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Conserved domains on  [gi|553911965|ref|WP_023139453|]
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MULTISPECIES: SIS domain-containing protein [Salmonella]

Protein Classification

glutamine--fructose-6-phosphate aminotransferase( domain architecture ID 11418683)

glutamine--fructose-6-phosphate aminotransferase catalyzes the formation of glucosamine 6-phosphate from fructose-6-phosphate and glutamine in the hexosamine biosynthetic pathway

CATH:  3.40.50.10490|3.60.20.10
EC:  2.6.1.16
Gene Ontology:  GO:0006541|GO:0097367|GO:0004360|GO:0005975|GO:0006002
PubMed:  12044898

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 33-158 9.05e-40

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: 136.47  E-value: 9.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  33 RIILTGSGTSYHGALTARAFMQRWCALPVDVCWPFMLDDETLARSGKALVVGISQGGGSLSTLAAMERARNVGHITASMA 112
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 553911965 113 GVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVA 158
Cdd:cd05008   81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 1-329 1.58e-34

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: 129.25  E-value: 1.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965   1 MNETPLRLLEMLTQTREDLWRAAQALTERGVTRIILTGSGTSYHGALTARAFMQRWCALPVDVCWP--FMLDDETLARSG 78
Cdd:COG2222    4 IAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPseLVVYPAYLKLEG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  79 kALVVGISQGGGSLSTLAAMERARNVGHITASMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVA 158
Cdd:COG2222   84 -TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAAWG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 159 GQQQrldgeqrrslllrMEKTFNHLPALITA--SQAWAQTNALALRDSADIRLTGPATLFGTVQEGALKMLETLRCPVSG 236
Cdd:COG2222  163 GDDA-------------LLAALDALPAALEAalAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 237 YEFEEFIHGIYNAFNAQSALIMLDPQPDARQ--DRLAQILGEWTPSIYRIGPQvENNGLNLNFPFVNDEDFAVFEYIIPL 314
Cdd:COG2222  230 YSAAEFRHGPKSLVDPGTLVVVLASEDPTREldLDLAAELRALGARVVAIGAE-DDAAITLPAIPDLHDALDPLLLLVVA 308

                        330
                 ....*....|....*
gi 553911965 315 QMLCAILPPQKGINP 329
Cdd:COG2222  309 QRLALALALARGLDP 323
 
Name Accession Description Interval E-value
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 33-158 9.05e-40

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: 136.47  E-value: 9.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  33 RIILTGSGTSYHGALTARAFMQRWCALPVDVCWPFMLDDETLARSGKALVVGISQGGGSLSTLAAMERARNVGHITASMA 112
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 553911965 113 GVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVA 158
Cdd:cd05008   81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 1-329 1.58e-34

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: 129.25  E-value: 1.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965   1 MNETPLRLLEMLTQTREDLWRAAQALTERGVTRIILTGSGTSYHGALTARAFMQRWCALPVDVCWP--FMLDDETLARSG 78
Cdd:COG2222    4 IAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPseLVVYPAYLKLEG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  79 kALVVGISQGGGSLSTLAAMERARNVGHITASMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVA 158
Cdd:COG2222   84 -TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAAWG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 159 GQQQrldgeqrrslllrMEKTFNHLPALITA--SQAWAQTNALALRDSADIRLTGPATLFGTVQEGALKMLETLRCPVSG 236
Cdd:COG2222  163 GDDA-------------LLAALDALPAALEAalAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 237 YEFEEFIHGIYNAFNAQSALIMLDPQPDARQ--DRLAQILGEWTPSIYRIGPQvENNGLNLNFPFVNDEDFAVFEYIIPL 314
Cdd:COG2222  230 YSAAEFRHGPKSLVDPGTLVVVLASEDPTREldLDLAAELRALGARVVAIGAE-DDAAITLPAIPDLHDALDPLLLLVVA 308

                        330
                 ....*....|....*
gi 553911965 315 QMLCAILPPQKGINP 329
Cdd:COG2222  309 QRLALALALARGLDP 323
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 201-340 2.14e-21

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: 88.86  E-value: 2.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 201 LRDSADIRLTGPATLFGTVQEGALKMLETLRCPVSGYEFEEFIHGIYNAFNAQSALIMLDPQPDARQ--DRLAQILGEWT 278
Cdd:cd05009   10 LKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEklESLIKEVKARG 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553911965 279 PSIYRIGPQVENNGLNLNFPFV--NDEDFAVFEYIIPLQMLCAILPPQKGINPAIPKDPQFHQK 340
Cdd:cd05009   90 AKVIVITDDGDAKDLADVVIRVpaTVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 7-187 4.68e-19

