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Conserved domains on  [gi|488403226|ref|WP_002472611|]
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6-phospho-3-hexuloisomerase [Staphylococcus pettenkoferi]

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 ...
 7-182 1.94e-87

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: 254.15  E-value: 1.94e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226    7 YRLVLDELDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGESTTPSIHEGDLFIVIS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226   87 GSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGTKHDAEG---SAQPLGSLFEQASQILLDSLVLDL 163
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGnykSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 488403226  164 MKELDVSEETMQQNHANLE 182
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 ...
 7-182 1.94e-87

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: 254.15  E-value: 1.94e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226    7 YRLVLDELDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGESTTPSIHEGDLFIVIS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226   87 GSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGTKHDAEG---SAQPLGSLFEQASQILLDSLVLDL 163
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGnykSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 488403226  164 MKELDVSEETMQQNHANLE 182
Cdd:TIGR03127 161 MKKKGLDEEEMKKRHANLE 179
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 6-179 7.16e-82

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: 240.17  E-value: 7.16e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226   6 NYRLVLDELDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGESTTPSIHEGDLFIVI 85
Cdd:cd05005    3 YLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLIAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  86 SGSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGTKHDAEG---SAQPLGSLFEQASQILLDSLVLD 162
Cdd:cd05005   83 SGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGehkSIQPLGTLFEQSALVFLDAVIAK 162

                        170
                 ....*....|....*..
gi 488403226 163 LMKELDVSEETMQQNHA 179
Cdd:cd05005  163 LMEELGVSEEEMKKRHA 179
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 14-182 1.52e-23

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 93.84  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  14 LDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGES------TTPSIHEGDLFIVISG 87
Cdd:COG1737  112 LEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGDghlqaeSAALLGPGDVVIAISF 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  88 SGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGTKHDAEGSAQPLGSLFeqasqILLDSLVLDLMKEL 167
Cdd:COG1737  192 SGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSSAFSSRVAQL-----ALIDALAAAVAQRD 266

                        170
                 ....*....|....*.
gi 488403226 168 -DVSEETMQQNHANLE 182
Cdd:COG1737  267 gDKARERLERTEALLS 282
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 35-135 2.08e-16

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: 71.56  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226   35 NAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGESTT------PSIHEGDLFIVISGSGSTEHLRLLADKAKSVGAQV 108
Cdd:pfam01380   4 KAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARGAKI 83

                          90       100
                  ....*....|....*....|....*..
gi 488403226  109 VLLSTKPESPIGELANTVIELPAGTKH 135
Cdd:pfam01380  84 IAITDSPGSPLAREADHVLYINAGPET 110
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
14-181 4.86e-08

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 51.24  E-value: 4.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  14 LDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLG------KNAHVIGeSTTPSIHEGDLFIVISG 87
Cdd:PRK15482 113 LEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGyrvaceADTHVQA-TVSQALKKGDVQIAISY 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  88 SGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGtkhDAEGSAQPLGSLFEQASqiLLDSLVLDLMKEL 167
Cdd:PRK15482 192 SGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSG---ETEWRSSSMSTRTAQNS--VTDLLFVGLVQLN 266

                        170
                 ....*....|....
gi 488403226 168 DVSEETMQQNHANL 181
Cdd:PRK15482 267 DVESLKMIQRSSEL 280
 
Name Accession Description Interval E-value
RuMP_HxlB TIGR03127
6-phospho 3-hexuloisomerase; Members of this protein family are 6-phospho 3-hexuloisomerase ...
 7-182 1.94e-87

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: 254.15  E-value: 1.94e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226    7 YRLVLDELDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGESTTPSIHEGDLFIVIS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226   87 GSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGTKHDAEG---SAQPLGSLFEQASQILLDSLVLDL 163
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGnykSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 488403226  164 MKELDVSEETMQQNHANLE 182
Cdd:TIGR03127 161 MKKKGLDEEEMKKRHANLE 179
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 6-179 7.16e-82

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: 240.17  E-value: 7.16e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226   6 NYRLVLDELDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGESTTPSIHEGDLFIVI 85
Cdd:cd05005    3 YLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLIAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  86 SGSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGTKHDAEG---SAQPLGSLFEQASQILLDSLVLD 162
Cdd:cd05005   83 SGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGehkSIQPLGTLFEQSALVFLDAVIAK 162

