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Conserved domains on  [gi|1083527499|gb|OGG27491|]
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hypothetical protein A2960_04320 [Candidatus Gottesmanbacteria bacterium RIFCSPLOWO2_01_FULL_39_12b]

Protein Classification

ribulose-phosphate 3-epimerase( domain architecture ID 10784968)

ribulose-phosphate 3-epimerase catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
6-208 1.01e-49

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


:

Pssm-ID: 439806  Cd Length: 218  Bit Score: 160.63  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   6 PAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFSDPLpFKDFK--TPVNLELHMMVKDPLRYLERFATSGFK 82
Cdd:COG0036     5 PSILSADFANLGEEVKRVEAAgADWIHIDVMDGHFVPNLTFGPPV-VKALRkhTDLPLDVHLMIENPDRYIEAFAEAGAD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  83 RFFAHVE-GNYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR----E 157
Cdd:COG0036    84 IITVHAEaTPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRelidE 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083527499 158 VDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALKSL 208
Cdd:COG0036   164 RGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
6-208 1.01e-49

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 160.63  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   6 PAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFSDPLpFKDFK--TPVNLELHMMVKDPLRYLERFATSGFK 82
Cdd:COG0036     5 PSILSADFANLGEEVKRVEAAgADWIHIDVMDGHFVPNLTFGPPV-VKALRkhTDLPLDVHLMIENPDRYIEAFAEAGAD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  83 RFFAHVE-GNYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR----E 157
Cdd:COG0036    84 IITVHAEaTPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRelidE 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083527499 158 VDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALKSL 208
Cdd:COG0036   164 RGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
4-206 2.15e-48

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 157.26  E-value: 2.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   4 VIPAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFSDPLpFKDFK--TPVNLELHMMVKDPLRYLERFATSG 80
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAgADWIHIDVMDGHFVPNLTFGPPV-VKALRkhTDLPLDVHLMVENPERYIEAFAKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  81 FKRFFAHVE-GNYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR--- 156
Cdd:cd00429    81 ADIITFHAEaTDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLReli 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083527499 157 -EVDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALK 206
Cdd:cd00429   161 pENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
1-206 1.69e-35

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 124.53  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   1 MIDVIPAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFsDPLPFKDFK--TPVNLELHMMVKDPLRYLERFA 77
Cdd:PRK05581    3 MVLIAPSILSADFARLGEEVKAVEAAgADWIHVDVMDGHFVPNLTI-GPPVVEAIRkvTKLPLDVHLMVENPDRYVPDFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  78 TSGFKRFFAHVEGN-YVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR 156
Cdd:PRK05581   82 KAGADIITFHVEASeHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1083527499 157 EV----DLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALK 206
Cdd:PRK05581  162 KLiderGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLR 215
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
4-193 4.67e-31

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 112.42  E-value: 4.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   4 VIPAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFSdPLPFKDFK--TPVNLELHMMVKDPLRYLERFATSG 80
Cdd:pfam00834   2 IAPSILSADFARLGEEIKAVENAgADWLHVDVMDGHFVPNLTIG-PLVVEALRplTDLPLDVHLMVEEPDRIIPDFAKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  81 FKRFFAHVEG-NYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR--- 156
Cdd:pfam00834  81 ADIISFHAEAtPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRkmi 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1083527499 157 -EVDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIF 193
Cdd:pfam00834 161 dERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
6-208 1.01e-49

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 160.63  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   6 PAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFSDPLpFKDFK--TPVNLELHMMVKDPLRYLERFATSGFK 82
Cdd:COG0036     5 PSILSADFANLGEEVKRVEAAgADWIHIDVMDGHFVPNLTFGPPV-VKALRkhTDLPLDVHLMIENPDRYIEAFAEAGAD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  83 RFFAHVE-GNYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR----E 157
Cdd:COG0036    84 IITVHAEaTPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRelidE 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083527499 158 VDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALKSL 208
Cdd:COG0036   164 RGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
4-206 2.15e-48

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 157.26  E-value: 2.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   4 VIPAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFSDPLpFKDFK--TPVNLELHMMVKDPLRYLERFATSG 80
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAgADWIHIDVMDGHFVPNLTFGPPV-VKALRkhTDLPLDVHLMVENPERYIEAFAKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  81 FKRFFAHVE-GNYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR--- 156
Cdd:cd00429    81 ADIITFHAEaTDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLReli 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083527499 157 -EVDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALK 206
Cdd:cd00429   161 pENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
1-206 1.69e-35

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 124.53  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   1 MIDVIPAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFsDPLPFKDFK--TPVNLELHMMVKDPLRYLERFA 77
Cdd:PRK05581    3 MVLIAPSILSADFARLGEEVKAVEAAgADWIHVDVMDGHFVPNLTI-GPPVVEAIRkvTKLPLDVHLMVENPDRYVPDFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  78 TSGFKRFFAHVEGN-YVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR 156
Cdd:PRK05581   82 KAGADIITFHVEASeHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1083527499 157 EV----DLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALK 206
Cdd:PRK05581  162 KLiderGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLR 215
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
4-207 6.39e-33