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: 88.15  E-value: 4.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965   7 RLLEMLTQTREDLWRAAQALteRGVTRIILTGSGTSYHGALTARAFMQRWCALPVDV-------CWPFMLDDETlarsgk 79
Cdd:COG0449  272 RLDEDGRVVLDELNLAAEDL--RNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVeiasefrYRDPVVDPGT------ 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  80 aLVVGISQGGGSLSTLAAMERARNVGHITASMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVAG 159
Cdd:COG0449  344 -LVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLAR 422

                        170       180       190
                 ....*....|....*....|....*....|
gi 553911965 160 QQQRLDGEQRRSLL--LRmektfnHLPALI 187
Cdd:COG0449  423 ARGTLSAEEEAELLeeLR------KLPEKI 446
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
29-187 2.70e-18

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 85.87  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  29 RGVTRIILTGSGTSYHGALTARAFMQRWCALPVDVCW-------PFMLDDETlarsgkaLVVGISQGGGSLSTLAAMERA 101
Cdd:PRK00331 287 KKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIasefryrDPVLSPKT-------LVIAISQSGETADTLAALRLA 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 102 RNVGHITASMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVAGQQQRLDGEQRRSLLLRMEktfn 181
Cdd:PRK00331 360 KELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELR---- 435


                 ....*.
gi 553911965 182 HLPALI 187
Cdd:PRK00331 436 ELPALI 441
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 31-333 7.39e-14

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 72.36  E-value: 7.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  31 VTRIILTGSGTSYHGALTARAFMQRWCAL-PVDVCWPFMLDDETLARSgKALVVGISQGGGSLSTLAAMERARNVGHITA 109
Cdd:PTZ00295 322 IKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVIDASELTLYRLPDE-DAGVIFISQSGETLDVVRALNLADELNLPKI 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 110 SMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVAGQQQRLDGEQRRSLLLR-MEKTFNHLPALIT 188
Cdd:PTZ00295 401 SVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKCSSLINsLHRLPTYIGMTLK 480

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 189 ASQAWAQTNALALRDSADIRLTGPATLFGTVQEGALKMLETLRCPVSGYEFEEFIHGIYNAFNAQSA----LIMLD---- 260
Cdd:PTZ00295 481 SCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEKNtpviLIILDdehk 560

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 261 -------PQPDARQDRL------AQILGEWTPSIYRIgpqvENNGLnLNfPFVNdedfavfeyIIPLQMLCAILPPQKGI 327
Cdd:PTZ00295 561 elminaaEQVKARGAYIivitddEDLVKDFADEIILI----PSNGP-LT-ALLA---------VIPLQLLAYEIAILRGI 625


                 ....*.
gi 553911965 328 NPAIPK 333
Cdd:PTZ00295 626 NPDKPR 631
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 33-156 3.85e-13

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: 65.78  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965   33 RIILTGSGTSYHGALTARAFMQRWCALPVDVCWPFMLDDETLARSGKA-LVVGISQGGGSLSTLAAMERARNVGHITASM 111
Cdd:pfam01380   7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDdLVIAISYSGETKDLLAAAELAKARGAKIIAI 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 553911965  112 AGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALA 156
Cdd:pfam01380  87 TDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
 
Name Accession Description Interval E-value
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 33-158 9.05e-40

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: 136.47  E-value: 9.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  33 RIILTGSGTSYHGALTARAFMQRWCALPVDVCWPFMLDDETLARSGKALVVGISQGGGSLSTLAAMERARNVGHITASMA 112
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 553911965 113 GVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVA 158
Cdd:cd05008   81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 1-329 1.58e-34

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: 129.25  E-value: 1.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965   1 MNETPLRLLEMLTQTREDLWRAAQALTERGVTRIILTGSGTSYHGALTARAFMQRWCALPVDVCWP--FMLDDETLARSG 78
Cdd:COG2222    4 IAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPseLVVYPAYLKLEG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  79 kALVVGISQGGGSLSTLAAMERARNVGHITASMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVA 158
Cdd:COG2222   84 -TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAAWG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 159 GQQQrldgeqrrslllrMEKTFNHLPALITA--SQAWAQTNALALRDSADIRLTGPATLFGTVQEGALKMLETLRCPVSG 236
Cdd:COG2222  163 GDDA-------------LLAALDALPAALEAalAADWPAAALAALADAERVVFLGRGPLYGLAREAALKLKELSAGHAEA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 237 YEFEEFIHGIYNAFNAQSALIMLDPQPDARQ--DRLAQILGEWTPSIYRIGPQvENNGLNLNFPFVNDEDFAVFEYIIPL 314
Cdd:COG2222  230 YSAAEFRHGPKSLVDPGTLVVVLASEDPTREldLDLAAELRALGARVVAIGAE-DDAAITLPAIPDLHDALDPLLLLVVA 308

