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Conserved domains on  [gi|2044733648|ref|WP_213420222|]
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MULTISPECIES: 6-phospho-3-hexuloisomerase [Bacillus]

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 3.44e-99

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: 284.20  E-value: 3.44e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   7 VAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEILTPPLGEGDLVIIGS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  87 GSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMPGSPKDQSNGNYKTIQPMGSLFEQTLLLFYDAVILKL 166
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 2044733648 167 MEKKGLDSETMFTHHANLE 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 3.44e-99

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: 284.20  E-value: 3.44e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   7 VAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEILTPPLGEGDLVIIGS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  87 GSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMPGSPKDQSNGNYKTIQPMGSLFEQTLLLFYDAVILKL 166
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 2044733648 167 MEKKGLDSETMFTHHANLE 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 1.89e-90

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: 261.74  E-value: 1.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   4 TEYVAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEILTPPLGEGDLVI 83
Cdd:cd05005     1 MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  84 IGSGSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMPGSPKDQSNGNYKTIQPMGSLFEQTLLLFYDAVI 163
Cdd:cd05005    81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQPLGTLFEQSALVFLDAVI 160

                         170
                  ....*....|....*....
gi 2044733648 164 LKLMEKKGLDSETMFTHHA 182
Cdd:cd05005   161 AKLMEELGVSEEEMKKRHA 179
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 32-157 1.11e-24

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: 93.13  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  32 HILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEILT------PPLGEGDLVIIGSGSGETKSLIDTAAKAKSLH 105
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2044733648 106 GIVAALTINPESSIGKQADLIIRMPGSPKDqSNGNYKTIQPMGSLFEQTLLL 157
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPET-GVASTKSITAQLAALDALAVA 131
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 5-171 3.06e-18

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 79.97  E-value: 3.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   5 EYVAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGE------ILTPPLGE 78
Cdd:COG1737   103 KVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGdghlqaESAALLGP 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  79 GDLVIIGSGSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMPgspkdqSNGNYKTIQPMGSLFEQTLLLf 158
Cdd:COG1737   183 GDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVP------SEEPTLRSSAFSSRVAQLALI- 255

                         170
                  ....*....|...
gi 2044733648 159 yDAVILKLMEKKG 171
Cdd:COG1737   256 -DALAAAVAQRDG 267
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
7-112 7.36e-05

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 42.06  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   7 VAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEI-----LTPPLGEGDL 81
Cdd:PRK11557   99 IKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAERDMhallaTVQALSPDDL 178

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2044733648  82 VIIGSGSGETKSLIDTAAKAKSLHGIVAALT 112
Cdd:PRK11557  179 LLAISYSGERRELNLAADEALRVGAKVLAIT 209
 
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 3.44e-99

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: 284.20  E-value: 3.44e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   7 VAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEILTPPLGEGDLVIIGS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  87 GSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMPGSPKDQSNGNYKTIQPMGSLFEQTLLLFYDAVILKL 166
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGNYKSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 2044733648 167 MEKKGLDSETMFTHHANLE 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 1.89e-90

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: 261.74  E-value: 1.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   4 TEYVAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEILTPPLGEGDLVI 83
Cdd:cd05005     1 MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  84 IGSGSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMPGSPKDQSNGNYKTIQPMGSLFEQTLLLFYDAVI 163
Cdd:cd05005    81 AISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQPLGTLFEQSALVFLDAVI 160

                         170
                  ....*....|....*....
gi 2044733648 164 LKLMEKKGLDSETMFTHHA 182
Cdd:cd05005   161 AKLMEELGVSEEEMKKRHA 179
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 32-157 1.11e-24

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: 93.13  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  32 HILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEILT------PPLGEGDLVIIGSGSGETKSLIDTAAKAKSLH 105
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2044733648 106 GIVAALTINPESSIGKQADLIIRMPGSPKDqSNGNYKTIQPMGSLFEQTLLL 157
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPET-GVASTKSITAQLAALDALAVA 131
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 5-171 3.06e-18

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 79.97  E-value: 3.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   5 EYVAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGE------ILTPPLGE 78
Cdd:COG1737   103 KVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGdghlqaESAALLGP 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  79 GDLVIIGSGSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMPgspkdqSNGNYKTIQPMGSLFEQTLLLf 158
Cdd:COG1737   183 GDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVP------SEEPTLRSSAFSSRVAQLALI- 255

                         170
                  ....*....|...
gi 2044733648 159 yDAVILKLMEKKG 171
Cdd:COG1737   256 -DALAAAVAQRDG 267
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 27-141 1.08e-15

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: 69.95  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  27 DQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVG-----EILTPPLGEGDLVIIGSGSGETKSLIDTAAKA 101
Cdd:cd05013     4 EKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSdphlqLMSAANLTPGDVVIAISFSGETKETVEAAEIA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2044733648 102 KSLHGIVAALTINPESSIGKQADLIIRMPGSPKDQSNGNY 141
Cdd:cd05013    84 KERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAF 123
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 39-113 1.66e-12

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: 60.08  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  39 IFTAGAGRSGLMAKSFAMRLMHM-GFNAHIVGEILTPP------LGEGDLVIIGSGSGETKSLIDTAAKAKSLHGIVAAL 111
Cdd:cd04795     1 IFVIGIGGSGAIAAYFALELLELtGIEVVALIATELEHasllslLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                  ..
gi 2044733648 112 TI 113
Cdd:cd04795    81 TD 82
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 8-137 5.80e-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: 54.13  E-value: 5.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   8 AEILN--ELHRSAAYISNEEADQLADHILSSH--QIFTAGAGRSGLMAKSFAMRLM-HMGFNAHIVG--EILT---PPLG 77
Cdd:COG2222     2 REIAQqpEAWRRALAALAAAIAALLARLRAKPprRVVLVGAGSSDHAAQAAAYLLErLLGIPVAALApsELVVypaYLKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  78 EGDLVIIGSGSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMPGSPkDQS 137
Cdd:COG2222    82 EGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGP-EKS 140
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 39-133 7.36e-09

KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.


