NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490248837|ref|WP_004146946|]
View 

MULTISPECIES: SIS domain-containing protein [Klebsiella]

Protein Classification

SIS domain-containing protein( domain architecture ID 11454870)

SIS (sugar isomerase) domain-containing protein such as Bacillus subtilis fructosamine deglycase FrlB, which catalyzes the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid

CATH:  3.40.50.10490
EC:  3.5.-.-
Gene Ontology:  GO:0097367|GO:0005975|GO:0016787
PubMed:  10203754
SCOP:  4000802

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 38-153 4.08e-45

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: 150.03  E-value: 4.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  38 LFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAIT 117
Cdd:cd05710    2 VFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLT 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490248837 118 RHADSPLAAAASWHIPM-CHKNGVEYEYMLLYWLFFR 153
Cdd:cd05710   82 DDEDSPLAKLADYVIVYgFEIDAVEEKYLLLYMLALR 118
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 18-333 9.01e-42

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: 148.12  E-value: 9.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  18 AARKQAETVADDIYDSGCSALFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTK 97
Cdd:COG2222   17 ALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  98 ESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHIPMC--HKNGV----EYEYMLL--YWLFfrvifrhGEFADYARFAS 169
Cdd:COG2222   97 EVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPagPEKSVaatkSFTTMLLalLALL-------AAWGGDDALLA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 170 QLELLPENLLQAKRQFDPRADSIAAQyhDCDYMMWIGGAEMWGEVYLFSMcILEEMQWKRTKSVSSAEFFHGTLELLEKE 249
Cdd:COG2222  170 ALDALPAALEAALAADWPAAALAALA--DAERVVFLGRGPLYGLAREAAL-KLKELSAGHAEAYSAAEFRHGPKSLVDPG 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 250 VPLFLVKGEGRCRALDERVERFAEKITDHLVVIDPRDYPLNGID--DAFRWIMAPcVVSTLLVDRLAAHFEHYTGHDLNI 327
Cdd:COG2222  247 TLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPaiPDLHDALDP-LLLLVVAQRLALALALARGLDPDT 325


                 ....*.
gi 490248837 328 RRYYRQ 333
Cdd:COG2222  326 PRHLNK 331
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 38-153 4.08e-45

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: 150.03  E-value: 4.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  38 LFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAIT 117
Cdd:cd05710    2 VFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLT 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490248837 118 RHADSPLAAAASWHIPM-CHKNGVEYEYMLLYWLFFR 153
Cdd:cd05710   82 DDEDSPLAKLADYVIVYgFEIDAVEEKYLLLYMLALR 118
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 18-333 9.01e-42

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: 148.12  E-value: 9.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  18 AARKQAETVADDIYDSGCSALFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTK 97
Cdd:COG2222   17 ALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  98 ESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHIPMC--HKNGV----EYEYMLL--YWLFfrvifrhGEFADYARFAS 169
Cdd:COG2222   97 EVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPagPEKSVaatkSFTTMLLalLALL-------AAWGGDDALLA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 170 QLELLPENLLQAKRQFDPRADSIAAQyhDCDYMMWIGGAEMWGEVYLFSMcILEEMQWKRTKSVSSAEFFHGTLELLEKE 249
Cdd:COG2222  170 ALDALPAALEAALAADWPAAALAALA--DAERVVFLGRGPLYGLAREAAL-KLKELSAGHAEAYSAAEFRHGPKSLVDPG 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 250 VPLFLVKGEGRCRALDERVERFAEKITDHLVVIDPRDYPLNGID--DAFRWIMAPcVVSTLLVDRLAAHFEHYTGHDLNI 327
Cdd:COG2222  247 TLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPaiPDLHDALDP-LLLLVVAQRLALALALARGLDPDT 325


                 ....*.
gi 490248837 328 RRYYRQ 333
Cdd:COG2222  326 PRHLNK 331
frlB PRK11382
fructoselysine 6-phosphate deglycase;
25-331 5.76e-21

