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Conserved domains on  [gi|499595940|ref|WP_011276674|]
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6-phospho-3-hexuloisomerase [Staphylococcus haemolyticus]

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 3.59e-96

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: 276.11  E-value: 3.59e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940    7 YKLILEELDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTTPSIKEHDLFVILS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940   87 GSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNVEG---SEQPLGSLFEQSSLLFLDSVVLGL 163
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGnykSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 499595940  164 METFDISEEEMQNNHANLE 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 3.59e-96

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: 276.11  E-value: 3.59e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940    7 YKLILEELDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTTPSIKEHDLFVILS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940   87 GSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNVEG---SEQPLGSLFEQSSLLFLDSVVLGL 163
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGnykSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 499595940  164 METFDISEEEMQNNHANLE 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 1.87e-83

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: 244.02  E-value: 1.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940   6 NYKLILEELDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTTPSIKEHDLFVIL 85
Cdd:cd05005    3 YLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLIAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  86 SGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNVEG---SEQPLGSLFEQSSLLFLDSVVLG 162
Cdd:cd05005   83 SGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGehkSIQPLGTLFEQSALVFLDAVIAK 162

                        170
                 ....*....|....*..
gi 499595940 163 LMETFDISEEEMQNNHA 179
Cdd:cd05005  163 LMEELGVSEEEMKKRHA 179
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 10-165 3.45e-22

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 90.37  E-value: 3.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  10 ILEELDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGES------TTPSIKEHDLFV 83
Cdd:COG1737  108 EIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGDghlqaeSAALLGPGDVVI 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  84 ILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNVEGseqPLGSLFeqSSLLFLDSVVLGL 163
Cdd:COG1737  188 AISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSS---AFSSRV--AQLALIDALAAAV 262


                 ..
gi 499595940 164 ME 165
Cdd:COG1737  263 AQ 264
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 36-137 5.50e-17

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 73.10  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940   36 AQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTT------PSIKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKVV 109
Cdd:pfam01380   5 AKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARGAKII 84

                          90       100
                  ....*....|....*....|....*...
gi 499595940  110 LLTTSPDSPIGELAETVIELPAGTKHNV 137
Cdd:pfam01380  85 AITDSPGSPLAREADHVLYINAGPETGV 112
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
14-174 1.03e-06

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 47.39  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  14 LDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFV-----VGESTTPSIKEHDLFVILSGS 88
Cdd:PRK15482 113 LEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGYRVACeadthVQATVSQALKKGDVQIAISYS 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  89 GSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGtkhNVEGSEQPLGSLFEQSSLlfLDSVVLGLMETFD 168
Cdd:PRK15482 193 GSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSG---ETEWRSSSMSTRTAQNSV--TDLLFVGLVQLND 267


                 ....*.
gi 499595940 169 ISEEEM 174
Cdd:PRK15482 268 VESLKM 273
 
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 3.59e-96

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: 276.11  E-value: 3.59e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940    7 YKLILEELDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTTPSIKEHDLFVILS 86
Cdd:TIGR03127   1 AKLILDEISQVASRIDEEELDKLADKIIKAKRIFVAGAGRSGLVGKAFAMRLMHLGFNVYVVGETTTPSIKKGDLLIAIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940   87 GSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNVEG---SEQPLGSLFEQSSLLFLDSVVLGL 163
Cdd:TIGR03127  81 GSGETESLVTVAKKAKEIGATVAAITTNPESTLGKLADVVVEIPAATKKDSEGnykSIQPLGSLFEQSLLLFLDAVILKL 160

                         170
                  ....*....|....*....
gi 499595940  164 METFDISEEEMQNNHANLE 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 1.87e-83

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: 244.02  E-value: 1.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940   6 NYKLILEELDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTTPSIKEHDLFVIL 85
Cdd:cd05005    3 YLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGETTTPAIGPGDLLIAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  86 SGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNVEG---SEQPLGSLFEQSSLLFLDSVVLG 162
Cdd:cd05005   83 SGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGehkSIQPLGTLFEQSALVFLDAVIAK 162

                        170
                 ....*....|....*..
gi 499595940 163 LMETFDISEEEMQNNHA 179
Cdd:cd05005  163 LMEELGVSEEEMKKRHA 179
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 10-165 3.45e-22

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 90.37  E-value: 3.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  10 ILEELDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGES------TTPSIKEHDLFV 83
Cdd:COG1737  108 EIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVVLLDGDghlqaeSAALLGPGDVVI 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  84 ILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNVEGseqPLGSLFeqSSLLFLDSVVLGL 163
Cdd:COG1737  188 AISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSS---AFSSRV--AQLALIDALAAAV 262


