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Conserved domains on  [gi|446361832|ref|WP_000439687|]
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MULTISPECIES: L-fuculose-phosphate aldolase [Enterobacteriaceae]

Protein Classification

class II aldolase/adducin head domain-containing protein( domain architecture ID 842)

class II aldolase/adducin head domain-containing protein involved in catalyzing central steps of carbohydrate metabolism; it promotes carbon-carbon bond cleavage and stabilizes enolate intermediates using divalent cations

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 1-213 1.10e-143

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.


The actual alignment was detected with superfamily member PRK08087:

Pssm-ID: 469663 [Multi-domain]  Cd Length: 215  Bit Score: 399.11  E-value: 1.10e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   1 MERIKLAEKIISTCREMNASGLNQGTSGNVSARYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLAC 80
Cdd:PRK08087   1 MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLPSSEWRFHMAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  81 YKARPELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAM 160
Cdd:PRK08087  81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446361832 161 DVTLEKTLWLAGETETLADLYIKCGGLHHDVPVLSEAEMTIVLEKFKTYGLKA 213
Cdd:PRK08087 161 EVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDEEIAVVLEKFKTYGLRI 213
 
Name Accession Description Interval E-value
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
1-213 1.10e-143

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 399.11  E-value: 1.10e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   1 MERIKLAEKIISTCREMNASGLNQGTSGNVSARYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLAC 80
Cdd:PRK08087   1 MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLPSSEWRFHMAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  81 YKARPELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAM 160
Cdd:PRK08087  81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446361832 161 DVTLEKTLWLAGETETLADLYIKCGGLHHDVPVLSEAEMTIVLEKFKTYGLKA 213
Cdd:PRK08087 161 EVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDEEIAVVLEKFKTYGLRI 213
fucA TIGR01086
L-fuculose phosphate aldolase; Members of this family are L-fuculose phosphate aldolase from ...
 2-212 1.60e-107

L-fuculose phosphate aldolase; Members of this family are L-fuculose phosphate aldolase from various Proteobacteria, encoded in fucose utilization operons. Homologs in other bacteria given similar annotation but scoring below the trusted cutoff may share extensive sequence similarity but are not experimenally characterized and are not found in apparent fucose utilization operons; we consider their annotation as L-fuculose phosphate aldolase to be tenuous. This model has been narrowed in scope from the previous version. [Energy metabolism, Sugars]


Pssm-ID: 188107  Cd Length: 214  Bit Score: 307.64  E-value: 1.60e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832    2 ERIKLAEKIISTCREMNASGLNQGTSGNVSARYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLACY 81
Cdd:TIGR01086   1 NRAELSQQIIDTCLEMTRLGLNQGTAGNVSVRYKDGMLITPTGIPYEKLTTEHIVYVDGNGKHEEGKLPSSEWQFHLSVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   82 KARPELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAMD 161
Cdd:TIGR01086  81 QTRPDANAVVHNHAIHCAAVSILNKSIPAIHYMVAASGTDHIPCVPYATFGSHKLASYVATGIKESKAILLQHHGLIACE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446361832  162 VTLEKTLWLAGETETLADLYIKCGGLHHDVPVLSEAEMTIVLEKFKTYGLK 212
Cdd:TIGR01086 161 VNLEKALWLAHEVEVLASLYLKTLAITLEVPVLSKEQMAVVLGKFKTYGLR 211
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-207 6.77e-69

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: 209.30  E-value: 6.77e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   1 MERIKLAEKIISTCREMNASGLNQGTSGNVSARYTGG-MLITPSGIAYSKMTPDMIVFVDDKGKPEAGKI-PSSEWLIHL 78
Cdd:COG0235    1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLkPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  79 ACYKARPELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGML 158
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGVV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446361832 159 AMDVTLEKTLWLAGETETLADLYIKCGGLhHDVPVLSEAEMTIVLEKFK 207
Cdd:COG0235  161 VWGKDLAEAFDRAEVLEEAARIQLLALAL-GGPLVLSDEEIDKLARKFG 208
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 5-207 1.19e-64