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 91.99  E-value: 5.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  25 TVADDIYDSGCSALFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAE 104
Cdd:PRK11382  34 AIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 105 WCKAQGIRVVAITRHADSPLAAAASWHIPMCHKNGVEYEYMLLYWLFFRVIFRHGEFADYARFASQLELLPENLLQAKRQ 184
Cdd:PRK11382 114 LGRACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRT 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 185 FDPRADSIAAQYHDCDYMMWIGGAEMWGEVYLFSMCILEEMQWKRTKSVSSAEFFHGTLELLEKEVPLFLVKGEGRCRAL 264
Cdd:PRK11382 194 WEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHT 273

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490248837 265 DERVERFAEKITDHLVVIDPRDyplngIDDAFRWIMAPCVVSTLLvDRLAAHFEHYTGHDLNIRRYY 331
Cdd:PRK11382 274 TERAINFVKQRTDNVIVIDYAE-----ISQGLHPWLAPFLMFVPM-EWLCYYLSIYKDHNPDERRYY 334
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 187-332 5.72e-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: 71.14  E-value: 5.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 187 PRADSIAAQYHDCDYMMWIGGAEMWGeVYLFSMCILEEMQWKRTKSVSSAEFFHGTLELLEKEVPLFLVKGEGRCRALDE 266
Cdd:cd05009    1 EDIKELAEKLKEAKSFYVLGRGPNYG-TALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490248837 267 RVERFAEKITDHLVVIDPRDYPLNGIDDAFR-----WIMAPcVVSTLLVDRLAAHFEHYTGHDLNIRRYYR 332
Cdd:cd05009   80 SLIKEVKARGAKVIVITDDGDAKDLADVVIRvpatvEELSP-LLYIVPLQLLAYHLAVARGIDPDKPRNLA 149
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 81-133 3.39e-10

DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 59.94  E-value: 3.39e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490248837  81 LNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHIP 133
Cdd:COG1737  180 LGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLY 232
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 58-132 9.75e-10

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 55.77  E-value: 9.75e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490248837   58 KELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHI 132
Cdd:pfam01380  28 EEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVL 102
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 38-252 2.38e-07

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 52.19  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  38 LFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRgHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAIT 117
Cdd:PTZ00394 357 ILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDR-RPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGIT 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 118 RHADSPLAAAASWHIPMchKNGVEYE------------YMLLYWLFF-----RVIFRHGEFADyarfasQLELLPENLLQ 180
Cdd:PTZ00394 436 NVVGSSISRLTHYAIHL--NAGVEVGvastkaytsqvvVLTLVALLLssdsvRLQERRNEIIR------GLAELPAAISE 507

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490248837 181 AKRQFDPRADSIAAQYHDCDYMMWIG-GAEMwgEVYLFSMCILEEMQWKRTKSVSSAEFFHGTLELLEKEVPL 252
Cdd:PTZ00394 508 CLKITHDPVKALAARLKESSSILVLGrGYDL--ATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPV 578
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 38-153 4.08e-45

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: 150.03  E-value: 4.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  38 LFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAIT 117
Cdd:cd05710    2 VFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLT 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490248837 118 RHADSPLAAAASWHIPM-CHKNGVEYEYMLLYWLFFR 153
Cdd:cd05710   82 DDEDSPLAKLADYVIVYgFEIDAVEEKYLLLYMLALR 118
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 18-333 9.01e-42