                        170
                 ....*....|....*..
gi 488403226 163 LMKELDVSEETMQQNHA 179
Cdd:cd05005  163 LMEELGVSEEEMKKRHA 179
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 14-182 1.52e-23

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 93.84  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  14 LDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGES------TTPSIHEGDLFIVISG 87
Cdd:COG1737  112 LEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGDghlqaeSAALLGPGDVVIAISF 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  88 SGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGTKHDAEGSAQPLGSLFeqasqILLDSLVLDLMKEL 167
Cdd:COG1737  192 SGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSSAFSSRVAQL-----ALIDALAAAVAQRD 266

                        170
                 ....*....|....*.
gi 488403226 168 -DVSEETMQQNHANLE 182
Cdd:COG1737  267 gDKARERLERTEALLS 282
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 24-161 2.36e-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: 81.89  E-value: 2.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  24 EQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGESTTP-----SIHEGDLFIVISGSGSTEHLRLLA 98
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQlmsaaNLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488403226  99 DKAKSVGAQVVLLSTKPESPIGELANTVIELPAGTKHDAEGSAQPLGSLFeqasqILLDSLVL 161
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQL-----ALIDALFL 138
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 35-135 2.08e-16

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: 71.56  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226   35 NAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGESTT------PSIHEGDLFIVISGSGSTEHLRLLADKAKSVGAQV 108
Cdd:pfam01380   4 KAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARGAKI 83

                          90       100
                  ....*....|....*....|....*..
gi 488403226  109 VLLSTKPESPIGELANTVIELPAGTKH 135
Cdd:pfam01380  84 IAITDSPGSPLAREADHVLYINAGPET 110
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 18-132 8.55e-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: 59.53  E-value: 8.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  18 LAHVEAEQAQAFVQEVLNA--EHVFVAGKGRSGFVANSFAMRLN-QLGKNAHVIGESTTPS-----IHEGDLFIVISGSG 89
Cdd:COG2222   14 ALAALAAAIAALLARLRAKppRRVVLVGAGSSDHAAQAAAYLLErLLGIPVAALAPSELVVypaylKLEGTLVVAISRSG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488403226  90 STEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAG 132
Cdd:COG2222   94 NSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAG 136
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 39-130 7.81e-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: 51.39  E-value: 7.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  39 VFVAGKGRSGFVANSFAMRLNQLGKNAHVIgeSTTPSIH-------EGDLFIVISGSGSTEHLRLLADKAKSVGAQVVLL 111
Cdd:cd05014    3 VVVTGVGKSGHIARKIAATLSSTGTPAFFL--HPTEALHgdlgmvtPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80

                         90
                 ....*....|....*....
gi 488403226 112 STKPESPIGELANTVIELP 130
Cdd:cd05014   81 TGNPNSTLAKLSDVVLDLP 99
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 38-132 1.63e-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: 50.57  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  38 HVFVAGKGRSGFVANSFAMRLNQLGK-NAHVIGESTT----PSIHEGDLFIVISGSG-STEHLRLLaDKAKSVGAQVVLL 111
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGiPVEVEAASEFryrrPLLDEDTLVIAISQSGeTADTLAAL-RLAKEKGAKTVAI 79

                         90       100
                 ....*....|....*....|.
gi 488403226 112 STKPESPIGELANTVIELPAG 132
Cdd:cd05008   80 TNVVGSTLAREADYVLYLRAG 100
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
14-181 4.86e-08

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 51.24  E-value: 4.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  14 LDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLG------KNAHVIGeSTTPSIHEGDLFIVISG 87
Cdd:PRK15482 113 LEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGyrvaceADTHVQA-TVSQALKKGDVQIAISY 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  88 SGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGtkhDAEGSAQPLGSLFEQASqiLLDSLVLDLMKEL 167
Cdd:PRK15482 192 SGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSG---ETEWRSSSMSTRTAQNS--VTDLLFVGLVQLN 266

                        170
                 ....*....|....
gi 488403226 168 DVSEETMQQNHANL 181
Cdd:PRK15482 267 DVESLKMIQRSSEL 280
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
14-131 1.07e-07

