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Conserved domains on  [gi|526089192|ref|WP_020839503|]
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SIS domain-containing protein [Salmonella enterica]

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

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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 ...
 23-148 5.58e-53

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: 170.06  E-value: 5.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  23 RVWFVGCGGSLTGFWPGKYFLDCEaSKLAVGYITSNEFVHATPKALGKNSVVILASQQGNTAETVAAARVAREKGAATIG 102
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKE-SKLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 526089192 103 LVYQPDTPLCEYSDYIIEYQWarypeTVDPAQQKAAYSLWLALEIL 148
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGF-----EIDAVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 4-326 1.14e-43

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: 152.75  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192   4 AHENARRIISDILGK---QNIERVWFVGCGGSltgfW----PGKYFLdCEASKLAVGYITSNEFVHATPKALGKNSVVIL 76
Cdd:COG2222   14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  77 ASQQGNTAETVAAARVAREKGAATIGLVYQPDTPLCEYSDYIIEYqwaryPETVDP--AQQKAAY-SLWLALEILAQteg 153
Cdd:COG2222   89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPL-----PAGPEKsvAATKSFTtMLLALLALLAA--- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 154 YAQYDELVSAFGRFSDVVHGAQRQVQEDAQrfAAAWKDEKVVYMMGSGPSFGAAHqESICILLEMQWINSASIHSGEYFH 233
Cdd:COG2222  161 WGGDDALLAALDALPAALEAALAADWPAAA--LAALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSAAEFRH 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 234 GPFEITEPGTQFILLQSSGRTRPLDDRAIRFIERYQGKLQLIDADKLGIQDLPT--DVGEYFCGLLHNCVLDVYNLALAT 311
Cdd:COG2222  238 GPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPAipDLHDALDPLLLLVVAQRLALALAL 317

                        330
                 ....*....|....*
gi 526089192 312 ARNHPLTTRRYMWKV 326
Cdd:COG2222  318 ARGLDPDTPRHLNKV 332
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 23-148 5.58e-53

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: 170.06  E-value: 5.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  23 RVWFVGCGGSLTGFWPGKYFLDCEaSKLAVGYITSNEFVHATPKALGKNSVVILASQQGNTAETVAAARVAREKGAATIG 102
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKE-SKLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 526089192 103 LVYQPDTPLCEYSDYIIEYQWarypeTVDPAQQKAAYSLWLALEIL 148
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGF-----EIDAVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 4-326 1.14e-43

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: 152.75  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192   4 AHENARRIISDILGK---QNIERVWFVGCGGSltgfW----PGKYFLdCEASKLAVGYITSNEFVHATPKALGKNSVVIL 76
Cdd:COG2222   14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  77 ASQQGNTAETVAAARVAREKGAATIGLVYQPDTPLCEYSDYIIEYqwaryPETVDP--AQQKAAY-SLWLALEILAQteg 153
Cdd:COG2222   89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPL-----PAGPEKsvAATKSFTtMLLALLALLAA--- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 154 YAQYDELVSAFGRFSDVVHGAQRQVQEDAQrfAAAWKDEKVVYMMGSGPSFGAAHqESICILLEMQWINSASIHSGEYFH 233
Cdd:COG2222  161 WGGDDALLAALDALPAALEAALAADWPAAA--LAALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSAAEFRH 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 234 GPFEITEPGTQFILLQSSGRTRPLDDRAIRFIERYQGKLQLIDADKLGIQDLPT--DVGEYFCGLLHNCVLDVYNLALAT 311
Cdd:COG2222  238 GPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPAipDLHDALDPLLLLVVAQRLALALAL 317

                        330
                 ....*....|....*
gi 526089192 312 ARNHPLTTRRYMWKV 326
Cdd:COG2222  318 ARGLDPDTPRHLNKV 332
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 180-327 1.52e-31

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: 115.82  E-value: 1.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 180 EDAQRFAAAWKDEKVVYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITEPGTQFILLQSSGRTRPLDD 259
Cdd:cd05009    1 EDIKELAEKLKEAKSFYVLGRGPNYGTA-LEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526089192 260 RAIRFIERYQGKLQLIDADKLGIQD------LPtDVGEYFCGLLHNCVLDVYNLALATAR-NHPLTTRRYMWKVE 327
Cdd:cd05009   80 SLIKEVKARGAKVIVITDDGDAKDLadvvirVP-ATVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKSVT 153
frlB PRK11382
fructoselysine 6-phosphate deglycase;
12-276 2.58e-28