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: 198.74  E-value: 1.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   5 KLAEKIISTCREMNASGLNQGTSGNVSARY--TGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLACYK 82
Cdd:cd00398    2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDrdRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKKPSSETPLHLALYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  83 ARPELNAVIHTHAVNSTAVAI-HNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPE--LADGVSKGIRESKSLLMQHHGMLA 159
Cdd:cd00398   82 ARPDIGCIVHTHSTHATAVSQlKEGLIPAGHTACAVYFTGDIPCTPYMTPETGEdeIGTQRALGFPNSKAVLLRNHGLFA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446361832 160 MDVTLEKTLWLAGETETLADLYIKCGGLHHDVPVLSEAEMTIVLEKFK 207
Cdd:cd00398  162 WGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-182 5.50e-61

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: 188.52  E-value: 5.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832    8 EKIISTCREMNASGLNQGTSGNVSAR-YTGGMLITPSGIAYSKMTPDMIVFVDDKGKP-EAGKIPSSEWLIHLACYKARP 85
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVvEGGLKPSSETPLHLAIYRARP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   86 ELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRE-SKSLLMQHHGMLAMDVTL 164
Cdd:pfam00596  81 DAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEELGERIAEALGGdRKAVLLRNHGLLVWGKTL 160

                         170
                  ....*....|....*...
gi 446361832  165 EKTLWLAGETETLADLYI 182
Cdd:pfam00596 161 EEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-182 1.15e-47

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: 154.72  E-value: 1.15e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832    10 IISTCREMNASGLNQGTSGNVSAR--YTGGMLITPSGIAYSKMTPDMIVFVDDKGK---PEAGKIPSSEWLIHLACYKAR 84
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARvgEEDLFLITPSGVDFGELTASDLVVVDLDGNvveGGGGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832    85 PELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAV-SGTDHIPCIPYYTFGS------PELADGVSKGIRESKSLLMQHHGM 157
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAaFLGGEIPYAPYAGPGTelaeegAELAEALAEALPDRPAVLLRNHGL 160

                          170       180
                   ....*....|....*....|....*
gi 446361832   158 LAMDVTLEKTLWLAGETETLADLYI 182
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
 
Name Accession Description Interval E-value
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
1-213 1.10e-143

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 399.11  E-value: 1.10e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   1 MERIKLAEKIISTCREMNASGLNQGTSGNVSARYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLAC 80
Cdd:PRK08087   1 MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLPSSEWRFHMAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  81 YKARPELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAM 160
Cdd:PRK08087  81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446361832 161 DVTLEKTLWLAGETETLADLYIKCGGLHHDVPVLSEAEMTIVLEKFKTYGLKA 213
Cdd:PRK08087 161 EVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDEEIAVVLEKFKTYGLRI 213
fucA TIGR01086
L-fuculose phosphate aldolase; Members of this family are L-fuculose phosphate aldolase from ...
 2-212 1.60e-107

L-fuculose phosphate aldolase; Members of this family are L-fuculose phosphate aldolase from various Proteobacteria, encoded in fucose utilization operons. Homologs in other bacteria given similar annotation but scoring below the trusted cutoff may share extensive sequence similarity but are not experimenally characterized and are not found in apparent fucose utilization operons; we consider their annotation as L-fuculose phosphate aldolase to be tenuous. This model has been narrowed in scope from the previous version. [Energy metabolism, Sugars]


Pssm-ID: 188107  Cd Length: 214  Bit Score: 307.64  E-value: 1.60e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832    2 ERIKLAEKIISTCREMNASGLNQGTSGNVSARYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLACY 81
Cdd:TIGR01086   1 NRAELSQQIIDTCLEMTRLGLNQGTAGNVSVRYKDGMLITPTGIPYEKLTTEHIVYVDGNGKHEEGKLPSSEWQFHLSVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   82 KARPELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAMD 161
Cdd:TIGR01086  81 QTRPDANAVVHNHAIHCAAVSILNKSIPAIHYMVAASGTDHIPCVPYATFGSHKLASYVATGIKESKAILLQHHGLIACE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446361832  162 VTLEKTLWLAGETETLADLYIKCGGLHHDVPVLSEAEMTIVLEKFKTYGLK 212
Cdd:TIGR01086 161 VNLEKALWLAHEVEVLASLYLKTLAITLEVPVLSKEQMAVVLGKFKTYGLR 211
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-207 6.77e-69

