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Conserved domains on  [gi|91202354|emb|CAJ75414|]
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conserved hypothetical sugar phosphate isomerase protein [Candidatus Kuenenia stuttgartiensis]

Protein Classification

SIS domain-containing protein( domain architecture ID 10141873)

SIS (sugar isomerase) domain-containing protein similar to Mycobacterium gastri 6-phospho-3-hexuloisomerase (PHI, EC 5.3.1.27) that catalyzes the isomerization between 3-hexulose 6-phosphate and fructose 6-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 19-197 9.60e-86

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: 250.57  E-value: 9.60e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  19 KPTTKIILNEIHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATTPNIDKGDLLI 98
Cdd:cd05005   1 MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  99 ACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQEIRTHNKINGSIQFRSTLFEQACLVYLDGVI 178
Cdd:cd05005  81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQPLGTLFEQSALVFLDAVI 160

                       170
                ....*....|....*....
gi 91202354 179 HLLVTELRSSEQEMNRRHS 197
Cdd:cd05005 161 AKLMEELGVSEEEMKKRHA 179
 
Name Accession Description Interval E-value
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 19-197 9.60e-86

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: 250.57  E-value: 9.60e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  19 KPTTKIILNEIHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATTPNIDKGDLLI 98
Cdd:cd05005   1 MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  99 ACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQEIRTHNKINGSIQFRSTLFEQACLVYLDGVI 178
Cdd:cd05005  81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQPLGTLFEQSALVFLDAVI 160

                       170
                ....*....|....*....
gi 91202354 179 HLLVTELRSSEQEMNRRHS 197
Cdd:cd05005 161 AKLMEELGVSEEEMKKRHA 179
RuMP_HxlB TIGR03127
6-phospho 3-hexuloisomerase; Members of this protein family are 6-phospho 3-hexuloisomerase ...
 23-200 4.30e-62

6-phospho 3-hexuloisomerase; Members of this protein family are 6-phospho 3-hexuloisomerase (PHI), or the PHI domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin.


Pssm-ID: 132171 [Multi-domain]  Cd Length: 179  Bit Score: 190.60  E-value: 4.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354    23 KIILNEIHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATTPNIDKGDLLIACSS 102
Cdd:TIGR03127   2 KLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAISG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   103 SGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQEIRTHNKINGSIQFRSTLFEQACLVYLDGVIHLLV 182
Cdd:TIGR03127  82 SGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQPLGSLFEQSLLLFLDAVILKLM 161

                         170
                  ....*....|....*...
gi 91202354   183 TELRSSEQEMNRRHSNLE 200
Cdd:TIGR03127 162 KKKGLDEEEMKKRHANLE 179
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 29-150 1.01e-23

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 94.99  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  29 IHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCV-GDATTP-----NIDKGDLLIACSS 102
Cdd:COG1737 112 LEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLdGDGHLQaesaaLLGPGDVVIAISF 191

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 91202354 103 SGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQEIR 150
Cdd:COG1737 192 SGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPT 239
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 47-149 3.02e-17

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 74.26  E-value: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354    47 SILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATT------PNIDKGDLLIACSSSGNTHITCYIAELAKKSF 120
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100
                  ....*....|....*....|....*....
gi 91202354   121 ATVAAITSQKNSPLTEYADIIVDLPVQEI 149
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPE 109
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
26-164 1.14e-12

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 65.10  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   26 LNEIHSVLDKINEQSFAQLFSSildAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGD----ATTPN-IDKGDLLIAC 100
Cdd:PRK15482 113 LEQTCALFDYARLQKIIEVISK---APFIQITGLGGSALVGRDLSFKLMKIGYRVACEADthvqATVSQaLKKGDVQIAI 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91202354  101 SSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDlpvqeirthnKINGSIQFRST 164
Cdd:PRK15482 190 SYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLD----------TVSGETEWRSS 243
 
Name Accession Description Interval E-value
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 19-197 9.60e-86

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: 250.57  E-value: 9.60e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  19 KPTTKIILNEIHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATTPNIDKGDLLI 98
Cdd:cd05005   1 MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  99 ACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQEIRTHNKINGSIQFRSTLFEQACLVYLDGVI 178
Cdd:cd05005  81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQPLGTLFEQSALVFLDAVI 160

                       170
                ....*....|....*....
gi 91202354 179 HLLVTELRSSEQEMNRRHS 197
Cdd:cd05005 161 AKLMEELGVSEEEMKKRHA 179
RuMP_HxlB TIGR03127
6-phospho 3-hexuloisomerase; Members of this protein family are 6-phospho 3-hexuloisomerase ...
 23-200 4.30e-62

6-phospho 3-hexuloisomerase; Members of this protein family are 6-phospho 3-hexuloisomerase (PHI), or the PHI domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin.


