:cd05010  81 RVIAISPESDAGIEDNSHYYLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNPCPSGTVNRVVQGV 151
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 55-187 1.24e-21

SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.


Pssm-ID: 240141 [Multi-domain]  Cd Length: 126  Bit Score: 89.48  E-value: 1.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  55 RIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTdlvtnPMDYLNPA--HPLLLISFGRSGNSPESVAAVELANQfvpE 132
Cdd:cd05008   1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAAS-----EFRYRRPLldEDTLVIAISQSGETADTLAALRLAKE---K 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131028 133 CYHLPITCNEAG-ALYQNAinSDNAFALLMPAETHDRGFAMTSSITTMMASCLAVF 187
Cdd:cd05008  73 GAKTVAITNVVGsTLAREA--DYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 48-187 1.82e-19

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: 83.50  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028    48 LLRKENlRIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTDLVTNPMDYLNPAHPLLLISFgrSGNSPESVAAVELAN 127
Cdd:pfam01380   1 LLAKAK-RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISY--SGETKDLLAAAELAK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   128 QFVPECyhLPITCNEAGALYQNAinsDNAFALLMPAEThdrGFAMTSSITTMMASCLAVF 187
Cdd:pfam01380  78 ARGAKI--IAITDSPGSPLAREA---DHVLYINAGPET---GVASTKSITAQLAALDALA 129
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 221-357 5.52e-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: 76.57  E-value: 5.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   221 YAPWKRIVYLGSGGLQGAARESALKvLELTAGKLAAFYDSPTgFRHGPKSLVDDETLvVVFVSSHPYTRqyDLDLLAELR 300
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIALELALK-FEEIGYKVVEVELASE-LRHGVLALVDEDDL-VIAISYSGETK--DLLAAAELA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131028   301 RDNQAMrVIAIAAESSDIVA--AGPHIILPPSRHfidVEQAFCFLMYAQTFALMQSLHM 357
Cdd:pfam01380  77 KARGAK-IIAITDSPGSPLAreADHVLYINAGPE---TGVASTKSITAQLAALDALAVA 131
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 221-364 2.87e-15

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: 72.68  E-value: 2.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028 221 YAPWKRIVYLGSGGLQGAARESALKVLElTAGKLAAFYdsPTG-FRHGPKSLVDDETLVVVFVSSHPytrqyDLDLLAEL 299
Cdd:cd05009  10 LKEAKSFYVLGRGPNYGTALEGALKLKE-TSYIHAEAY--SAGeFKHGPIALVDEGTPVIFLAPEDR-----LEEKLESL 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131028 300 RRDNQAM--RVIAIAAESSDIVAAGPHIILPPSrhfIDVEQAFCFLMYAQTFALMQSLHMGNTPDTP 364
Cdd:cd05009  82 IKEVKARgaKVIVITDDGDAKDLADVVIRVPAT---VEELSPLLYIVPLQLLAYHLAVARGIDPDKP 145
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 227-313 7.00e-11

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: 58.15  E-value: 7.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028 227 IVYLGSGGLQGAARESALKVLELTagKLAAFYDSPTGFRHGPKSLVDDETLVVVFVSSHPYTRqYDLDLLAELRRdnQAM 306
Cdd:cd04795   1 IFVIGIGGSGAIAAYFALELLELT--GIEVVALIATELEHASLLSLLRKGDVVIALSYSGRTE-ELLAALEIAKE--LGI 75


                ....*..
gi 16131028 307 RVIAIAA 313
Cdd:cd04795  76 PVIAITD 82
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 55-186 3.59e-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: 51.39  E-value: 3.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  55 RIILTGAGTSAFIGDIIAPWLAShTGKNFSAVPTTDLVTNPMDYLNPAHPLLLISfgRSGNSPESVAAVELANQFvpECY 134
Cdd:cd05014   2 KVVVTGVGKSGHIARKIAATLSS-TGTPAFFLHPTEALHGDLGMVTPGDVVIAIS--NSGETDELLNLLPHLKRR--GAP 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 16131028 135 HLPITCNEAGALYQnaiNSDNAFALLMPAETHDRGFAMTSSITTMMAS--CLAV 186
Cdd:cd05014  77 IIAITGNPNSTLAK---LSDVVLDLPVEEEACPLGLAPTTSTTAMLALgdALAV 127
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 225-364 8.97e-05