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: 209.30  E-value: 6.77e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   1 MERIKLAEKIISTCREMNASGLNQGTSGNVSARYTGG-MLITPSGIAYSKMTPDMIVFVDDKGKPEAGKI-PSSEWLIHL 78
Cdd:COG0235    1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLkPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  79 ACYKARPELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGML 158
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGVV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446361832 159 AMDVTLEKTLWLAGETETLADLYIKCGGLhHDVPVLSEAEMTIVLEKFK 207
Cdd:COG0235  161 VWGKDLAEAFDRAEVLEEAARIQLLALAL-GGPLVLSDEEIDKLARKFG 208
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 5-207 1.19e-64

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: 198.74  E-value: 1.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   5 KLAEKIISTCREMNASGLNQGTSGNVSARY--TGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLACYK 82
Cdd:cd00398    2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDrdRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKKPSSETPLHLALYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  83 ARPELNAVIHTHAVNSTAVAI-HNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPE--LADGVSKGIRESKSLLMQHHGMLA 159
Cdd:cd00398   82 ARPDIGCIVHTHSTHATAVSQlKEGLIPAGHTACAVYFTGDIPCTPYMTPETGEdeIGTQRALGFPNSKAVLLRNHGLFA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446361832 160 MDVTLEKTLWLAGETETLADLYIKCGGLHHDVPVLSEAEMTIVLEKFK 207
Cdd:cd00398  162 WGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-182 5.50e-61

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: 188.52  E-value: 5.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832    8 EKIISTCREMNASGLNQGTSGNVSAR-YTGGMLITPSGIAYSKMTPDMIVFVDDKGKP-EAGKIPSSEWLIHLACYKARP 85
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVvEGGLKPSSETPLHLAIYRARP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   86 ELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRE-SKSLLMQHHGMLAMDVTL 164
Cdd:pfam00596  81 DAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEELGERIAEALGGdRKAVLLRNHGLLVWGKTL 160

                         170
                  ....*....|....*...
gi 446361832  165 EKTLWLAGETETLADLYI 182
Cdd:pfam00596 161 EEAFYLAEELERAAEIQL 178
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
8-210 6.32e-53

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 169.16  E-value: 6.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   8 EKIISTCREMNASGLNQGTSGNVSA--RYTGGMLITPSGIAYSKMTPDMIVFVDDKGK-PEAGKIPSSEWLIHLACYKAR 84
Cdd:PRK06833   8 EEIVAYGKKLISSGLTKGTGGNISIfnREQGLMAITPSGIDYFEIKPEDIVIMDLDGKvVEGERKPSSELDMHLIFYRNR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  85 PELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDhIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAMDVTL 164
Cdd:PRK06833  88 EDINAIVHTHSPYATTLACLGWELPAVHYLIAVAGPN-VRCAEYATFGTKELAENAFEAMEDRRAVLLANHGLLAGANNL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446361832 165 EKTLWLAGETETLADLYIKCGGLHHDVpVLSEAEMTIVLEKFKTYG 210
Cdd:PRK06833 167 KNAFNIAEEIEFCAEIYYQTKSIGEPK-LLPEDEMENMAEKFKTYG 211
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-182 1.15e-47

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: 154.72  E-value: 1.15e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832    10 IISTCREMNASGLNQGTSGNVSAR--YTGGMLITPSGIAYSKMTPDMIVFVDDKGK---PEAGKIPSSEWLIHLACYKAR 84
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARvgEEDLFLITPSGVDFGELTASDLVVVDLDGNvveGGGGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832    85 PELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAV-SGTDHIPCIPYYTFGS------PELADGVSKGIRESKSLLMQHHGM 157
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAaFLGGEIPYAPYAGPGTelaeegAELAEALAEALPDRPAVLLRNHGL 160

                          170       180
                   ....*....|....*....|....*
gi 446361832   158 LAMDVTLEKTLWLAGETETLADLYI 182
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 10-193 2.65e-30

