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Conserved domains on  [gi|447102508|ref|WP_001179764|]
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MULTISPECIES: rhamnulose-1-phosphate aldolase [Enterobacteriaceae]

Protein Classification

rhamnulose-1-phosphate aldolase( domain architecture ID 10012058)

rhamnulose-1-phosphate aldolase catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03634 PRK03634
rhamnulose-1-phosphate aldolase; Provisional
 1-274 0e+00

rhamnulose-1-phosphate aldolase; Provisional


:

Pssm-ID: 179615 [Multi-domain]  Cd Length: 274  Bit Score: 519.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   1 MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYKDNFHAQPRYIPLSQPMPLLANTPFIVTGSGKFFR 80
Cdd:PRK03634   1 MQNILDSWFVQGMIKVTSDLWLKGWDERNGGNISLRLTEEEVAPYGDDFHQQPRYIPLSQPMPELAGTYFLVTGSGKFFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  81 NVQLDPAANLGVVKVDSDGAGYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAV 160
Cdd:PRK03634  81 NVQLDPAANLGVIRIDSDGAGYHILWGLTNGGKPTSELPAHLMSHIARLKATNGKDRVIMHCHATNLIALTYVLELDEAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 161 FTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVK 240
Cdd:PRK03634 161 FTRTLWEMSTECLVVFPDGVGIVPWMVPGTDEIGQATAEKMQKHDLVLWPKHGVFGSGPTLDEAFGLIDTAEKSAEIYVK 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 447102508 241 VYSMGGMKQTISREELIALGKRFGVTPLASALAL 274
Cdd:PRK03634 241 VLSMGGMKQTITDEELIALGERFGVTPLASALAL 274
 
Name Accession Description Interval E-value
PRK03634 PRK03634
rhamnulose-1-phosphate aldolase; Provisional
 1-274 0e+00

rhamnulose-1-phosphate aldolase; Provisional


Pssm-ID: 179615 [Multi-domain]  Cd Length: 274  Bit Score: 519.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   1 MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYKDNFHAQPRYIPLSQPMPLLANTPFIVTGSGKFFR 80
Cdd:PRK03634   1 MQNILDSWFVQGMIKVTSDLWLKGWDERNGGNISLRLTEEEVAPYGDDFHQQPRYIPLSQPMPELAGTYFLVTGSGKFFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  81 NVQLDPAANLGVVKVDSDGAGYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAV 160
Cdd:PRK03634  81 NVQLDPAANLGVIRIDSDGAGYHILWGLTNGGKPTSELPAHLMSHIARLKATNGKDRVIMHCHATNLIALTYVLELDEAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 161 FTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVK 240
Cdd:PRK03634 161 FTRTLWEMSTECLVVFPDGVGIVPWMVPGTDEIGQATAEKMQKHDLVLWPKHGVFGSGPTLDEAFGLIDTAEKSAEIYVK 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 447102508 241 VYSMGGMKQTISREELIALGKRFGVTPLASALAL 274
Cdd:PRK03634 241 VLSMGGMKQTITDEELIALGERFGVTPLASALAL 274
rhamnu_1P_ald TIGR02624
rhamnulose-1-phosphate aldolase; Members of this family are the enzyme RhaD, ...
 1-272 0e+00

rhamnulose-1-phosphate aldolase; Members of this family are the enzyme RhaD, rhamnulose-1-phosphate aldolase.