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 112.02  E-value: 2.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  12 ISDILGKQNIERVWFVGCGGSLTGFWPGKYFLDcEASKLAVGYITSNEFVHATPKALGKNSVVILASQQGNTAETVAAAR 91
Cdd:PRK11382  35 IVEEMVKRDIDRIYFVACGSPLNAAQTAKHLAD-RFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  92 VAREKGAATIGLVYQPDTPLCEYSDYIIEYQwaryPETVDPAQQKAAYSLwlALEILAQTEGYAQYDELVSAFGRFSDVV 171
Cdd:PRK11382 114 LGRACGALTAAFTKRADSPITSAAEFSIDYQ----ADCIWEIHLLLCYSV--VLEMITRLAPNAEIGKIKNDLKQLPNAL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 172 HGAQRQVQEDAQRFAAAWKDEKVVYMMGSGPSFGAAHQESICILLEMQWINSASIHSGEYFHGPFEITEPGTQFILLQSS 251
Cdd:PRK11382 188 GHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGN 267

                        250       260
                 ....*....|....*....|....*
gi 526089192 252 GRTRPLDDRAIRFIERYQGKLQLID 276
Cdd:PRK11382 268 DESRHTTERAINFVKQRTDNVIVID 292
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 23-119 2.40e-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. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 60.39  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192   23 RVWFVGCGGSltgfwpgkYFLdCEASKLAVGYITSN--------EFVHATPKALGKNSVVILASQQGNTAETVAAARVAR 94
Cdd:pfam01380   7 RIFVIGRGTS--------YAI-ALELALKFEEIGYKvvevelasELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAK 77

                          90       100
                  ....*....|....*....|....*
gi 526089192   95 EKGAATIGLVYQPDTPLCEYSDYII 119
Cdd:pfam01380  78 ARGAKIIAITDSPGSPLAREADHVL 102
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 22-172 1.97e-09

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 57.63  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  22 ERVWFVGCGGSltgFWPGKYFldceASKL------AVGYITSNEFVHATPKALGKNSVVILASQQGNTAETVAAARVARE 95
Cdd:COG1737  135 RRIYIFGVGAS---APVAEDL----AYKLlrlgknVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKE 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  96 KGAATIGLVYQPDTPLCEYSDYIIeyqwaRYPETVDPAQQKAAYSLWLAL---EILAqtEGYAQ--YDELVSAFGRFSDV 170
Cdd:COG1737  208 RGAKVIAITDSPLSPLAKLADVVL-----YVPSEEPTLRSSAFSSRVAQLaliDALA--AAVAQrdGDKARERLERTEAL 280


                 ..
gi 526089192 171 VH 172
Cdd:COG1737  281 LS 282
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
19-104 2.67e-07

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 51.97  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  19 QNIERVWFVGCGGS----LTGfwpgKYFLdceaSKLA-----VGYitSNEFVHATPkALGKNSVVILASQQGNTAETVAA 89
Cdd:PRK00331 287 KKIDRIYIVACGTSyhagLVA----KYLI----ESLAgipveVEI--ASEFRYRDP-VLSPKTLVIAISQSGETADTLAA 355

                         90
                 ....*....|....*
gi 526089192  90 ARVAREKGAATIGLV 104
Cdd:PRK00331 356 LRLAKELGAKTLAIC 370
 
Name Accession Description Interval E-value
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 23-148 5.58e-53

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: 170.06  E-value: 5.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  23 RVWFVGCGGSLTGFWPGKYFLDCEaSKLAVGYITSNEFVHATPKALGKNSVVILASQQGNTAETVAAARVAREKGAATIG 102
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKE-SKLPVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 526089192 103 LVYQPDTPLCEYSDYIIEYQWarypeTVDPAQQKAAYSLWLALEIL 148
Cdd:cd05710   80 LTDDEDSPLAKLADYVIVYGF-----EIDAVEEKYLLLYMLALRLL 120
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 4-326 1.14e-43