                 ..
gi 499595940 164 ME 165
Cdd:COG1737  263 AQ 264
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 24-131 2.39e-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: 2.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  24 EQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTTP-----SIKEHDLFVILSGSGSTEHLRLLA 98
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQlmsaaNLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499595940  99 EKAQSIGAKVVLLTTSPDSPIGELAETVIELPA 131
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSS 113
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 36-137 5.50e-17

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


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 73.10  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940   36 AQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTT------PSIKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKVV 109
Cdd:pfam01380   5 AKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElrhgvlALVDEDDLVIAISYSGETKDLLAAAELAKARGAKII 84

                          90       100
                  ....*....|....*....|....*...
gi 499595940  110 LLTTSPDSPIGELAETVIELPAGTKHNV 137
Cdd:pfam01380  85 AITDSPGSPLAREADHVLYINAGPETGV 112
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 12-137 2.03e-13

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: 66.85  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  12 EELDRTLSHVQDEqYDRFANDV--NGAQRIFTAGKGRSGFMANSFAMRLN-QLGKEAFVVGESTTPS-----IKEHDLFV 83
Cdd:COG2222    9 EAWRRALAALAAA-IAALLARLraKPPRRVVLVGAGSSDHAAQAAAYLLErLLGIPVAALAPSELVVypaylKLEGTLVV 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499595940  84 ILSGSG-STEHLRLLaEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNV 137
Cdd:COG2222   88 AISRSGnSPEVVAAL-ELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSV 141
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 38-130 1.36e-10

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: 56.01  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  38 RIFTAGKGRSGFMANSFAMRLNQLGKEAFVVgestTPS---------IKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKV 108
Cdd:cd05014    2 KVVVTGVGKSGHIARKIAATLSSTGTPAFFL----HPTealhgdlgmVTPGDVVIAISNSGETDELLNLLPHLKRRGAPI 77

                         90       100
                 ....*....|....*....|..
gi 499595940 109 VLLTTSPDSPIGELAETVIELP 130
Cdd:cd05014   78 IAITGNPNSTLAKLSDVVLDLP 99
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 38-132 5.46e-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: 51.73  E-value: 5.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  38 RIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGEST-----TPSIKEHDLFVILSGSG-STEHLRLLaEKAQSIGAKVVLL 111
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASefryrRPLLDEDTLVIAISQSGeTADTLAAL-RLAKEKGAKTVAI 79

                         90       100
                 ....*....|....*....|.
gi 499595940 112 TTSPDSPIGELAETVIELPAG 132
Cdd:cd05008   80 TNVVGSTLAREADYVLYLRAG 100
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
14-174 1.03e-06

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 47.39  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  14 LDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFV-----VGESTTPSIKEHDLFVILSGS 88
Cdd:PRK15482 113 LEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGYRVACeadthVQATVSQALKKGDVQIAISYS 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  89 GSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGtkhNVEGSEQPLGSLFEQSSLlfLDSVVLGLMETFD 168
Cdd:PRK15482 193 GSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSG---ETEWRSSSMSTRTAQNSV--TDLLFVGLVQLND 267


                 ....*.
gi 499595940 169 ISEEEM 174
Cdd:PRK15482 268 VESLKM 273
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 72-133 3.25e-06

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


Pssm-ID: 240214 [Multi-domain]  Cd Length: 120  Bit Score: 44.10  E-value: 3.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595940  72 TTP-SIKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGT 133
Cdd:cd05710   40 TGPkRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIVYGFEI 102
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 78-132 5.12e-06

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


Pssm-ID: 240140 [Multi-domain]  Cd Length: 257  Bit Score: 45.21  E-value: 5.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499595940  78 EHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAG 132
Cdd:cd05007  118 ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITG 172
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
14-163 3.10e-05

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 43.37  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  14 LDRTLS-------HVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGES-----TTPSIKEHDL 81
Cdd:PRK14101 439 LDNTVSailqlreHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLymqaaSAALLGKGDV 518

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  82 FVILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSpDSPIGELAETVIElpagTKHnVEGSEQPLGSLFEQSSLLFLDSVVL 161
Cdd:PRK14101 519 IVAVSKSGRAPELLRVLDVAMQAGAKVIAITSS-NTPLAKRATVALE----TDH-IEMRESQLSMISRILHLVMIDILAV 592


                 ..
gi 499595940 162 GL 163
Cdd:PRK14101 593 GV 594
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
11-131 3.17e-05