Pssm-ID: 131673  Cd Length: 270  Bit Score: 503.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508    1 MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYKDnFHAQPRYIPLSQPMPLLANTPFIVTGSGKFFR 80
Cdd:TIGR02624   1 MQDILDSPFVQEMIKTTSDLWRLGWDERNGGNISLRLDEEEVAPYLD-FHQVPRKIPLKFPAPELANKYFLVTGSGKFFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   81 NVQLDPAANLGVVKVDSDGAGYHILWGLTNEAVPTSELPAHFLSHCERIKATNgKDRVIMHCHATNLIALTYVLENDTAV 160
Cdd:TIGR02624  80 NVEENPAENLGILRVSEDGASVHLLWGLTDGGVPTSELPAHFMSHIARLKVDP-ENRVIMHCHATNLIAMTFTHELDEAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  161 FTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVK 240
Cdd:TIGR02624 159 FTRTLWQMCTECLVVFPDGVGIIPWMVPGTNEIGEATAEKMKEHRLVLWPHHGIFGAGPSLDETFGLIETAEKSAEVYTK 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 447102508  241 VYSMGGMKQTISREELIALGKRFGVTPLASAL 272
Cdd:TIGR02624 239 VYSQGGVKQTISDEQLIALAKRFGVTPKAGYL 270
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 7-264 7.72e-76

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 229.56  E-value: 7.72e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   7 SWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDAdiapykdnfhaqpryiplsqpmpllanTPFIVTGSGKFFRNVQldp 86
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDR---------------------------GYFLITPSGVDYEEMT--- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  87 AANLGVVkvdsDGAGYHILwgltnEAVPTSELPAHFLSHCERIKAtngkdRVIMHCHATNLIALTYVlendtavFTRQLW 166
Cdd:cd00398   51 ASDLVVV----DAQGKVVE-----GKKPSSETPLHLALYRARPDI-----GCIVHTHSTHATAVSQL-------KEGLIP 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 167 EGSTECLVVFPDGVGILPWMVP--GTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVKVYSM 244
Cdd:cd00398  110 AGHTACAVYFTGDIPCTPYMTPetGEDEIGTQRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSM 189

                        250       260
                 ....*....|....*....|
gi 447102508 245 GGMKQTISREELIALGKRFG 264
Cdd:cd00398  190 GGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 11-264 1.07e-33

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 121.48  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  11 QGMIKATTDAWLKGWDERNGGNLTLRLDDADiapykdnfhaqpryiplsqpmpllantpFIVTGSGKFFRNVQldpAANL 90
Cdd:COG0235    8 EELAAAGRRLARRGLVDGTAGNISVRLDDDR----------------------------FLITPSGVDFGELT---PEDL 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  91 gvVKVDSDGagyHILWGltnEAVPTSELPAHFLSHCERIKAtngkdRVIMHCHATNLIALTYVLENDTAVFTrqlwegsT 170
Cdd:COG0235   57 --VVVDLDG---NVVEG---DLKPSSETPLHLAIYRARPDV-----GAVVHTHSPYATALSALGEPLPPLEQ-------T 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 171 ECLVVFPDgVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVKVYSMGGmKQT 250
Cdd:COG0235  117 EAAAFLGD-VPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGG-PLV 194

                        250
                 ....*....|....
gi 447102508 251 ISREELIALGKRFG 264
Cdd:COG0235  195 LSDEEIDKLARKFG 208
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 13-239 3.16e-30

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 111.96  E-value: 3.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508    13 MIKATTDAWLKGWDERNGGNLTLRLDDADIapykdnfhaqpryiplsqpmpllantpFIVTGSGKFFRNVQldpAANLgv 92
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDL---------------------------FLITPSGVDFGELT---ASDL-- 48

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508    93 VKVDSDGAgyHILWGLTneAVPTSELPAHFLSHCERIKAtngkdRVIMHCHATNLIALtyvlendTAVFTRQLWEGSTEC 172
Cdd:smart01007  49 VVVDLDGN--VVEGGGG--PKPSSETPLHLAIYRARPDV-----GAVVHTHSPYATAL-------AALGKPLPLLPTEQA 112

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447102508   173 LVVFPDGVGILPWMVPGTD------EIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLV 239
Cdd:smart01007 113 AAFLGGEIPYAPYAGPGTElaeegaELAEALAEALPDRPAVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 11-239 4.29e-25