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 111.27  E-value: 2.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  10 IISTCREMNASGLNQGTSGNVSARYT-GGMLITPSGIAYSKMTPDMIVFVDDKG---KPEAGKIPSSEWLIHLACYKARP 85
Cdd:PRK05874  11 VLAAAKDMLRRGLVEGTAGNISARRSdGNVVITPSSVDYAEMLLHDLVLVDAGGavlHAKDGRSPSTELNLHLACYRAFD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  86 ELNAVIHTHAVNSTAVAIHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAMDVTLE 165
Cdd:PRK05874  91 DIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCTEYAASGTPEVGRNAVRALEGRAAALIANHGLVAVGPRPD 170

                        170       180
                 ....*....|....*....|....*...
gi 446361832 166 KTLWLAGETETLADLYIKCGGLHHDVPV 193
Cdd:PRK05874 171 QVLRVTALVERTAQIVWGARALGGPVPI 198
PRK08130 PRK08130
putative aldolase; Validated
 1-207 3.66e-28

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 105.34  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   1 MERIKLAEKIISTCREMNASGLNQGTSGNVSARYT-GGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLA 79
Cdd:PRK08130   1 MTEQALREEIVRLGRSLFQRGYTVGSAGNISARLDdGGWLVTPTGSCLGRLDPARLSKVDADGNWLSGDKPSKEVPLHRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  80 CYKARPELNAVIHTHAVNSTAVAI-----HNHSIPAIH-YMVAVSGtdHIPCIPYYTFGSPELADGVSKGIRESKSLLMQ 153
Cdd:PRK08130  81 IYRNNPECGAVVHLHSTHLTALSClggldPTNVLPPFTpYYVMRVG--HVPLIPYYRPGDPAIAEALAGLAARYRAVLLA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446361832 154 HHGMLAMDVTLEKTLWLAGETETLADLYIKCGGlhHDVPVLSEAEMTIVLEKFK 207
Cdd:PRK08130 159 NHGPVVWGSSLEAAVNATEELEETAKLILLLGG--RPPRYLTDEEIAELRSTFG 210
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 26-178 4.78e-28

L-ribulose-5-phosphate 4-epimerase; Validated


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 105.47  E-value: 4.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  26 TSGNVSARYTGG--MLITPSGIAYSKMTPDMIVFVDDKGKP-EAGKIPSSEWLIHLACYKARPELNAVIHTHAVNSTAVA 102
Cdd:PRK06557  31 TSGNVSARDPGTdlVVIKPSGVSYDDLTPEDMVVVDLDGNVvEGDLKPSSDTASHLYVYRHMPDVGGVVHTHSTYATAWA 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446361832 103 IHNHSIPAIHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKS--LLMQHHGMLAMDVTLEKTLWLAGETETLA 178
Cdd:PRK06557 111 ARGEPIPCVLTAMADEFGGPIPVGPFALIGDEAIGKGIVETLKGGRSpaVLMQNHGVFTIGKDAEDAVKAAVMVEEVA 188
PRK08333 PRK08333
aldolase;
9-181 2.71e-20

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 84.10  E-value: 2.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   9 KIISTCREMNASGLNQGTSGNVSARYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLACYKARPELN 88
Cdd:PRK08333   7 QLVKYSKLAHERGLTAAFGGNLSIRVGNLVFIKATGSVMDELTREQVAVIDLNGNQLSSVRPSSEYRLHLAVYRNRPDVR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  89 AVIHTHAVNS-TAVAIHNHSIPAIHYMVAVSgTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAMDVTLEKT 167
Cdd:PRK08333  87 AIAHLHPPYSiVASTLLEEELPIITPEAELY-LKKIPILPFRPAGSVELAEQVAEAMKEYDAVIMERHGIVTVGRSLREA 165

                        170
                 ....*....|....
gi 446361832 168 LWLAGETETLADLY 181
Cdd:PRK08333 166 FYKAELVEESAKLW 179
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 5-125 4.71e-20