Pssm-ID: 240145 [Multi-domain]  Cd Length: 128  Bit Score: 51.77  E-value: 7.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  39 IFTAGAGRSGLMAKSFAMRLMHMGFNAHIV--GEILTPPLG---EGDLVIIGSGSGETKSLIDTAAKAKSLHGIVAALTI 113
Cdd:cd05014     3 VVVTGVGKSGHIARKIAATLSSTGTPAFFLhpTEALHGDLGmvtPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITG 82

                          90       100
                  ....*....|....*....|
gi 2044733648 114 NPESSIGKQADLIIRMPGSP 133
Cdd:cd05014    83 NPNSTLAKLSDVVLDLPVEE 102
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 39-127 5.51e-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: 49.03  E-value: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  39 IFTAGAGRS---GLMAKSFAMRLMHMGFNAHIVGEIL--TPPLGEGDLVIIGSGSGETKSLIDTAAKAKSLHGIVAALTI 113
Cdd:cd05008     2 ILIVGCGTSyhaALVAKYLLERLAGIPVEVEAASEFRyrRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITN 81

                          90
                  ....*....|....
gi 2044733648 114 NPESSIGKQADLII 127
Cdd:cd05008    82 VVGSTLAREADYVL 95
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 12-130 9.20e-07

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: 47.66  E-value: 9.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  12 NELHRSAAYIsNEEADQLADHILSSH-QIFTAGAGRSGLMAKSFAMRLMHMGFNAHIV--GEILTPPLG---EGDLVIIG 85
Cdd:COG0794    20 EALAALAERL-DESFEKAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGTPAFFLhpAEASHGDLGmitPGDVVIAI 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2044733648  86 SGSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMP 130
Cdd:COG0794    99 SNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLP 143
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 74-141 6.08e-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: 40.64  E-value: 6.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044733648  74 PPLGEGDLVIIGSGSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLIIRMpGSPKDQSNGNY 141
Cdd:cd05710    43 KRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIVY-GFEIDAVEEKY 109
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
7-112 7.36e-05

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 42.06  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   7 VAEILNELHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGFNAHIVGEI-----LTPPLGEGDL 81
Cdd:PRK11557   99 IKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAERDMhallaTVQALSPDDL 178

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2044733648  82 VIIGSGSGETKSLIDTAAKAKSLHGIVAALT 112
Cdd:PRK11557  179 LLAISYSGERRELNLAADEALRVGAKVLAIT 209
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 74-127 1.51e-04

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: 41.54  E-value: 1.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2044733648  74 PPLGEGDLVIIGSGSGETkslIDT-AA--KAKSLHGIVAALTINPESSIGKQADLII 127
Cdd:COG0449   337 PVVDPGTLVIAISQSGET---ADTlAAlrEAKEKGAKVLAICNVVGSTIARESDAVL 390
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 78-135 5.46e-04

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 39.59  E-value: 5.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2044733648  78 EGDLVIIGSGSGETKSLIDTAAKAKSLHGIVAALTiNPESSIGKQADLIIRMPgSPKD 135
Cdd:PRK11302  175 DGDVVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPLAREATLALTLD-VPED 230
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
5-127 5.89e-04

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 39.30  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648   5 EYVAEILNE-----LHRSAAYISNEEADQLADHILSSHQIFTAGAGRSGLMAKSFAMRLMHMGF------NAHIVGEIlT 73
Cdd:PRK15482   99 EVIARKLNRekelaLEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGYrvaceaDTHVQATV-S 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2044733648  74 PPLGEGDLVIIGSGSGETKSLIDTAAKAKSLHGIVAALTINPESSIGKQADLII 127
Cdd:PRK15482  178 QALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTL 231
PRK10892 PRK10892
arabinose-5-phosphate isomerase KdsD;
20-130 6.26e-04

arabinose-5-phosphate isomerase KdsD;


Pssm-ID: 182814 [Multi-domain]  Cd Length: 326  Bit Score: 39.32  E-value: 6.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044733648  20 YIsNEEADQLADHILSSH-QIFTAGAGRSGLMAKSFAMRLMHMGFNAHIV--GEILTPPLG---EGDLVIIGSGSGETKS 93
Cdd:PRK10892   31 YI-NQDFTLACEKMFWCKgKVVVMGMGKSGHIGRKMAATFASTGTPSFFVhpGEAAHGDLGmvtPQDVVIAISNSGESSE 109

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2044733648  94 LIDTAAKAKSLHGIVAALTINPESSIGKQAD--LIIRMP 130
Cdd:PRK10892  110 ILALIPVLKRLHVPLICITGRPESSMARAADihLCVKVP 148
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
74-127 7.81e-04

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 39.26  E-value: 7.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2044733648  74 PPLGEGDLVIIGSGSGETkslIDT-AA--KAKSLHGIVAALTINPESSIGKQADLII 127
Cdd:PRK00331  332 PVLSPKTLVIAISQSGET---ADTlAAlrLAKELGAKTLAICNVPGSTIARESDAVL 385
 
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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