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 118.18  E-value: 6.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   4 VIPAILENDFTEVEKKIRSVENLVS-WVQIDIADNTLVPNSTFSdPLPFKDFK--TPVNLELHMMVKDPLRYLERFATSG 80
Cdd:PLN02334   10 IAPSILSADFANLAEEAKRVLDAGAdWLHVDVMDGHFVPNLTIG-PPVVKALRkhTDAPLDCHLMVTNPEDYVPDFAKAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  81 FKRFFAHVEG---NYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLD--NLDCVLVMAIEAGESGRPFRGDTIEKIKKI 155
Cdd:PLN02334   89 ASIFTFHIEQastIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEkgLVDMVLVMSVEPGFGGQSFIPSMMDKVRAL 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1083527499 156 REVDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALKS 207
Cdd:PLN02334  169 RKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRA 220
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
4-193 4.67e-31

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 112.42  E-value: 4.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   4 VIPAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFSdPLPFKDFK--TPVNLELHMMVKDPLRYLERFATSG 80
Cdd:pfam00834   2 IAPSILSADFARLGEEIKAVENAgADWLHVDVMDGHFVPNLTIG-PLVVEALRplTDLPLDVHLMVEEPDRIIPDFAKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  81 FKRFFAHVEG-NYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIR--- 156
Cdd:pfam00834  81 ADIISFHAEAtPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRkmi 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1083527499 157 -EVDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIF 193
Cdd:pfam00834 161 dERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
6-206 2.70e-30

D-ribulose-5-phosphate 3-epimerase; Provisional


Pssm-ID: 240303  Cd Length: 228  Bit Score: 111.23  E-value: 2.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   6 PAILENDFTEVEKKIRSVENL-VSWVQIDIADNTLVPNSTFSDPLpFKDFK--TP-VNLELHMMVKDPLRYLERFATSGF 81
Cdd:PTZ00170   11 PSILAADFSKLADEAQDVLSGgADWLHVDVMDGHFVPNLSFGPPV-VKSLRkhLPnTFLDCHLMVSNPEKWVDDFAKAGA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  82 KRFFAHVE--GNYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDN--LDCVLVMAIEAGESGRPFRGDTIEKIKKIRE 157
Cdd:PTZ00170   90 SQFTFHIEatEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVRELRK 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1083527499 158 VDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALK 206
Cdd:PTZ00170  170 RYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLR 218
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
6-183 7.54e-21

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 86.59  E-value: 7.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   6 PAILENDFTEVEKKIRSVENLVSWVQIDIADNTLVPNSTFSdplPF--KDFK--TPVNLELHMMVKDPLRYLERFATSGF 81
Cdd:PRK09722    7 PSLMCMDLLKFKEQIEFLNSKADYFHIDIMDGHFVPNLTLS---PFfvSQVKklASKPLDVHLMVTDPQDYIDQLADAGA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  82 KRFFAHVE--GNYVDEYIEKCYQLGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAGESGRPFRGDTIEKIKKIREV- 158
Cdd:PRK09722   84 DFITLHPEtiNGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKALr 163
                         170       180
                  ....*....|....*....|....*...
gi 1083527499 159 ---DLEIPIAVDGAMNEENARKVVAVGA 183
Cdd:PRK09722  164 ernGLEYLIEVDGSCNQKTYEKLMEAGA 191
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
8-207 2.16e-09

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 55.27  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499   8 ILENDFTEVEKKIRSV-ENLVSWVQIDIADNTLVPNSTFSdPLPFKDFKTPVNLELHMMVKDPLRYLERFATSGFKRFFA 86
Cdd:PRK08091   19 ILASNWLKFNETLTTLsENQLRLLHFDIADGQFSPFFTVG-AIAIKQFPTHCFKDVHLMVRDQFEVAKACVAAGADIVTL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499  87 HVEgNYVD-----EYIEKCYQlGVEVGLAIDGPTSFEMIHKYLDNLDCVLVMAIEAgESGRPFRGDTIEK-----IKKIR 156
Cdd:PRK08091   98 QVE-QTHDlaltiEWLAKQKT-TVLIGLCLCPETPISLLEPYLDQIDLIQILTLDP-RTGTKAPSDLILDrviqvENRLG 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083527499 157 EVDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALKS 207
Cdd:PRK08091  175 NRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKS 225
thiE PRK00043
thiamine phosphate synthase;
149-208 3.66e-06

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 45.94  E-value: 3.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083527499 149 IEKIKKIREVDLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALKSL 208
Cdd:PRK00043  148 LEGLREIRAAVGDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAA 207
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
149-207 5.45e-05

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 42.12  E-value: 5.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1083527499 149 IEKIKKIREVdLEIPIAVDGAMNEENARKVVAVGATRINSNSYIFKSTDIKGAVEALKS 207
Cdd:cd00564   139 LELLREIAEL-VEIPVVAIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
 
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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