Pssm-ID: 132171 [Multi-domain]  Cd Length: 179  Bit Score: 190.60  E-value: 4.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354    23 KIILNEIHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATTPNIDKGDLLIACSS 102
Cdd:TIGR03127   2 KLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAISG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   103 SGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQEIRTHNKINGSIQFRSTLFEQACLVYLDGVIHLLV 182
Cdd:TIGR03127  82 SGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQPLGSLFEQSLLLFLDAVILKLM 161

                         170
                  ....*....|....*...
gi 91202354   183 TELRSSEQEMNRRHSNLE 200
Cdd:TIGR03127 162 KKKGLDEEEMKKRHANLE 179
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 29-150 1.01e-23

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 94.99  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  29 IHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCV-GDATTP-----NIDKGDLLIACSS 102
Cdd:COG1737 112 LEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLdGDGHLQaesaaLLGPGDVVIAISF 191

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 91202354 103 SGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQEIR 150
Cdd:COG1737 192 SGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPT 239
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 39-149 1.70e-22

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: 88.05  E-value: 1.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  39 QSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATTP-----NIDKGDLLIACSSSGNTHITCYIA 113
Cdd:cd05013   1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQlmsaaNLTPGDVVIAISFSGETKETVEAA 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 91202354 114 ELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQEI 149
Cdd:cd05013  81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEG 116
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 47-149 3.02e-17

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 74.26  E-value: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354    47 SILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATT------PNIDKGDLLIACSSSGNTHITCYIAELAKKSF 120
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100
                  ....*....|....*....|....*....
gi 91202354   121 ATVAAITSQKNSPLTEYADIIVDLPVQEI 149
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPE 109
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
26-164 1.14e-12

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 65.10  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   26 LNEIHSVLDKINEQSFAQLFSSildAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGD----ATTPN-IDKGDLLIAC 100
Cdd:PRK15482 113 LEQTCALFDYARLQKIIEVISK---APFIQITGLGGSALVGRDLSFKLMKIGYRVACEADthvqATVSQaLKKGDVQIAI 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91202354  101 SSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDlpvqeirthnKINGSIQFRST 164
Cdd:PRK15482 190 SYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLD----------TVSGETEWRSS 243
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
29-139 2.62e-12

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 64.02  E-value: 2.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   29 IHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGD-----ATTPNIDKGDLLIACSSS 103
Cdd:PRK11557 106 MRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAERDmhallATVQALSPDDLLLAISYS 185

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 91202354  104 GNTHITCYIAELAKKSFATVAAITSQKNSPLTEYAD 139
Cdd:PRK11557 186 GERRELNLAADEALRVGAKVLAITGFTPNALQQRAS 221
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 54-148 2.83e-12

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: 61.02  E-value: 2.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  54 IFVTGQGRSGLVSRTFAMRLTHIGLNAYCV-------GDATTpnIDKGDLLIACSSSGNTHITCYIAELAKKSFATVAAI 126
Cdd:cd05014   3 VVVTGVGKSGHIARKIAATLSSTGTPAFFLhptealhGDLGM--VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80

                        90       100
                ....*....|....*....|..
gi 91202354 127 TSQKNSPLTEYADIIVDLPVQE 148
Cdd:cd05014  81 TGNPNSTLAKLSDVVLDLPVEE 102
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 27-148 4.30e-12

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: 63.46  E-value: 4.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  27 NEIHSVLDKINEqSFAQLFSSILDAKN-IFVTGQGRSGLVSRTFAMRLTHIGLNAYCV-------GDATTpnIDKGDLLI 98
Cdd:COG0794  20 EALAALAERLDE-SFEKAVELILNCKGrVVVTGMGKSGHIARKIAATLASTGTPAFFLhpaeashGDLGM--ITPGDVVI 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 91202354  99 ACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQE 148
Cdd:COG0794  97 AISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVER 146
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 26-145 5.50e-09

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: 54.52  E-value: 5.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  26 LNEIHSV------LDKINEQSFAQLFSSILDAKN--IFVTGQGRSGLVSRTFAMRL-THIGLNAYCVG--DATT---PNI 91
Cdd:COG2222   1 AREIAQQpeawrrALAALAAAIAALLARLRAKPPrrVVLVGAGSSDHAAQAAAYLLeRLLGIPVAALApsELVVypaYLK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 91202354  92 DKGDLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLP 145
Cdd:COG2222  81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLP 134
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
23-150 1.17e-08

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 54.15  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   23 KIILNEIHSVL---DKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGD-----ATTPNIDKG 94
Cdd:PRK14101 437 KVLDNTVSAILqlrEHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDlymqaASAALLGKG 516

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 91202354   95 DLLIACSSSGNTHITCYIAELAKKSFATVAAITSQkNSPLTEYADIIVDLPVQEIR 150
Cdd:PRK14101 517 DVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSS-NTPLAKRATVALETDHIEMR 571
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 53-128 1.29e-08

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: 51.11  E-value: 1.29e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91202354  53 NIFVTGQGRSGLVSRTF-AMRLTHIGLNAYCVGDATTPN-IDKGDLLIACSSSGNTHITCYIAELAKKSFATVAAITS 128
Cdd:cd05017   1 NIVILGMGGSGIGGDLLeSLLLDEAKIPVYVVKDYTLPAfVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAITS 78
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 47-128 1.87e-08