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 98.00  E-value: 4.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   11 QGMIKATTDAWLKGWDERNGGNLTLRLDDADiapykdnfhaqpryiplsqpmpllantpFIVTGSGKFFRNVQldpAANL 90
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGDG----------------------------FLITPSGVDFGELT---PEDL 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   91 gvVKVDSDgaGYHILWGLTneavPTSELPAHFLSHCERIKAtngkdRVIMHCHATNLIALtyvlendtAVFTRQLWEGST 170
Cdd:pfam00596  50 --VVVDLD--GNVVEGGLK----PSSETPLHLAIYRARPDA-----GAVVHTHSPYATAL--------SLAKEGLPPITQ 108

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  171 ECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHS-LVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLV 239
Cdd:pfam00596 109 EAADFLGGDIPIIPYYTPGTEELGERIAEALGGDRkAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
 
Name Accession Description Interval E-value
PRK03634 PRK03634
rhamnulose-1-phosphate aldolase; Provisional
 1-274 0e+00

rhamnulose-1-phosphate aldolase; Provisional


Pssm-ID: 179615 [Multi-domain]  Cd Length: 274  Bit Score: 519.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   1 MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYKDNFHAQPRYIPLSQPMPLLANTPFIVTGSGKFFR 80
Cdd:PRK03634   1 MQNILDSWFVQGMIKVTSDLWLKGWDERNGGNISLRLTEEEVAPYGDDFHQQPRYIPLSQPMPELAGTYFLVTGSGKFFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  81 NVQLDPAANLGVVKVDSDGAGYHILWGLTNEAVPTSELPAHFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAV 160
Cdd:PRK03634  81 NVQLDPAANLGVIRIDSDGAGYHILWGLTNGGKPTSELPAHLMSHIARLKATNGKDRVIMHCHATNLIALTYVLELDEAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 161 FTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVK 240
Cdd:PRK03634 161 FTRTLWEMSTECLVVFPDGVGIVPWMVPGTDEIGQATAEKMQKHDLVLWPKHGVFGSGPTLDEAFGLIDTAEKSAEIYVK 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 447102508 241 VYSMGGMKQTISREELIALGKRFGVTPLASALAL 274
Cdd:PRK03634 241 VLSMGGMKQTITDEELIALGERFGVTPLASALAL 274
rhamnu_1P_ald TIGR02624
rhamnulose-1-phosphate aldolase; Members of this family are the enzyme RhaD, ...
 1-272 0e+00

rhamnulose-1-phosphate aldolase; Members of this family are the enzyme RhaD, rhamnulose-1-phosphate aldolase.


Pssm-ID: 131673  Cd Length: 270  Bit Score: 503.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508    1 MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYKDnFHAQPRYIPLSQPMPLLANTPFIVTGSGKFFR 80
Cdd:TIGR02624   1 MQDILDSPFVQEMIKTTSDLWRLGWDERNGGNISLRLDEEEVAPYLD-FHQVPRKIPLKFPAPELANKYFLVTGSGKFFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   81 NVQLDPAANLGVVKVDSDGAGYHILWGLTNEAVPTSELPAHFLSHCERIKATNgKDRVIMHCHATNLIALTYVLENDTAV 160
Cdd:TIGR02624  80 NVEENPAENLGILRVSEDGASVHLLWGLTDGGVPTSELPAHFMSHIARLKVDP-ENRVIMHCHATNLIAMTFTHELDEAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  161 FTRQLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVK 240
Cdd:TIGR02624 159 FTRTLWQMCTECLVVFPDGVGIIPWMVPGTNEIGEATAEKMKEHRLVLWPHHGIFGAGPSLDETFGLIETAEKSAEVYTK 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 447102508  241 VYSMGGMKQTISREELIALGKRFGVTPLASAL 272
Cdd:TIGR02624 239 VYSQGGVKQTISDEQLIALAKRFGVTPKAGYL 270
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 7-264 7.72e-76