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: 152.75  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192   4 AHENARRIISDILGK---QNIERVWFVGCGGSltgfW----PGKYFLdCEASKLAVGYITSNEFVHATPKALGKNSVVIL 76
Cdd:COG2222   14 ALAALAAAIAALLARlraKPPRRVVLVGAGSS----DhaaqAAAYLL-ERLLGIPVAALAPSELVVYPAYLKLEGTLVVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  77 ASQQGNTAETVAAARVAREKGAATIGLVYQPDTPLCEYSDYIIEYqwaryPETVDP--AQQKAAY-SLWLALEILAQteg 153
Cdd:COG2222   89 ISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPL-----PAGPEKsvAATKSFTtMLLALLALLAA--- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 154 YAQYDELVSAFGRFSDVVHGAQRQVQEDAQrfAAAWKDEKVVYMMGSGPSFGAAHqESICILLEMQWINSASIHSGEYFH 233
Cdd:COG2222  161 WGGDDALLAALDALPAALEAALAADWPAAA--LAALADAERVVFLGRGPLYGLAR-EAALKLKELSAGHAEAYSAAEFRH 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 234 GPFEITEPGTQFILLQSSGRTRPLDDRAIRFIERYQGKLQLIDADKLGIQDLPT--DVGEYFCGLLHNCVLDVYNLALAT 311
Cdd:COG2222  238 GPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAITLPAipDLHDALDPLLLLVVAQRLALALAL 317

                        330
                 ....*....|....*
gi 526089192 312 ARNHPLTTRRYMWKV 326
Cdd:COG2222  318 ARGLDPDTPRHLNKV 332
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 180-327 1.52e-31

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: 115.82  E-value: 1.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 180 EDAQRFAAAWKDEKVVYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITEPGTQFILLQSSGRTRPLDD 259
Cdd:cd05009    1 EDIKELAEKLKEAKSFYVLGRGPNYGTA-LEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 526089192 260 RAIRFIERYQGKLQLIDADKLGIQD------LPtDVGEYFCGLLHNCVLDVYNLALATAR-NHPLTTRRYMWKVE 327
Cdd:cd05009   80 SLIKEVKARGAKVIVITDDGDAKDLadvvirVP-ATVEELSPLLYIVPLQLLAYHLAVARgIDPDKPRNLAKSVT 153
frlB PRK11382
fructoselysine 6-phosphate deglycase;
12-276 2.58e-28

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 112.02  E-value: 2.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  12 ISDILGKQNIERVWFVGCGGSLTGFWPGKYFLDcEASKLAVGYITSNEFVHATPKALGKNSVVILASQQGNTAETVAAAR 91
Cdd:PRK11382  35 IVEEMVKRDIDRIYFVACGSPLNAAQTAKHLAD-RFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  92 VAREKGAATIGLVYQPDTPLCEYSDYIIEYQwaryPETVDPAQQKAAYSLwlALEILAQTEGYAQYDELVSAFGRFSDVV 171
Cdd:PRK11382 114 LGRACGALTAAFTKRADSPITSAAEFSIDYQ----ADCIWEIHLLLCYSV--VLEMITRLAPNAEIGKIKNDLKQLPNAL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 172 HGAQRQVQEDAQRFAAAWKDEKVVYMMGSGPSFGAAHQESICILLEMQWINSASIHSGEYFHGPFEITEPGTQFILLQSS 251
Cdd:PRK11382 188 GHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGN 267

                        250       260
                 ....*....|....*....|....*
gi 526089192 252 GRTRPLDDRAIRFIERYQGKLQLID 276
Cdd:PRK11382 268 DESRHTTERAINFVKQRTDNVIVID 292
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 23-147 5.86e-16

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: 72.91  E-value: 5.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  23 RVWFVGCGGSL-TGFwPGKYFLDcEASKLAVGYITSNEFVHATPkALGKNSVVILASQQGNTAETVAAARVAREKGAATI 101
Cdd:cd05008    1 RILIVGCGTSYhAAL-VAKYLLE-RLAGIPVEVEAASEFRYRRP-LLDEDTLVIAISQSGETADTLAALRLAKEKGAKTV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 526089192 102 GLVYQPDTPLCEYSDYIIeYQWARYPETVdpAQQKAAYS-----LWLALEI 147
Cdd:cd05008   78 AITNVVGSTLAREADYVL-YLRAGPEISV--AATKAFTSqllalLLLALAL 125
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 23-279 3.01e-12