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: 148.12  E-value: 9.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  18 AARKQAETVADDIYDSGCSALFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTK 97
Cdd:COG2222   17 ALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  98 ESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHIPMC--HKNGV----EYEYMLL--YWLFfrvifrhGEFADYARFAS 169
Cdd:COG2222   97 EVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPagPEKSVaatkSFTTMLLalLALL-------AAWGGDDALLA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 170 QLELLPENLLQAKRQFDPRADSIAAQyhDCDYMMWIGGAEMWGEVYLFSMcILEEMQWKRTKSVSSAEFFHGTLELLEKE 249
Cdd:COG2222  170 ALDALPAALEAALAADWPAAALAALA--DAERVVFLGRGPLYGLAREAAL-KLKELSAGHAEAYSAAEFRHGPKSLVDPG 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 250 VPLFLVKGEGRCRALDERVERFAEKITDHLVVIDPRDYPLNGID--DAFRWIMAPcVVSTLLVDRLAAHFEHYTGHDLNI 327
Cdd:COG2222  247 TLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPaiPDLHDALDP-LLLLVVAQRLALALALARGLDPDT 325


                 ....*.
gi 490248837 328 RRYYRQ 333
Cdd:COG2222  326 PRHLNK 331
frlB PRK11382
fructoselysine 6-phosphate deglycase;
25-331 5.76e-21

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 91.99  E-value: 5.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  25 TVADDIYDSGCSALFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAE 104
Cdd:PRK11382  34 AIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 105 WCKAQGIRVVAITRHADSPLAAAASWHIPMCHKNGVEYEYMLLYWLFFRVIFRHGEFADYARFASQLELLPENLLQAKRQ 184
Cdd:PRK11382 114 LGRACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRT 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 185 FDPRADSIAAQYHDCDYMMWIGGAEMWGEVYLFSMCILEEMQWKRTKSVSSAEFFHGTLELLEKEVPLFLVKGEGRCRAL 264
Cdd:PRK11382 194 WEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHT 273

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490248837 265 DERVERFAEKITDHLVVIDPRDyplngIDDAFRWIMAPCVVSTLLvDRLAAHFEHYTGHDLNIRRYY 331
Cdd:PRK11382 274 TERAINFVKQRTDNVIVIDYAE-----ISQGLHPWLAPFLMFVPM-EWLCYYLSIYKDHNPDERRYY 334
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 187-332 5.72e-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: 71.14  E-value: 5.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 187 PRADSIAAQYHDCDYMMWIGGAEMWGeVYLFSMCILEEMQWKRTKSVSSAEFFHGTLELLEKEVPLFLVKGEGRCRALDE 266
Cdd:cd05009    1 EDIKELAEKLKEAKSFYVLGRGPNYG-TALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490248837 267 RVERFAEKITDHLVVIDPRDYPLNGIDDAFR-----WIMAPcVVSTLLVDRLAAHFEHYTGHDLNIRRYYR 332
Cdd:cd05009   80 SLIKEVKARGAKVIVITDDGDAKDLADVVIRvpatvEELSP-LLYIVPLQLLAYHLAVARGIDPDKPRNLA 149
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 38-117 1.93e-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.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 65.09  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  38 LFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRGHKKL-NKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAI 116
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                 .
gi 490248837 117 T 117
Cdd:cd04795   81 T 81
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 56-135 2.49e-13

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: 65.98  E-value: 2.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  56 FAKELTSVPVYLEQAAELIHRGhKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHIPMC 135
Cdd:cd05008   20 LLERLAGIPVEVEAASEFRYRR-PLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVLYLR 98
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 81-133 3.39e-10

DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 59.94  E-value: 3.39e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490248837  81 LNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHIP 133
Cdd:COG1737  180 LGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLY 232
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 24-133 3.84e-10

RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.


Pssm-ID: 240144 [Multi-domain]  Cd Length: 139  Bit Score: 57.24  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  24 ETVADDIYDSGcsALFFASVGGSLapMMAiNEFAKELTSV--PVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVA 101
Cdd:cd05013    4 EKAVDLLAKAR--RIYIFGVGSSG--LVA-EYLAYKLLRLgkPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVE 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490248837 102 IAEWCKAQGIRVVAITRHADSPLAAAASWHIP 133
Cdd:cd05013   79 AAEIAKERGAKVIAITDSANSPLAKLADIVLL 110
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 58-132 9.75e-10