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 44.48  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  225 KRIVYLGSGGLQGAARESALKVLELT--------AGKLaafydsptgfRHGPKSLVDDETLVVVFVsshPYTRQYDLDLL 296
Cdd:PTZ00394 527 SSILVLGRGYDLATAMEAALKVKELSyvhtegihSGEL----------KHGPLALIDETSPVLAMC---THDKHFGLSKS 593

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131028  297 AELRRDNQAMRVIAIAAES-SDIVAAGPHIILPPSrhFIDVEQAFCFLMYAQTFALMQSLHMGNTPDTP 364
Cdd:PTZ00394 594 AVQQVKARGGAVVVFATEVdAELKAAASEIVLVPK--TVDCLQCVVNVIPFQLLAYYMALLRGNNVDCP 660
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 14-364 1.15e-04

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 44.24  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   14 TWTEEEIRHQPRAWIRSLTNIDALRSA--------LNNFLEPLLRKENLriILTGAGTSAFIGDIIAPWLAS-HTGKNFS 84
Cdd:PTZ00295 277 HWTLKEIFEQPIALSRALNNGGRLSGYnnrvklggLDQYLEELLNIKNL--ILVGCGTSYYAALFAASIMQKlKCFNTVQ 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028   85 AVPTTDLvtNPMDYLNPAHPLLLISfgRSGNSPESVAAVELANQfvpecyhlpITCNEAGALyqNAINSdnafallMPAE 164
Cdd:PTZ00295 355 VIDASEL--TLYRLPDEDAGVIFIS--QSGETLDVVRALNLADE---------LNLPKISVV--NTVGS-------LIAR 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  165 THDRGF--------------AMTSSITTMMA-----------SCLAVFAPETINS---------QTFRDVADRCQAILTS 210
Cdd:PTZ00295 413 STDCGVylnagrevavastkAFTSQVTVLSLialwfaqnkeySCSNYKCSSLINSlhrlptyigMTLKSCEEQCKRIAEK 492

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  211 LGDfsegvfgyapwKRIVY-LGSGGLQGAARESALKVLELTagklaafYDSPTGF-----RHGPKSLVD--DETLVVVFV 282
Cdd:PTZ00295 493 LKN-----------AKSMFiLGKGLGYPIALEGALKIKEIT-------YIHAEGFsggalKHGPFALIDkeKNTPVILII 554

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  283 SSHPYtrqYDLDLLAELRRDNQAMRVIAIaAESSDIVAAGP-HIILPPSrhfIDVEQAFCFLMYAQTFALMQSLHMGNTP 361
Cdd:PTZ00295 555 LDDEH---KELMINAAEQVKARGAYIIVI-TDDEDLVKDFAdEIILIPS---NGPLTALLAVIPLQLLAYEIAILRGINP 627


                 ...
gi 16131028  362 DTP 364
Cdd:PTZ00295 628 DKP 630
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
239-364 1.64e-03

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 40.41  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  239 ARESALKVLELT--------AGKLaafydsptgfRHGPKSLVDDETLVVVFVsshPYTRQYDLDL--LAELR-RDNqamR 307
Cdd:PRK00331 476 ALEGALKLKEISyihaegyaAGEL----------KHGPIALIDEGMPVVAIA---PNDELYEKTKsnIQEVKaRGA---R 539

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  308 VIAIAAESSDIVAAGPHIILPPsrhfiDVEQAFCFLMYA---QTFALMQSLHMGNTPDTP 364
Cdd:PRK00331 540 VIVIADEGDEVAEEADDVIEVP-----EVHELLAPLLYVvplQLLAYHVALARGTDVDKP 594
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 39-180 3.69e-03

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: 37.21  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131028  39 SALNNFLEPLLRKEnlRIILTGAGTSAFIGDIIAPwLASHTGKNFSAVPTTDLVTNPMDYLNPAHPLLLISFgrSGNSPE 118
Cdd:cd05013   1 EALEKAVDLLAKAR--RIYIFGVGSSGLVAEYLAY-KLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISF--SGETKE 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131028 119 SVAAVELANQFvpECYHLPITCNEAGALYQNAinsDnaFALLMPA-ETHDRGFAMTSSITTMM 180
Cdd:cd05013  76 TVEAAEIAKER--GAKVIAITDSANSPLAKLA---D--IVLLVSSeEGDFRSSAFSSRIAQLA 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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