                        330
                 ....*....|....*
gi 553911965 315 QMLCAILPPQKGINP 329
Cdd:COG2222  309 QRLALALALARGLDP 323
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 201-340 2.14e-21

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: 88.86  E-value: 2.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 201 LRDSADIRLTGPATLFGTVQEGALKMLETLRCPVSGYEFEEFIHGIYNAFNAQSALIMLDPQPDARQ--DRLAQILGEWT 278
Cdd:cd05009   10 LKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEklESLIKEVKARG 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553911965 279 PSIYRIGPQVENNGLNLNFPFV--NDEDFAVFEYIIPLQMLCAILPPQKGINPAIPKDPQFHQK 340
Cdd:cd05009   90 AKVIVITDDGDAKDLADVVIRVpaTVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 7-187 4.68e-19

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: 88.15  E-value: 4.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965   7 RLLEMLTQTREDLWRAAQALteRGVTRIILTGSGTSYHGALTARAFMQRWCALPVDV-------CWPFMLDDETlarsgk 79
Cdd:COG0449  272 RLDEDGRVVLDELNLAAEDL--RNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVeiasefrYRDPVVDPGT------ 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  80 aLVVGISQGGGSLSTLAAMERARNVGHITASMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVAG 159
Cdd:COG0449  344 -LVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLAR 422

                        170       180       190
                 ....*....|....*....|....*....|
gi 553911965 160 QQQRLDGEQRRSLL--LRmektfnHLPALI 187
Cdd:COG0449  423 ARGTLSAEEEAELLeeLR------KLPEKI 446
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
29-187 2.70e-18

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 85.87  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  29 RGVTRIILTGSGTSYHGALTARAFMQRWCALPVDVCW-------PFMLDDETlarsgkaLVVGISQGGGSLSTLAAMERA 101
Cdd:PRK00331 287 KKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIasefryrDPVLSPKT-------LVIAISQSGETADTLAALRLA 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 102 RNVGHITASMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVAGQQQRLDGEQRRSLLLRMEktfn 181
Cdd:PRK00331 360 KELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELR---- 435


                 ....*.
gi 553911965 182 HLPALI 187
Cdd:PRK00331 436 ELPALI 441
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 27-228 2.22e-16

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 80.18  E-value: 2.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  27 TERGVTRIILTGSGTSYHGALTARAFMQRWCALPV---------DVCWPFMLDDEtlarsgkalVVGISQGGGSLSTLAA 97
Cdd:PLN02981 359 TIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVtmelasdllDRQGPIYREDT---------AVFVSQSGETADTLRA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  98 MERARNVGHITASMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVAGQQqrLDGEQRRSLLlrME 177
Cdd:PLN02981 430 LEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQIVAMTMLALALGEDS--ISSRSRREAI--ID 505

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 553911965 178 KTFNhLP-ALITASQAWAQTNALA--LRDSADIRLTGPATLFGTVQEGALKMLE 228
Cdd:PLN02981 506 GLFD-LPnKVREVLKLDQEMKELAelLIDEQSLLVFGRGYNYATALEGALKVKE 558
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 31-333 7.39e-14

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 72.36  E-value: 7.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  31 VTRIILTGSGTSYHGALTARAFMQRWCAL-PVDVCWPFMLDDETLARSgKALVVGISQGGGSLSTLAAMERARNVGHITA 109
Cdd:PTZ00295 322 IKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVIDASELTLYRLPDE-DAGVIFISQSGETLDVVRALNLADELNLPKI 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 110 SMAGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVAGQQQRLDGEQRRSLLLR-MEKTFNHLPALIT 188
Cdd:PTZ00295 401 SVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKCSSLINsLHRLPTYIGMTLK 480

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 189 ASQAWAQTNALALRDSADIRLTGPATLFGTVQEGALKMLETLRCPVSGYEFEEFIHGIYNAFNAQSA----LIMLD---- 260
Cdd:PTZ00295 481 SCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEKNtpviLIILDdehk 560