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 55.77  E-value: 9.75e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490248837   58 KELTSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHI 132
Cdd:pfam01380  28 EEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLAREADHVL 102
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 81-134 7.29e-09

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: 56.14  E-value: 7.29e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490248837  81 LNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHIPM 134
Cdd:COG0794   89 ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDL 142
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 61-134 3.66e-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: 3.66e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490248837  61 TSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHIPM 134
Cdd:cd05014   25 TGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDL 98
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 38-252 2.38e-07

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 52.19  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  38 LFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRgHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAIT 117
Cdd:PTZ00394 357 ILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDR-RPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGIT 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837 118 RHADSPLAAAASWHIPMchKNGVEYE------------YMLLYWLFF-----RVIFRHGEFADyarfasQLELLPENLLQ 180
Cdd:PTZ00394 436 NVVGSSISRLTHYAIHL--NAGVEVGvastkaytsqvvVLTLVALLLssdsvRLQERRNEIIR------GLAELPAAISE 507

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490248837 181 AKRQFDPRADSIAAQYHDCDYMMWIG-GAEMwgEVYLFSMCILEEMQWKRTKSVSSAEFFHGTLELLEKEVPL 252
Cdd:PTZ00394 508 CLKITHDPVKALAARLKESSSILVLGrGYDL--ATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPV 578
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
81-135 5.99e-05

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 43.98  E-value: 5.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490248837  81 LNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAAswHIPMC 135
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLA--DYVIC 237
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 86-128 9.12e-05

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: 42.56  E-value: 9.12e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 490248837  86 VVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAA 128
Cdd:cd05005   78 LLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLA 120
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 86-134 9.43e-05

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 43.44  E-value: 9.43e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 490248837  86 VVVTLSKSGDTKESVAIAEWCKAQGIRVVAITrHADSPLAAAASWHIPM 134
Cdd:PRK11302 178 VVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPLAREATLALTL 225
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
79-130 1.45e-04

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 42.76  E-value: 1.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490248837  79 KKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASW 130
Cdd:PRK15482 178 QALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHF 229
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 38-118 1.17e-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: 38.40  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  38 LFFASVGGSLAP--MMAINEFAKEltSVPVYLEQAAELihrgHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVA 115
Cdd:cd05017    2 IVILGMGGSGIGgdLLESLLLDEA--KIPVYVVKDYTL----PAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVA 75


                 ...
gi 490248837 116 ITR 118
Cdd:cd05017   76 ITS 78
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 35-125 1.22e-03

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 40.50  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  35 CSALFFASVGGSLAPMMAINEFAKELTSVPVYLEQAAELIHRgHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVV 114
Cdd:PLN02981 363 SRRIVFIGCGTSYNAALAARPILEELSGVPVTMELASDLLDR-QGPIYREDTAVFVSQSGETADTLRALEYAKENGALCV 441

                         90
                 ....*....|.
gi 490248837 115 AITRHADSPLA 125
Cdd:PLN02981 442 GITNTVGSAIS 452
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 38-117 1.83e-03

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 39.58  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248837  38 LFFASVGGSLAPMMAINEFAKELTSVPVYLeqaaeliHRGHK---KLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVV 114
Cdd:PRK08674  37 IVISGMGGSGIGGDLLRILLFDELKVPVFV-------NRDYTlpaFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKII 109


                 ...
gi 490248837 115 AIT 117
Cdd:PRK08674 110 AIT 112
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
61-128 7.80e-03

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 37.82  E-value: 7.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490248837  61 TSVPVYLEQAAELIHRGHKKLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAA 128
Cdd:PRK11543  67 TGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAA 134
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 70-132 9.86e-03

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 37.07  E-value: 9.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490248837  70 AAELIHRGhkkLNKDAVVVTLSKSGDTKESVAIAEWCKAQGIRVVAITRHADSPLAAAASWHI 132
Cdd:PRK05441 121 AADLKAIN---LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAI 180
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH