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Conserved domains on  [gi|1054098436|ref|WP_066154431|]
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MULTISPECIES: 6-phospho-3-hexuloisomerase [Bacillaceae]

Protein Classification

6-phospho-3-hexuloisomerase( domain architecture ID 10799006)

6-phospho-3-hexuloisomerase (PHI) 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
RuMP_HxlB TIGR03127
6-phospho 3-hexuloisomerase; Members of this protein family are 6-phospho 3-hexuloisomerase ...
 7-185 5.17e-92

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: 265.71  E-value: 5.17e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   7 LAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGETVTANLEKDDLLIIGS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  87 GSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLPGSPKDQSESEYKTIQPMGSLFEQTMLLFYDALILRF 166
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 1054098436 167 MEKKGLDSTKMYGKHANLE 185
Cdd:TIGR03127 161 MKKKGLDEEEMKKRHANLE 179
 
Name Accession Description Interval E-value
RuMP_HxlB TIGR03127
6-phospho 3-hexuloisomerase; Members of this protein family are 6-phospho 3-hexuloisomerase ...
 7-185 5.17e-92

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: 265.71  E-value: 5.17e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   7 LAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGETVTANLEKDDLLIIGS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  87 GSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLPGSPKDQSESEYKTIQPMGSLFEQTMLLFYDALILRF 166
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 1054098436 167 MEKKGLDSTKMYGKHANLE 185
Cdd:TIGR03127 161 MKKKGLDEEEMKKRHANLE 179
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 4-182 3.69e-85

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: 248.64  E-value: 3.69e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   4 TQYLAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGETVTANLEKDDLLI 83
Cdd:cd05005     1 MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  84 IGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLPGSPKDQSESEYKTIQPMGSLFEQTMLLFYDALI 163
Cdd:cd05005    81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQPLGTLFEQSALVFLDAVI 160

                         170
                  ....*....|....*....
gi 1054098436 164 LRFMEKKGLDSTKMYGKHA 182
Cdd:cd05005   161 AKLMEELGVSEEEMKKRHA 179
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 5-171 5.38e-25

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 97.69  E-value: 5.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   5 QYLAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGE------TVTANLEK 78
Cdd:COG1737   103 KVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGdghlqaESAALLGP 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  79 DDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLPgspkdqSESEYKTIQPMGSLFEQTMLLf 158
Cdd:COG1737   183 GDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVP------SEEPTLRSSAFSSRVAQLALI- 255

                         170
                  ....*....|...
gi 1054098436 159 yDALILRFMEKKG 171
Cdd:COG1737   256 -DALAAAVAQRDG 267
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 32-153 1.15e-21

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: 85.43  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  32 KILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGETVT------ANLEKDDLLIIGSGSGETKTLVSIAEKAKSLG 105
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1054098436 106 GTVAAVTISPDSTIGKLADIIIKLPGSPKDQSESeYKTIQPMGSLFEQ 153
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPETGVAS-TKSITAQLAALDA 127
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
14-124 2.13e-10

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 58.17  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  14 LSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMG------IDAYVIGeTVTANLEKDDLLIIGSG 87
Cdd:PRK15482  113 LEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGyrvaceADTHVQA-TVSQALKKGDVQIAISY 191

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1054098436  88 SGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLAD 124
Cdd:PRK15482  192 SGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAH 228
 
Name Accession Description Interval E-value
RuMP_HxlB TIGR03127
6-phospho 3-hexuloisomerase; Members of this protein family are 6-phospho 3-hexuloisomerase ...
 7-185 5.17e-92

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: 265.71  E-value: 5.17e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   7 LAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGETVTANLEKDDLLIIGS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  87 GSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLPGSPKDQSESEYKTIQPMGSLFEQTMLLFYDALILRF 166
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 1054098436 167 MEKKGLDSTKMYGKHANLE 185
Cdd:TIGR03127 161 MKKKGLDEEEMKKRHANLE 179
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 4-182 3.69e-85

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: 248.64  E-value: 3.69e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   4 TQYLAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGETVTANLEKDDLLI 83
Cdd:cd05005     1 MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  84 IGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLPGSPKDQSESEYKTIQPMGSLFEQTMLLFYDALI 163
Cdd:cd05005    81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQPLGTLFEQSALVFLDAVI 160

                         170
                  ....*....|....*....
gi 1054098436 164 LRFMEKKGLDSTKMYGKHA 182
Cdd:cd05005   161 AKLMEELGVSEEEMKKRHA 179
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 5-171 5.38e-25

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 97.69  E-value: 5.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   5 QYLAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGE------TVTANLEK 78
Cdd:COG1737   103 KVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGdghlqaESAALLGP 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  79 DDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLPgspkdqSESEYKTIQPMGSLFEQTMLLf 158
Cdd:COG1737   183 GDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVP------SEEPTLRSSAFSSRVAQLALI- 255