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 43.21  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  11 LEELDRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGES-----TTPSIKEHDLFVIL 85
Cdd:PRK11337 115 LQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAhimlmSAALLQEGDVVLVV 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499595940  86 SGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPA 131
Cdd:PRK11337 195 SHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTA 240
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 39-112 3.94e-05

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: 40.44  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  39 IFTAGKGRSGFMANSFAMRLNQLGKEAfVVGESTTPS--------IKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVL 110
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIE-VVALIATELehasllslLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIA 79


                 ..
gi 499595940 111 LT 112
Cdd:cd04795   80 IT 81
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 38-130 4.41e-05

D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440557 [Multi-domain]  Cd Length: 317  Bit Score: 42.66  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  38 RIFTAGKGRSGFMANSFAMRLNQLGKEAFVVgestTPS---------IKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKV 108
Cdd:COG0794   46 RVVVTGMGKSGHIARKIAATLASTGTPAFFL----HPAeashgdlgmITPGDVVIAISNSGETEELLALLPLLKRLGVPL 121

                         90       100
                 ....*....|....*....|..
gi 499595940 109 VLLTTSPDSPIGELAETVIELP 130
Cdd:COG0794  122 IAITGNPDSTLARAADVVLDLP 143
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 76-132 5.18e-05

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 42.46  E-value: 5.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499595940  76 IKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAG 132
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVG 185
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 78-128 1.89e-04

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 40.83  E-value: 1.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499595940  78 EHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIE 128
Cdd:PRK12570 127 ADDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAIS 177
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 38-124 2.76e-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: 38.79  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  38 RIFTAGKGRSGFMANSF-AMRLNQLGKEAFVV-GESTTPSIKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSp 115
Cdd:cd05017    1 NIVILGMGGSGIGGDLLeSLLLDEAKIPVYVVkDYTLPAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAITSG- 79


                 ....*....
gi 499595940 116 dspiGELAE 124
Cdd:cd05017   80 ----GKLLE 84
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 7-132 9.36e-04

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 38.81  E-value: 9.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940   7 YKLILEELDRTLSHVQDEQYDRFANdvngaqrIFTAGKGRSGF---MANSFAMRlnQLGKEAFVVGESTTPS-IKEHDLF 82
Cdd:PRK08674  12 PEQFEEALEIAISLDLEEDLEKIDN-------IVISGMGGSGIggdLLRILLFD--ELKVPVFVNRDYTLPAfVDEKTLV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499595940  83 VILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSpdspiGELAE-------TVIELPAG 132
Cdd:PRK08674  83 IAVSYSGNTEETLSAVEQALKRGAKIIAITSG-----GKLKEmakehglPVIIVPGG 134
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
38-178 2.59e-03

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 37.44  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  38 RIFTAGKGRSGFMANSFAMRLNQLGKEAFVVGESTT-----PSIKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLT 112
Cdd:PRK11543  44 KVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEAlhgdlGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMT 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940 113 TSPDSPIGELAETVIELpagtkhNVEGSEQPLGsLFEQSS----LLFLDSVVLGLMETFDISEEEMQNNH 178
Cdd:PRK11543 124 GKPTSPLGLAAKAVLDI------SVEREACPMH-LAPTSStvntLMMGDALAMAVMQARGFNEEDFARSH 186
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 78-130 6.15e-03

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 36.13  E-value: 6.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499595940  78 EHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLTtSPDSPIGELAETVIELP 130
Cdd:PRK11302 175 DGDVVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPLAREATLALTLD 226
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 80-138 6.78e-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: 35.56  E-value: 6.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499595940  80 DLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPAGTKHNVE 138
Cdd:cd05006  103 DVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHVPSDDTPRIQ 161
PRK13938 PRK13938
phosphoheptose isomerase; Provisional
 15-131 9.25e-03

phosphoheptose isomerase; Provisional


Pssm-ID: 139997 [Multi-domain]  Cd Length: 196  Bit Score: 35.48  E-value: 9.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595940  15 DRTLSHVQDEQYDRFANDVNGAQRIFTAGKGRSGFMANSFAMRLN--------QLGKEAF------------------VV 68
Cdd:PRK13938  24 DRVLLEAARAIGDRLIAGYRAGARVFMCGNGGSAADAQHFAAELTghlifdrpPLGAEALhansshltavandydydtVF 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595940  69 GESTTPSIKEHDLFVILSGSGSTEHLRLLAEKAQSIGAKVVLLTTSPDSPIGELAETVIELPA 131
Cdd:PRK13938 104 ARALEGSARPGDTLFAISTSGNSMSVLRAAKTARELGVTVVAMTGESGGQLAEFADFLINVPS 166
 
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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