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183460  Cd Length: 228  Bit Score: 84.47  E-value: 4.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   5 KLAEKIISTCREMNASGLNQGTSGNVSA--RYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKI-PSSEWLIHLACY 81
Cdd:PRK12348   3 KLKQQVFEANMDLPRYGLVTFTWGNVSAidRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYrPSSDTATHLELY 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446361832  82 KARPELNAVIHTHAVNSTAVAIHNHSIPAIhymvavsGTDH-------IPC 125
Cdd:PRK12348  83 RRYPSLGGIVHTHSTHATAWAQAGLAIPAL-------GTTHadyffgdIPC 126
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
26-130 2.15e-19

L-ribulose-5-phosphate 4-epimerase AraD;


Pssm-ID: 236181  Cd Length: 231  Bit Score: 82.57  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  26 TSGNVSA--RYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKI-PSSEWLIHLACYKARPELNAVIHTHAVNSTAVA 102
Cdd:PRK08193  25 TWGNVSAidRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLkPSSDTPTHLVLYKAFPEIGGIVHTHSRHATAWA 104

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446361832 103 IHNHSIPAIhymvavsGTDH-------IPCIPYYT 130
Cdd:PRK08193 105 QAGRDIPAL-------GTTHadyfygdIPCTRKMT 132
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
1-99 2.52e-19

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 81.91  E-value: 2.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   1 MERIKLAEKIISTCREMNASGLNQGTSGNVSARYTGG-MLITPSGIAYSKMTPDMIVFVDDKGKP-EAGKIPSSEWLIHL 78
Cdd:PRK09220   1 MTLEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQhCAITVSGKDKGSLTAEDFLQVDIAGNAvPSGRKPSAETLLHT 80

                         90       100
                 ....*....|....*....|.
gi 446361832  79 ACYKARPELNAVIHTHAVNST 99
Cdd:PRK09220  81 QLYRLFPEIGAVLHTHSVNAT 101
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 26-125 4.62e-14

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183459  Cd Length: 231  Bit Score: 68.31  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  26 TSGNVSA--RYTGGMLITPSGIAYSKMTPDMIVFVD-DKGKP-EAGKIPSSEWLIHLACYKARPELNAVIHTHAVNSTAV 101
Cdd:PRK12347  25 TWGNVSAvdETRQLMVIKPSGVEYDVMTADDMVVVEiASGKVvEGSKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIW 104

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446361832 102 AIHNHSIPAIhymvavsGTDH-------IPC 125
Cdd:PRK12347 105 SQAGLDLPAW-------GTTHadyfygaIPC 128
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 5-125 7.15e-14

L-ribulose-5-phosphate 4-epimerase; Provisional


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 67.94  E-value: 7.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   5 KLAEKIISTCREMNASGLNQGTSGNVSA--RYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKI-PSSEWLIHLACY 81
Cdd:PRK13145   5 EMRERVCAANKSLPKHGLVKFTWGNVSEvcRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLnPSSDLPTHVELY 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446361832  82 KARPELNAVIHTHAVNSTAVAIHNHSIPaihymvaVSGTDH-------IPC 125
Cdd:PRK13145  85 KAWPEVGGIVHTHSTEAVGWAQAGRDIP-------FYGTTHadyfygpIPC 128
PRK08660 PRK08660
aldolase;
19-165 9.72e-13

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 63.82  E-value: 9.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  19 ASGLNQGTSGNVSARYTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSEWLIHLACYKARPELnAVIHTHAVNS 98
Cdd:PRK08660  14 AHGLVSSHFGNISVRTGDGLLITRTGSMLDEITEGDVIEVGIDDDGSVDPLASSETPVHRAIYRRTSAK-AIVHAHPPYA 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446361832  99 TAVAIHNHSIPAI----HYMVavsgtDHIPCIPyYTFGSPELADGVSKGIRESKSLLMQHHGMLAMDVTLE 165
Cdd:PRK08660  93 VALSLLEDEIVPLdsegLYFL-----GTIPVVG-GDIGSGELAENVARALSEHKGVVVRGHGTFAIGKTLE 157
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
15-156 4.03e-10