                         170
                  ....*....|...
gi 1054098436 159 yDALILRFMEKKG 171
Cdd:COG1737   256 -DALAAAVAQRDG 267
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 32-153 1.15e-21

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: 85.43  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  32 KILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGETVT------ANLEKDDLLIIGSGSGETKTLVSIAEKAKSLG 105
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1054098436 106 GTVAAVTISPDSTIGKLADIIIKLPGSPKDQSESeYKTIQPMGSLFEQ 153
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPETGVAS-TKSITAQLAALDA 127
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 27-164 1.20e-20

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: 83.05  E-value: 1.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  27 EKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGET-----VTANLEKDDLLIIGSGSGETKTLVSIAEKA 101
Cdd:cd05013     4 EKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPhlqlmSAANLTPGDVVIAISFSGETKETVEAAEIA 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054098436 102 KSLGGTVAAVTISPDSTIGKLADIIIKLPgspkdqSESEYKTIQPMGSLFEQTMLLfyDALIL 164
Cdd:cd05013    84 KERGAKVIAITDSANSPLAKLADIVLLVS------SEEGDFRSSAFSSRIAQLALI--DALFL 138
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 38-133 4.66e-13

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: 62.95  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  38 KIFVAGAGRSGFMGKSFVMRMMHMGIDAYVI--GETVTANL---EKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVT 112
Cdd:cd05014     2 KVVVTGVGKSGHIARKIAATLSSTGTPAFFLhpTEALHGDLgmvTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAIT 81

                          90       100
                  ....*....|....*....|.
gi 1054098436 113 ISPDSTIGKLADIIIKLPGSP 133
Cdd:cd05014    82 GNPNSTLAKLSDVVLDLPVEE 102
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 5-137 1.62e-11

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: 61.45  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   5 QYLAEVVQELSRTVDLISDEeAEKLVNKILESK--KIFVAGAGRSGFMGKSFV-MRMMHMGIDAYVIG--ETVTANL--- 76
Cdd:COG2222     2 REIAQQPEAWRRALAALAAA-IAALLARLRAKPprRVVLVGAGSSDHAAQAAAyLLERLLGIPVAALApsELVVYPAylk 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054098436  77 EKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLPGSPkDQS 137
Cdd:COG2222    81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGP-EKS 140
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 39-113 4.47e-11

SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 56.61  E-value: 4.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  39 IFVAGAGRSGFMGKSFVMRMMHM-GIDAYVIGET------VTANLEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAV 111
Cdd:cd04795     1 IFVIGIGGSGAIAAYFALELLELtGIEVVALIATelehasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                  ..
gi 1054098436 112 TI 113
Cdd:cd04795    81 TD 82
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 12-130 2.12e-10

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: 58.45  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  12 QELSRTVDLIsDEEAEKLVNKILESK-KIFVAGAGRSGFMGKSFVMRMMHMGIDAYVI--GEtvtAN------LEKDDLL 82
Cdd:COG0794    20 EALAALAERL-DESFEKAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGTPAFFLhpAE---AShgdlgmITPGDVV 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1054098436  83 IIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLP 130
Cdd:COG0794    96 IAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLP 143
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
14-124 2.13e-10

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 58.17  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  14 LSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMG------IDAYVIGeTVTANLEKDDLLIIGSG 87
Cdd:PRK15482  113 LEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGyrvaceADTHVQA-TVSQALKKGDVQIAISY 191

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1054098436  88 SGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLAD 124
Cdd:PRK15482  192 SGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAH 228
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
7-117 3.67e-09

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 54.39  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   7 LAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGI------DAYVIGETVTAnLEKDD 80
Cdd:PRK11557   99 IKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGInavaerDMHALLATVQA-LSPDD 177

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1054098436  81 LLIIGSGSGETKTLVSIAEKAKSLGGTVAAVT-ISPDS 117
Cdd:PRK11557  178 LLLAISYSGERRELNLAADEALRVGAKVLAITgFTPNA 215
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 38-127 3.74e-09

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: 52.50  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  38 KIFVAGAGRSGFMGKSF-VMRMMHMGIDAYVIGETVTAN----LEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVT 112
Cdd:cd05008     1 RILIVGCGTSYHAALVAkYLLERLAGIPVEVEAASEFRYrrplLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                          90
                  ....*....|....*
gi 1054098436 113 ISPDSTIGKLADIII 127
Cdd:cd05008    81 NVVGSTLAREADYVL 95
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 5-130 3.08e-06

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: 45.19  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   5 QYLAEVVQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRS-------------GFMGKSFVMRMMHMGIDA------ 65
Cdd:cd05006     2 QESIQLKEALLELLAEAIEQAAQLLAEALLNGGKILICGNGGSaadaqhfaaelvkRFEKERPGLPAIALTTDTsiltai 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054098436  66 -------YVIGETVTANLEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLP 130
Cdd:cd05006    82 andygyeEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVP 153
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
3-133 6.05e-06

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 45.14  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   3 TTQYLAEV----VQELSRTVDLISDEEAEKLVNKILESKKIFVAGAGRSGFMGKSFVMRMMHMGIDAYVIGETVT----- 73
Cdd:PRK11337  103 PQDVVNKVfntsLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAHImlmsa 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054098436  74 ANLEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIII--KLPGSP 133
Cdd:PRK11337  183 ALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVIcsTAQGSP 244
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 76-127 2.00e-05

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 43.91  E-value: 2.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054098436  76 LEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIII 127
Cdd:PRK12570  125 LTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAI 176
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 63-141 2.96e-05

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: 41.79  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  63 IDAYVIGETVTAN---LEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIkLPGSPKDQSES 139
Cdd:cd05710    29 VFVYNAAEFLHTGpkrLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI-VYGFEIDAVEE 107


                  ..
gi 1054098436 140 EY 141
Cdd:cd05710   108 KY 109
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 74-130 1.77e-04

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: 40.97  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054098436  74 ANLEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLP 130
Cdd:cd05007   114 INLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALI 170
PRK10892 PRK10892
arabinose-5-phosphate isomerase KdsD;
38-130 4.27e-04

arabinose-5-phosphate isomerase KdsD;


Pssm-ID: 182814 [Multi-domain]  Cd Length: 326  Bit Score: 39.71  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  38 KIFVAGAGRSGFMGKSFVMRMMHMGIDAYVI--GETVTANL---EKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVT 112
Cdd:PRK10892   49 KVVVMGMGKSGHIGRKMAATFASTGTPSFFVhpGEAAHGDLgmvTPQDVVIAISNSGESSEILALIPVLKRLHVPLICIT 128

                          90       100
                  ....*....|....*....|
gi 1054098436 113 ISPDSTIGKLADI--IIKLP 130
Cdd:PRK10892  129 GRPESSMARAADIhlCVKVP 148
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 76-127 1.59e-03

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 38.46  E-value: 1.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054098436  76 LEKDDLLIIGSGSGET-KTLVSIaEKAKSLGGTVAAVTISPDSTIGKLADIII 127
Cdd:COG0449   339 VDPGTLVIAISQSGETaDTLAAL-REAKEKGAKVLAICNVVGSTIARESDAVL 390
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 24-131 2.04e-03

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 38.04  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  24 EEAEKLVNKILESKKIFVAGAGRSGFMG---KSFVMRMMHmgIDAYVI-GETVTANLEKDDLLIIGSGSGETKTLVSIAE 99
Cdd:PRK08674   22 AISLDLEEDLEKIDNIVISGMGGSGIGGdllRILLFDELK--VPVFVNrDYTLPAFVDEKTLVIAVSYSGNTEETLSAVE 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1054098436 100 KAKSLGGTVAAVTispdsTIGKLADI-------IIKLPG 131
Cdd:PRK08674  100 QALKRGAKIIAIT-----SGGKLKEMakehglpVIIVPG 133
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
5-171 4.71e-03

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 36.67  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436   5 QYLAEVVQELSRTVDLIsDEEAEKLVNKILESK-KIFVAGAGRSGFMGKSFVMRMMHMGIDAYVI--GETVTANL---EK 78
Cdd:PRK11543   11 QTLMLELQEASRLPERL-GDDFVRAANIILHCEgKVVVSGIGKSGHIGKKIAATLASTGTPAFFVhpAEALHGDLgmiES 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  79 DDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLpgspKDQSESEYKTIQPMGSLFEQTMLlf 158
Cdd:PRK11543   90 RDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDI----SVEREACPMHLAPTSSTVNTLMM-- 163

                         170
                  ....*....|...
gi 1054098436 159 YDALILRFMEKKG 171
Cdd:PRK11543  164 GDALAMAVMQARG 176
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 74-130 4.90e-03

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 36.68  E-value: 4.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054098436  74 ANLEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTISPDSTIGKLADIIIKLP 130
Cdd:PRK05441  127 INLTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVV 183
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 38-131 8.61e-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: 34.55  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054098436  38 KIFVAGAGRSGFMGkSFVMRMM--HMGIDAYVI-GETVTANLEKDDLLIIGSGSGETKTLVSIAEKAKSLGGTVAAVTis 114
Cdd:cd05017     1 NIVILGMGGSGIGG-DLLESLLldEAKIPVYVVkDYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT-- 77

                          90       100
                  ....*....|....*....|....
gi 1054098436 115 pdsTIGKLADI-------IIKLPG 131
Cdd:cd05017    78 ---SGGKLLEMarehgvpVIIIPK 98
 
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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