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 67.21  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  23 RVWFVGCGGSLTGFWPGKYFLDcEASKLAVGYITSNEFVHATPKaLGKNSVVILASQQGNTAETVAAARVAREKGAATIG 102
Cdd:PTZ00394 356 RILFIACGTSLNSCLAVRPLFE-ELVPLPISVENASDFLDRRPR-IQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVG 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 103 LVYQPDTPLCEYSDYIIEYQWArypETVDPAQQKAAYSLWLALEILA----QTEGYAQ--YDELVSAFGRFSDVVHGAQR 176
Cdd:PTZ00394 434 ITNVVGSSISRLTHYAIHLNAG---VEVGVASTKAYTSQVVVLTLVAlllsSDSVRLQerRNEIIRGLAELPAAISECLK 510

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192 177 QVQEDAQRFAAAWKDEKVVYMMGSGPSFGAAhQESICILLEMQWINSASIHSGEYFHGPFEITEPGTQFILLQSSGRTRP 256
Cdd:PTZ00394 511 ITHDPVKALAARLKESSSILVLGRGYDLATA-MEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFG 589

                        250       260
                 ....*....|....*....|...
gi 526089192 257 LDDRAIRFIERYQGKLQLIDADK 279
Cdd:PTZ00394 590 LSKSAVQQVKARGGAVVVFATEV 612
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 23-119 2.40e-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. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 60.39  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192   23 RVWFVGCGGSltgfwpgkYFLdCEASKLAVGYITSN--------EFVHATPKALGKNSVVILASQQGNTAETVAAARVAR 94
Cdd:pfam01380   7 RIFVIGRGTS--------YAI-ALELALKFEEIGYKvvevelasELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAK 77

                          90       100
                  ....*....|....*....|....*
gi 526089192   95 EKGAATIGLVYQPDTPLCEYSDYII 119
Cdd:pfam01380  78 ARGAKIIAITDSPGSPLAREADHVL 102
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 22-122 2.30e-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: 58.01  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  22 ERVWFVGCGGSltgFWPGKYFldceASKL-----AVGYITSNEFVHATPKALGKNSVVILASQQGNTAETVAAARVAREK 96
Cdd:cd05013   14 RRIYIFGVGSS---GLVAEYL----AYKLlrlgkPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86

                         90       100
                 ....*....|....*....|....*.
gi 526089192  97 GAATIGLVYQPDTPLCEYSDYIIEYQ 122
Cdd:cd05013   87 GAKVIAITDSANSPLAKLADIVLLVS 112
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 22-172 1.97e-09

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 57.63  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  22 ERVWFVGCGGSltgFWPGKYFldceASKL------AVGYITSNEFVHATPKALGKNSVVILASQQGNTAETVAAARVARE 95
Cdd:COG1737  135 RRIYIFGVGAS---APVAEDL----AYKLlrlgknVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKE 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  96 KGAATIGLVYQPDTPLCEYSDYIIeyqwaRYPETVDPAQQKAAYSLWLAL---EILAqtEGYAQ--YDELVSAFGRFSDV 170
Cdd:COG1737  208 RGAKVIAITDSPLSPLAKLADVVL-----YVPSEEPTLRSSAFSSRVAQLaliDALA--AAVAQrdGDKARERLERTEAL 280


                 ..
gi 526089192 171 VH 172
Cdd:COG1737  281 LS 282
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 3-120 3.59e-08

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: 52.58  E-value: 3.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192   3 VAHENARRIISDIlgkQNIERVWFVGCGGSltGFwPGKYFldceASKLA--------VGYITsnefvhaTPkALGKNSVV 74
Cdd:cd05005   18 IDEEELDKLISAI---LNAKRIFVYGAGRS--GL-VAKAF----AMRLMhlglnvyvVGETT-------TP-AIGPGDLL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 526089192  75 ILASQQGNTAETVAAARVAREKGAATIGLVYQPDTPLCEYSDYIIE 120
Cdd:cd05005   80 IAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
19-104 2.67e-07

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 51.97  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  19 QNIERVWFVGCGGS----LTGfwpgKYFLdceaSKLA-----VGYitSNEFVHATPkALGKNSVVILASQQGNTAETVAA 89
Cdd:PRK00331 287 KKIDRIYIVACGTSyhagLVA----KYLI----ESLAgipveVEI--ASEFRYRDP-VLSPKTLVIAISQSGETADTLAA 355

                         90
                 ....*....|....*
gi 526089192  90 ARVAREKGAATIGLV 104
Cdd:PRK00331 356 LRLAKELGAKTLAIC 370
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 68-120 3.16e-06

N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.