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 53.06  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   47 SILDAKNIFVTGQGRSGLVS---RTFAMRLTHIGLnaYCVGDATTPN-IDKGDLLIACSSSGNTHITCYIAELAKKSFAT 122
Cdd:PRK08674  30 DLEKIDNIVISGMGGSGIGGdllRILLFDELKVPV--FVNRDYTLPAfVDEKTLVIAVSYSGNTEETLSAVEQALKRGAK 107


                 ....*.
gi 91202354  123 VAAITS 128
Cdd:PRK08674 108 IIAITS 113
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 53-145 4.21e-08

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: 49.80  E-value: 4.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  53 NIFVTGQGRS---GLVSRTFAMRLTHIGLNAYcvgDAT-----TPNIDKGDLLIACSSSGNTHITCYIAELAKKSFATVA 124
Cdd:cd05008   1 RILIVGCGTSyhaALVAKYLLERLAGIPVEVE---AASefryrRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTV 77

                        90       100
                ....*....|....*....|.
gi 91202354 125 AITSQKNSPLTEYADIIVDLP 145
Cdd:cd05008  78 AITNVVGSTLAREADYVLYLR 98
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
12-148 8.70e-07

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 48.22  E-value: 8.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   12 NTTTLVIKPTTKIILNEIHSVLDKINEQSFAQLFSSILDAKNIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDA----- 86
Cdd:PRK11337 101 DAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAhimlm 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91202354   87 TTPNIDKGDLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQE 148
Cdd:PRK11337 181 SAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQG 242
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 86-142 1.78e-06

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: 45.26  E-value: 1.78e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 91202354  86 ATTPNIDKGDLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIV 142
Cdd:cd05710  40 TGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI 96
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 90-146 2.05e-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: 46.75  E-value: 2.05e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 91202354  90 NIDKGDLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPV 146
Cdd:cd05007 115 NLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALIT 171
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 54-127 3.76e-06

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: 43.52  E-value: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354  54 IFVTGQGRSGLVSRTFAMRLTHI-GLNAYCVGDATTP------NIDKGDLLIACSSSGNTHITCYIAELAKKSFATVAAI 126
Cdd:cd04795   1 IFVIGIGGSGAIAAYFALELLELtGIEVVALIATELEhasllsLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                .
gi 91202354 127 T 127
Cdd:cd04795  81 T 81
G6PI_arch TIGR02128
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ...
 52-128 8.77e-06

bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member of the larger PGI superfamily and only distantly related to other glucose-6-phosphate isomerases. The family is limited to the archaea.


Pssm-ID: 273988 [Multi-domain]  Cd Length: 308  Bit Score: 45.12  E-value: 8.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354    52 KNIFVTGQGRSGLVSRTFAMRLTHIGLNA--YCVGDATTPNIDKGD-LLIACSSSGNTHITCYIAELAKKSFATVAAITS 128
Cdd:TIGR02128  22 DEIVICGMGGSGIAGRIISILLLEKSFQGpvFVVKDYRLPRFVDGKtLLIAVSYSGNTEETLSAVEEAKKKGAKVIAITS 101
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 90-148 2.06e-05

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 43.83  E-value: 2.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 91202354   90 NIDKGDLLIACSSSGNTHITCYIAELAKKSFATVAAITSqKNSPLTEYADIIVDLPVQE 148
Cdd:PRK11302 172 NSSDGDVVVLISHTGRTKSLVELAQLARENGATVIAITS-AGSPLAREATLALTLDVPE 229
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
19-147 2.57e-05

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 43.60  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91202354   19 KPTTKIILNEIHSVLDKINEqSFAQLFSSILDAK-NIFVTGQGRSGLVSRTFAMRLTHIGLNAYCVGDATTPNIDKG--- 94
Cdd:PRK11543  10 RQTLMLELQEASRLPERLGD-DFVRAANIILHCEgKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGmie 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 91202354   95 --DLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQ 147
Cdd:PRK11543  89 srDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVE 143
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 90-146 3.69e-05

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 43.23  E-value: 3.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 91202354   90 NIDKGDLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPV 146
Cdd:PRK05441 128 NLTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVV 184
PRK13938 PRK13938
phosphoheptose isomerase; Provisional
 94-148 2.09e-04

phosphoheptose isomerase; Provisional


Pssm-ID: 139997 [Multi-domain]  Cd Length: 196  Bit Score: 40.49  E-value: 2.09e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 91202354   94 GDLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLPVQE 148
Cdd:PRK13938 114 GDTLFAISTSGNSMSVLRAAKTARELGVTVVAMTGESGGQLAEFADFLINVPSRD 168
GmhA COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
93-149 1.07e-03

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 38.17  E-value: 1.07e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91202354  93 KGDLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLP------VQEI 149
Cdd:COG0279 109 PGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGLADIEIRVPsdstarIQEV 171
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 93-149 2.43e-03

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: 37.10  E-value: 2.43e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91202354  93 KGDLLIACSSSGNTHITCYIAELAKKSFATVAAITSQKNSPLTEYADIIVDLP------VQEI 149
Cdd:cd05006 101 PGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPsddtprIQEV 163
 
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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