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 50.15  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  14 LDSTLAHVEAEQAQAFVQEVLNAEHVFVAGKGRSGFVANSFAMRLNQLGKNA------HVIgESTTPSIHEGDLFIVISG 87
Cdd:PRK11557 106 MRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAvaerdmHAL-LATVQALSPDDLLLAISY 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488403226  88 SGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELAN----TVIELPA 131
Cdd:PRK11557 185 SGERRELNLAADEALRVGAKVLAITGFTPNALQQRAShclyTIAEEQA 232
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 12-130 1.66e-06

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: 46.89  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  12 DELDSTLAHVEAEQAQAfVQEVLNAE-HVFVAGKGRSGFVANSFAMRLNQLGKNAHVIgeSTTPSIH-------EGDLFI 83
Cdd:COG0794   20 EALAALAERLDESFEKA-VELILNCKgRVVVTGMGKSGHIARKIAATLASTGTPAFFL--HPAEASHgdlgmitPGDVVI 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488403226  84 VISGSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELP 130
Cdd:COG0794   97 AISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLP 143
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 39-112 1.89e-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: 44.29  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  39 VFVAGKGRSGFVANSFAMRLNQLGKnAHVIGESTTPSIH--------EGDLFIVISGSGSTEHLRLLADKAKSVGAQVVL 110
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTG-IEVVALIATELEHasllsllrKGDVVIALSYSGRTEELLAALEIAKELGIPVIA 79


                 ..
gi 488403226 111 LS 112
Cdd:cd04795   80 IT 81
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 78-132 9.15e-05

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: 41.74  E-value: 9.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488403226  78 EGDLFIVISGSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAG 132
Cdd:cd05007  118 ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITG 172
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
35-176 1.69e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 40.90  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  35 NAEHVFVAGKGRSGFVANSFAMRLNQLGKNAHVIGES-----TTPSIHEGDLFIVISGSGSTEHLRLLADKAKSVGAQVV 109
Cdd:PRK11337 139 QARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAhimlmSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKII 218

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488403226 110 LLSTKPESPIGELANTVIELPA-GTKHDAEGSAQPLGSLfeqasqILLDSL-VLDLMKELDVSEETMQQ 176
Cdd:PRK11337 219 CITNSYHSPIAKLADYVICSTAqGSPLLGENAAARIAQL------NILDAFfVSVAQLNIEQAEINLQK 281
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 76-132 3.45e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 40.15  E-value: 3.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488403226  76 IHEGDLFIVISGSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAG 132
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVG 185
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 39-132 3.76e-04

The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.


Pssm-ID: 240148 [Multi-domain]  Cd Length: 119  Bit Score: 38.40  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488403226  39 VFVAGKGRSGfVANSFAMRLNQLGKNAHVI---GESTTPSIHEGDLFIVISGSGSTEHLRLLADKAKSVGAQVVLLSTKP 115
Cdd:cd05017    2 IVILGMGGSG-IGGDLLESLLLDEAKIPVYvvkDYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAITSGG 80

                         90       100
                 ....*....|....*....|.
gi 488403226 116 EspIGELANT----VIELPAG 132
Cdd:cd05017   81 K--LLEMAREhgvpVIIIPKG 99
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 72-133 4.23e-04

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: 38.33  E-value: 4.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488403226  72 TTP-SIHEGDLFIVISGSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPAGT 133
Cdd:cd05710   40 TGPkRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIVYGFEI 102
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 77-130 4.38e-04

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 39.59  E-value: 4.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488403226  77 HEGDLFIVISGSGSTEHLRLLADKAKSVGAQVVLLsTKPESPIGELANTVIELP 130
Cdd:PRK11302 174 SDGDVVVLISHTGRTKSLVELAQLARENGATVIAI-TSAGSPLAREATLALTLD 226
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 77-131 1.54e-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: 37.49  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488403226  77 HEGDLFIVISGSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVIELPA 131
Cdd:cd05006  100 QPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPS 154
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 80-144 2.59e-03

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 37.36  E-value: 2.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488403226  80 DLFIVISGSGSTEHLRLLADKAKSVGAQVVLLSTKPESPIGELANTVI------ELPAGTKHDAEGSAQPL 144
Cdd:PRK12570 129 DVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAIspvvgpEVLTGSTRLKSGTAQKM 199
 
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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