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 229.56  E-value: 7.72e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   7 SWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDAdiapykdnfhaqpryiplsqpmpllanTPFIVTGSGKFFRNVQldp 86
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDR---------------------------GYFLITPSGVDYEEMT--- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  87 AANLGVVkvdsDGAGYHILwgltnEAVPTSELPAHFLSHCERIKAtngkdRVIMHCHATNLIALTYVlendtavFTRQLW 166
Cdd:cd00398   51 ASDLVVV----DAQGKVVE-----GKKPSSETPLHLALYRARPDI-----GCIVHTHSTHATAVSQL-------KEGLIP 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 167 EGSTECLVVFPDGVGILPWMVP--GTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVKVYSM 244
Cdd:cd00398  110 AGHTACAVYFTGDIPCTPYMTPetGEDEIGTQRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSM 189

                        250       260
                 ....*....|....*....|
gi 447102508 245 GGMKQTISREELIALGKRFG 264
Cdd:cd00398  190 GGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 11-264 1.07e-33

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 121.48  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  11 QGMIKATTDAWLKGWDERNGGNLTLRLDDADiapykdnfhaqpryiplsqpmpllantpFIVTGSGKFFRNVQldpAANL 90
Cdd:COG0235    8 EELAAAGRRLARRGLVDGTAGNISVRLDDDR----------------------------FLITPSGVDFGELT---PEDL 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  91 gvVKVDSDGagyHILWGltnEAVPTSELPAHFLSHCERIKAtngkdRVIMHCHATNLIALTYVLENDTAVFTrqlwegsT 170
Cdd:COG0235   57 --VVVDLDG---NVVEG---DLKPSSETPLHLAIYRARPDV-----GAVVHTHSPYATALSALGEPLPPLEQ-------T 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 171 ECLVVFPDgVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLVKVYSMGGmKQT 250
Cdd:COG0235  117 EAAAFLGD-VPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGG-PLV 194

                        250
                 ....*....|....
gi 447102508 251 ISREELIALGKRFG 264
Cdd:COG0235  195 LSDEEIDKLARKFG 208
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 13-239 3.16e-30

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 111.96  E-value: 3.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508    13 MIKATTDAWLKGWDERNGGNLTLRLDDADIapykdnfhaqpryiplsqpmpllantpFIVTGSGKFFRNVQldpAANLgv 92
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDL---------------------------FLITPSGVDFGELT---ASDL-- 48

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508    93 VKVDSDGAgyHILWGLTneAVPTSELPAHFLSHCERIKAtngkdRVIMHCHATNLIALtyvlendTAVFTRQLWEGSTEC 172
Cdd:smart01007  49 VVVDLDGN--VVEGGGG--PKPSSETPLHLAIYRARPDV-----GAVVHTHSPYATAL-------AALGKPLPLLPTEQA 112

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447102508   173 LVVFPDGVGILPWMVPGTD------EIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLV 239
Cdd:smart01007 113 AAFLGGEIPYAPYAGPGTElaeegaELAEALAEALPDRPAVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 11-239 4.29e-25

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 98.00  E-value: 4.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   11 QGMIKATTDAWLKGWDERNGGNLTLRLDDADiapykdnfhaqpryiplsqpmpllantpFIVTGSGKFFRNVQldpAANL 90
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGDG----------------------------FLITPSGVDFGELT---PEDL 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508   91 gvVKVDSDgaGYHILWGLTneavPTSELPAHFLSHCERIKAtngkdRVIMHCHATNLIALtyvlendtAVFTRQLWEGST 170
Cdd:pfam00596  50 --VVVDLD--GNVVEGGLK----PSSETPLHLAIYRARPDA-----GAVVHTHSPYATAL--------SLAKEGLPPITQ 108

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  171 ECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHS-LVLWPFHGVFGSGSTLDETFGLIDTAEKSAQVLV 239
Cdd:pfam00596 109 EAADFLGGDIPIIPYYTPGTEELGERIAEALGGDRkAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
PRK08130 PRK08130
putative aldolase; Validated
 31-266 2.12e-06