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 56.98  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  15 REMNASGLNQGTSGNVSARYTGG---MLITPSGIAYSKMTPDMIVFVDDKGKP---EAGKiPSSEWLIHLACYKaRPELN 88
Cdd:PRK06754  16 KELAARDWFPATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDFLLVDHDGKPveeTELK-PSAETLLHTHIYN-NTNAG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  89 AVIHTHAVNST----------AVAIHNHS-IPAIHYMvAVSGTDHIPCIPYYtFGSPELADGVSKGIR-ESKSLLMQHHG 156
Cdd:PRK06754  94 CVLHVHTVDNNviselygddgAVTFQGQEiIKALGIW-EENAEIHIPIIENH-ADIPTLAEEFAKHIQgDSGAVLIRNHG 171
PRK06357 PRK06357
hypothetical protein; Provisional
 2-168 5.69e-10

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 56.71  E-value: 5.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   2 ERIKLAE--KIISTCREMNASGlnqgtsGNVSARYTGG-----MLITPSGIA---YSKMTPDMIVFVDdkgkPEAGKI-- 69
Cdd:PRK06357   6 EREDLAKvvKTMFDRKETNAAG------GNISVRMTAEknkeyIIMTPTLMSeakLCDLSPYQILVVD----LNTGEVie 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  70 ----PSSEWLIHLACYKARPELNAVIHTHAVNSTAVAIHNHSIPaiHYMVAVSGTDHIPCIPYYTFGSPELADGVSKGIR 145
Cdd:PRK06357  76 gvgrVTREINMHEAAYVANPKIKCVYHSHAKESMFWATLGLEMP--NLTEATQKLGKIPTLPFAPATSPELAEIVRKHLI 153

                        170       180
                 ....*....|....*....|....*....
gi 446361832 146 ESKSLLMQH------HGMLAMDVTLEKTL 168
Cdd:PRK06357 154 ELGDKAVPSafllnsHGIVITDTSLHKAY 182
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 6-171 1.58e-09

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 56.18  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   6 LAEKIISTCREMNASGLNQGTSGNVSARY-TGGMLIT-PSGIAYSKMTPDMIVFVDDKGKPEAGK-IPSSEWLIHLACYK 82
Cdd:PRK07090  31 LRQKLALTCRILFDAGHDSGLAGQITARAeAPGTYYTqRLGLGFDEITASNLLLVDEDLNVLDGEgMPNPANRFHSWIYR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  83 ARPELNAVIHTHAVNSTAVAIhnHSIPAIhymvaVSgtdHIPCIPYY---TF-----GSP---ELADGVSKGIRESKSLL 151
Cdd:PRK07090 111 ARPDVNCIIHTHPPHVAALSM--LEVPLV-----VS---HMDTCPLYddcAFlkdwpGVPvgnEEGEIISAALGDKRAIL 180

                        170       180
                 ....*....|....*....|
gi 446361832 152 MQHHGMLAMDVTLEKTLWLA 171
Cdd:PRK07090 181 LSHHGQLVAGKSIEEACVLA 200
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 26-125 1.07e-08

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 106181  Cd Length: 231  Bit Score: 53.58  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  26 TSGNVSA--RYTGGMLITPSGIAYSKMTPDMIVFVD-DKGKP-EAGKIPSSEWLIHLACYKARPELNAVIHTHAVNSTAV 101
Cdd:PRK13213  25 TWGNVSGidREHGLVVIKPSGVEYDVMSVNDMVVVDlATGKVvEGDKKPSSDTDTHLVLYRAFAEIGGIVHTHSRHATIW 104

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446361832 102 AIHNHSIPAIhymvavsGTDH-------IPC 125
Cdd:PRK13213 105 AQAGKSLSAL-------GTTHadyfygpIPC 128
PRK06208 PRK06208
class II aldolase/adducin family protein;
2-100 1.47e-08

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 53.45  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   2 ERIKLAEKIISTCREMNASGLNQGTSGNVSAR---YTGGMLITPSGIAYSKMTPDMIVFVDDKGKPEAGKIPSSE--WLI 76
Cdd:PRK06208  39 ERLHRKQRLAAAFRLFARFGFDEGLAGHITARdpeLPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDRPLNRaaFAI 118

                         90       100
                 ....*....|....*....|....
gi 446361832  77 HLACYKARPELNAVIHTHAVNSTA 100
Cdd:PRK06208 119 HSAIHEARPDVVAAAHTHSTYGKA 142
PRK06486 PRK06486
aldolase;
3-103 3.39e-07