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 261 -------PQPDARQDRL------AQILGEWTPSIYRIgpqvENNGLnLNfPFVNdedfavfeyIIPLQMLCAILPPQKGI 327
Cdd:PTZ00295 561 elminaaEQVKARGAYIivitddEDLVKDFADEIILI----PSNGP-LT-ALLA---------VIPLQLLAYEIAILRGI 625


                 ....*.
gi 553911965 328 NPAIPK 333
Cdd:PTZ00295 626 NPDKPR 631
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 33-245 8.11e-14

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 72.22  E-value: 8.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  33 RIILTGSGTSYHGALTARAFMQRWCALPVDV-CWPFMLDDETLARSGKALVVgISQGGGSLSTLAAMERARNVGHITASM 111
Cdd:PTZ00394 356 RILFIACGTSLNSCLAVRPLFEELVPLPISVeNASDFLDRRPRIQRDDVCFF-VSQSGETADTLMALQLCKEAGAMCVGI 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 112 AGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALAVAGQQQRLdgEQRRSLLLRmekTFNHLPALItaSQ 191
Cdd:PTZ00394 435 TNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRL--QERRNEIIR---GLAELPAAI--SE 507

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965 192 AWAQTN----ALA--LRDSADIRLTGPATLFGTVQEGALKMLETLRCPVSGYEFEEFIHG 245
Cdd:PTZ00394 508 CLKITHdpvkALAarLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELKHG 567
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 33-156 3.85e-13

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: 65.78  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965   33 RIILTGSGTSYHGALTARAFMQRWCALPVDVCWPFMLDDETLARSGKA-LVVGISQGGGSLSTLAAMERARNVGHITASM 111
Cdd:pfam01380   7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDdLVIAISYSGETKDLLAAAELAKARGAKIIAI 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 553911965  112 AGVAPATIDRAADYILTVPCGEETAGAKTKGYHCTVLNLMLLALA 156
Cdd:pfam01380  87 TDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 72-136 4.47e-07

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 49.47  E-value: 4.47e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553911965  72 ETLARSGKaLVVGISQGGGSLSTLAAMERARNVGHITASMAGVAPATIDRAADYILTVPCgEETA 136
Cdd:PRK13937 101 EALGRPGD-VLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLIVPS-DDTP 163
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 17-135 1.06e-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: 44.53  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  17 EDLWRAAQALTERGvtRIILTGSGTSyhgALTARAFMQRWCALPVDVcwpFMLDDETLARSGKA------LVVGISQGGG 90
Cdd:cd05013    1 EALEKAVDLLAKAR--RIYIFGVGSS---GLVAEYLAYKLLRLGKPV---VLLSDPHLQLMSAAnltpgdVVIAISFSGE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 553911965  91 SLSTLAAMERARNVGHITASMAGVAPATIDRAADYILTVPCGEET 135
Cdd:cd05013   73 TKETVEAAEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGD 117
frlB PRK11382
fructoselysine 6-phosphate deglycase;
26-127 4.87e-04

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 41.53  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553911965  26 LTERGVTRIILTGSGTSYHGALTARAFMQRWCALPVDVCWPFMLDDETLAR-SGKALVVGISQGGGSLSTLAAMERARNV 104
Cdd:PRK11382  39 MVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRlDDRCAVIGVSDYGKTEEVIKALELGRAC 118

                         90       100
                 ....*....|....*....|...
gi 553911965 105 GHITASMAGVAPATIDRAADYIL 127
Cdd:PRK11382 119 GALTAAFTKRADSPITSAAEFSI 141
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 72-130 8.61e-04

Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).


Pssm-ID: 240139 [Multi-domain]  Cd Length: 177  Bit Score: 39.80  E-value: 8.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 553911965  72 ETLARSGKALVvGISQGGGSLSTLAAMERARNVGHITASMAGVAPATIDRAADYILTVP 130
Cdd:cd05006   96 EALGQPGDVLI-GISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVP 153
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 33-105 3.50e-03

The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.


Pssm-ID: 240148 [Multi-domain]  Cd Length: 119  Bit Score: 36.86  E-value: 3.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553911965  33 RIILTGSGTSYHGALTARAFMQRWCALPVdvcwpFMLDDETLAR--SGKALVVGISQGGGSLSTLAAMERARNVG 105
Cdd:cd05017    1 NIVILGMGGSGIGGDLLESLLLDEAKIPV-----YVVKDYTLPAfvDRKTLVIAVSYSGNTEETLSAVEQAKERG 70
 
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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