Pssm-ID: 240140 [Multi-domain]  Cd Length: 257  Bit Score: 47.52  E-value: 3.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 526089192  68 LGKNSVVILASQQGNTAETVAAARVAREKGAATIGLVYQPDTPLCEYSDYIIE 120
Cdd:cd05007  116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIA 168
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 68-120 1.15e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 43.23  E-value: 1.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 526089192  68 LGKNSVVILASQQGNTAETVAAARVAREKGAATIGLVYQPDTPLCEYSDYIIE 120
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIE 181
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 23-101 1.54e-04

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: 40.71  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  23 RVWFVGCGGSltgFWPGKYFLDCEASKLAVgyitsNEFVHAT---PKALGKNSVVILASQQGNTAETVAAARVAREKGAA 99
Cdd:cd05017    1 NIVILGMGGS---GIGGDLLESLLLDEAKI-----PVYVVKDytlPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAK 72


                 ..
gi 526089192 100 TI 101
Cdd:cd05017   73 IV 74
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
28-152 1.81e-04

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 42.38  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  28 GCGGS-LTGfwpgkyfLDCEASKLAVGYITSNE---FVHAT-PKALGKNSVVILASQQGNTAETVAAARVAREKGAATIG 102
Cdd:PRK15482 142 GLGGSaLVG-------RDLSFKLMKIGYRVACEadtHVQATvSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIA 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 526089192 103 LVYQPDTPLCEYSDYII-----EYQWARYPETVDPAQQKAAYSLWLALEILAQTE 152
Cdd:PRK15482 215 ITSLADSPLRRLAHFTLdtvsgETEWRSSSMSTRTAQNSVTDLLFVGLVQLNDVE 269
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 60-119 2.20e-04

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: 42.27  E-value: 2.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526089192  60 FVHATpKA----LG---KNSVVILASQQGNTAETVAAARVAREKGAATIGLVYQPDTPLCEYSDYII 119
Cdd:COG0794   75 FLHPA-EAshgdLGmitPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVL 140
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 20-101 6.53e-04

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 41.12  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  20 NIERVWFVGCGGSLTGfwpGKYFLDCEASKLAVGYITSNEFVhaTPKALGKNSVVILASQQGNTAETVAAARVAREKGAA 99
Cdd:PRK08674  33 KIDNIVISGMGGSGIG---GDLLRILLFDELKVPVFVNRDYT--LPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAK 107


                 ..
gi 526089192 100 TI 101
Cdd:PRK08674 108 II 109
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 73-111 7.32e-04

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 40.75  E-value: 7.32e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 526089192  73 VVILASQQGNTAETVAAARVAREKGAATIGLVyQPDTPL 111
Cdd:PRK11302 178 VVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPL 215
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 26-101 8.64e-04

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: 37.74  E-value: 8.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526089192  26 FVGCGGSLTgfwPGKYF--LDCEASKLAVGYITSNEFVHATPKALG-KNSVVILASQQGNTAETVAAARVAREKGAATI 101
Cdd:cd04795    3 VIGIGGSGA---IAAYFalELLELTGIEVVALIATELEHASLLSLLrKGDVVIALSYSGRTEELLAALEIAKELGIPVI 78
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
68-119 1.14e-03

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 40.13  E-value: 1.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 526089192  68 LGKNSVVILASQQGNTAETVAAARVAREKGAATIGLVYQPDTPLCEYSDYII 119
Cdd:PRK11337 185 LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 23-120 4.94e-03

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: 36.75  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526089192  23 RVWFVGCGGSltgfwpGKYfldceASKLA-----VG----YITSNEFVHATPKALGKNSVVILASQQGNTAETVAAARVA 93
Cdd:cd05014    2 KVVVTGVGKS------GHI-----ARKIAatlssTGtpafFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHL 70

                         90       100
                 ....*....|....*....|....*..
gi 526089192  94 REKGAATIGLVYQPDTPLCEYSDYIIE 120
Cdd:cd05014   71 KRRGAPIIAITGNPNSTLAKLSDVVLD 97
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 68-104 6.37e-03

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: 433326 [Multi-domain]  Cd Length: 138  Bit Score: 36.42  E-value: 6.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 526089192   68 LGKNSVVILASQQGNTAETVAAARVAREKGAATIGLV 104
Cdd:pfam13580 101 GRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALT 137
 
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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