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 49.32  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832   3 RIKLAekiisTCREMNAS-GLNQGTSGNVSARYTGG---MLITPSGIAYSKMTPDMIVFVDDKGKPEAG--KIPSSEWLI 76
Cdd:PRK06486  28 RVDLA-----ACFRAAARhGLEEGICNHFSAVLPGHddlFLVNPYGYAFSEITASDLLICDFDGNVLAGrgEPEATAFFI 102

                         90       100
                 ....*....|....*....|....*..
gi 446361832  77 HLACYKARPELNAVIHTHAVNSTAVAI 103
Cdd:PRK06486 103 HARIHRAIPRAKAAFHTHMPYATALSL 129
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 30-102 1.58e-06

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 47.15  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  30 VSARYTGG---MLITPSGIAYSKMTPDMIVFVDDKGKpeagKIPSSEW-------LIHLACYKARPELNAVIHTHAVNST 99
Cdd:PRK07044  41 ISARVPGEehhFLINPYGLLFDEITASNLVKIDLDGN----VVDDSPYpvnpagfTIHSAIHAARPDAHCVMHTHTTAGV 116


                 ...
gi 446361832 100 AVA 102
Cdd:PRK07044 117 AVS 119
PRK03634 PRK03634
rhamnulose-1-phosphate aldolase; Provisional
 55-206 1.07e-05

rhamnulose-1-phosphate aldolase; Provisional


Pssm-ID: 179615 [Multi-domain]  Cd Length: 274  Bit Score: 44.98  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  55 IVFVDDKGKP-------EAGKIPSSEWLIHLACYKAR-----PELNAVIHTHAVNSTAVAiHNHSIPA---------IHY 113
Cdd:PRK03634  92 VIRIDSDGAGyhilwglTNGGKPTSELPAHLMSHIARlkatnGKDRVIMHCHATNLIALT-YVLELDEavftrtlweMST 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832 114 MVAVSGTDHIPCIPYYTFGSPELADGVSKGIRESKSLLMQHHGMLAMDVTLEKTLwlaGETETL---ADLYIKCGGLHHD 190
Cdd:PRK03634 171 ECLVVFPDGVGIVPWMVPGTDEIGQATAEKMQKHDLVLWPKHGVFGSGPTLDEAF---GLIDTAeksAEIYVKVLSMGGM 247

                        170
                 ....*....|....*.
gi 446361832 191 VPVLSEAEMTIVLEKF 206
Cdd:PRK03634 248 KQTITDEELIALGERF 263
PRK06661 PRK06661
hypothetical protein; Provisional
 21-169 3.72e-05

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 43.28  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  21 GLNQGTSGNVSARYTGG--MLITPSGIAYSKMTPDMIVFVDDKGKPEAGK---IPSSEWLIHLACYKARPELNAVIHTHA 95
Cdd:PRK06661  18 SLDDHTYTHLSARPKNAdfYYIYPFGLRFEEVTTENLLKVSLDGQILEGEeyqYNKTGYFIHGSIYKTRPDISAIFHYHT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446361832  96 VNSTAV-AIHNHSIP----AIHYMVAVSgtdhipcipYYTFGSPELaDGVSKGIR------ESKSLLMQHHGMLAMDVTL 164
Cdd:PRK06661  98 PASIAVsALKCGLLPisqwALHFYDRIS---------YHNYNSLAL-DADKQSSRlvndlkQNYVMLLRNHGAITCGKTI 167


                 ....*
gi 446361832 165 EKTLW 169
Cdd:PRK06661 168 HEAMF 172
PRK07490 PRK07490
hypothetical protein; Provisional
 39-111 3.62e-03

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 37.39  E-value: 3.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446361832  39 LITPSGIAYSKMTPDMIVFVD--DKGKPEAGKIP-SSEWLIHLACYKARPELNAVIHTHAVNSTAVA-IHNHSIPAI 111
Cdd:PRK07490  47 LLNPKWKHFSRIRASDLLLLDadDPSTAERPDVPdATAWAIHGQIHRRLPHARCVMHVHSVYATALAcLADPTLPPI 123
 
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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