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 47.18  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  31 GNLTLRLDDADiapykdnfhaqpryiplsqpmpLLAnTPfivTGS--GKffrnvqLDPAAnlgVVKVDSDGagyhilwgl 108
Cdd:PRK08130  28 GNISARLDDGG----------------------WLV-TP---TGSclGR------LDPAR---LSKVDADG--------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 109 tnEAV----PTSELPAHflshcERIKATNGKDRVIMHCHATNLIALTYVLENDTavftrqlwegsTECL------VVFPD 178
Cdd:PRK08130  64 --NWLsgdkPSKEVPLH-----RAIYRNNPECGAVVHLHSTHLTALSCLGGLDP-----------TNVLppftpyYVMRV 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 179 G-VGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAqvlvKVYSM-GGMK-QTISREE 255
Cdd:PRK08130 126 GhVPLIPYYRPGDPAIAEALAGLAARYRAVLLANHGPVVWGSSLEAAVNATEELEETA----KLILLlGGRPpRYLTDEE 201

                        250
                 ....*....|.
gi 447102508 256 LIALGKRFGVT 266
Cdd:PRK08130 202 IAELRSTFGAR 212
PRK08660 PRK08660
aldolase;
70-238 8.46e-05

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 42.25  E-value: 8.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508  70 FIVTGSGkffrnVQLDPAANLGVVKVDSDGAGyhilwGLTNEAvpTSELPahflSHCERIKATNGKdrVIMHCHATNLIA 149
Cdd:PRK08660  33 LLITRTG-----SMLDEITEGDVIEVGIDDDG-----SVDPLA--SSETP----VHRAIYRRTSAK--AIVHAHPPYAVA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 150 LTyvLENDTAVFTRQlwEGSTEClvvfpdgvGILPWMV--PGTDEIGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGL 227
Cdd:PRK08660  95 LS--LLEDEIVPLDS--EGLYFL--------GTIPVVGgdIGSGELAENVARALSEHKGVVVRGHGTFAIGKTLEEAYIY 162

                        170
                 ....*....|.
gi 447102508 228 IDTAEKSAQVL 238
Cdd:PRK08660 163 TSQLEHSCKVL 173
PRK08333 PRK08333
aldolase;
114-237 2.29e-04

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 40.96  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 114 PTSELPAHFLSHCERikatngKD-RVIMHCHATNLIALTYVLENDTAVFTRQlwegsTEclvVFPDGVGILPWMVPGTDE 192
Cdd:PRK08333  68 PSSEYRLHLAVYRNR------PDvRAIAHLHPPYSIVASTLLEEELPIITPE-----AE---LYLKKIPILPFRPAGSVE 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447102508 193 IGQATAQEMQKHSLVLWPFHGVFGSGSTLDETFGLIDTAEKSAQV 237
Cdd:PRK08333 134 LAEQVAEAMKEYDAVIMERHGIVTVGRSLREAFYKAELVEESAKL 178
PRK07490 PRK07490
hypothetical protein; Provisional
 137-245 4.08e-03

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 37.78  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 137 RVIMHCHATNLIALTYV-------LENDTAVFTRQlwegsteclVVFPDGVGILpwmvpGTDEIGQATAQEMQKHSLVLW 209
Cdd:PRK07490  99 RCVMHVHSVYATALACLadptlppIDQNTARFFNR---------VAVDTLYGGM-----ALEEEGERLAGLLGDKRRLLM 164

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 447102508 210 PFHGVFGSGSTLDETFGLIDTAEKSAQVLVKVYSMG 245
Cdd:PRK07490 165 GNHGVLVTGDTVAEAFDDLYYFERACQTYITALSTG 200
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
137-233 4.68e-03

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 38.29  E-value: 4.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447102508 137 RVIMHCHATNLIALTyvleN--DTAVFTRQlwegsteclvVFPDGVGILPWMVPGTD---EIGQATAQEMQKHSLVLWPf 211
Cdd:PRK08324 125 KHVDHTHPDAIIAIA----NapDGEELTRE----------IFGDRVGWVPYVRPGFDlalAIAEAVRANPGAEGVVLGK- 189

                         90       100
                 ....*....|....*....|....*.
gi 447102508 212 HGVFGSGSTLDE----TFGLIDTAEK 233
Cdd:PRK08324 190 HGLFTWGDTAKEayerTIEIITRAEE 215
 
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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