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Conserved domains on  [gi|514062314|ref|WP_016528625|]
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L-fuculose-phosphate aldolase [Glaesserella parasuis]

Protein Classification

L-fuculose-phosphate aldolase( domain architecture ID 10012997)

L-fuculose-phosphate aldolase catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde; Also able to catalyze the reversible cleavage of D-ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1-phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
1-215 4.71e-166

L-fuculose-phosphate aldolase;


:

Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 455.74  E-value: 4.71e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   1 MNRQTLARKIIDTCLEMTRLGLNQGTAGNISVRYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAV 80
Cdd:PRK08087   1 MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLPSSEWRFHMAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  81 YQTRPELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAA 160
Cdd:PRK08087  81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 514062314 161 EVNLEKALWVAHEVEVLAQWYLKLLATTPDVPVLSDEEIKVVLGKFSTYGLRVEE 215
Cdd:PRK08087 161 EVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE 215
 
Name Accession Description Interval E-value
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
1-215 4.71e-166

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 455.74  E-value: 4.71e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   1 MNRQTLARKIIDTCLEMTRLGLNQGTAGNISVRYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAV 80
Cdd:PRK08087   1 MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLPSSEWRFHMAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  81 YQTRPELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAA 160
Cdd:PRK08087  81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 514062314 161 EVNLEKALWVAHEVEVLAQWYLKLLATTPDVPVLSDEEIKVVLGKFSTYGLRVEE 215
Cdd:PRK08087 161 EVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE 215
fucA TIGR01086
L-fuculose phosphate aldolase; Members of this family are L-fuculose phosphate aldolase from ...
 2-215 7.37e-146

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: 404.71  E-value: 7.37e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314    2 NRQTLARKIIDTCLEMTRLGLNQGTAGNISVRYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAVY 81
Cdd:TIGR01086   1 NRAELSQQIIDTCLEMTRLGLNQGTAGNVSVRYKDGMLITPTGIPYEKLTTEHIVYVDGNGKHEEGKLPSSEWQFHLSVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   82 QTRPELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAAE 161
Cdd:TIGR01086  81 QTRPDANAVVHNHAIHCAAVSILNKSIPAIHYMVAASGTDHIPCVPYATFGSHKLASYVATGIKESKAILLQHHGLIACE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 514062314  162 VNLEKALWVAHEVEVLAQWYLKLLATTPDVPVLSDEEIKVVLGKFSTYGLRVEE 215
Cdd:TIGR01086 161 VNLEKALWLAHEVEVLASLYLKTLAITLEVPVLSKEQMAVVLGKFKTYGLRIEE 214
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 6-206 1.02e-83

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: 247.28  E-value: 1.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   6 LARKIIDTCLEMTRLGLNQGTAGNISVRYQD--GMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAVYQT 83
Cdd:cd00398    3 LKRKIIAACLLLDLYGWVTGTGGNVSARDRDrgYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKKPSSETPLHLALYRA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  84 RPELNAVVHNHAINCTGVSILNK-DIPAIHYMIAVTGTNHVPCVPYATF--GTWQLAEYVKQGIAKSKAILLQHHGMIAA 160
Cdd:cd00398   83 RPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPetGEDEIGTQRALGFPNSKAVLLRNHGLFAW 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 514062314 161 EVNLEKALWVAHEVEVLAQWYLKLLATTPDVPVLSDEEIKVVLGKF 206
Cdd:cd00398  163 GPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRK 208
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-207 6.65e-74

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: 222.40  E-value: 6.65e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   1 MNRQTLARKIIDTCLEMTRLGLNQGTAGNISVRYQDG-MLITPSGMPYEKMTEDDIVYVDNEGNFEAGKL-PSSEWQFHL 78
Cdd:COG0235    1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLkPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  79 AVYQTRPELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMI 158
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGVV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514062314 159 AAEVNLEKALWVAHEVEVLAQWYLKLLATTPdVPVLSDEEIKVVLGKFS 207
Cdd:COG0235  161 VWGKDLAEAFDRAEVLEEAARIQLLALALGG-PLVLSDEEIDKLARKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-182 8.83e-64

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: 195.46  E-value: 8.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314    8 RKIIDTCLEMTRLGLNQGTAGNISVR-YQDGMLITPSGMPYEKMTEDDIVYVDNEGN-FEAGKLPSSEWQFHLAVYQTRP 85
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNvVEGGLKPSSETPLHLAIYRARP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   86 ELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGI-AKSKAILLQHHGMIAAEVNL 164
Cdd:pfam00596  81 DAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEELGERIAEALgGDRKAVLLRNHGLLVWGKTL 160

                         170
                  ....*....|....*...
gi 514062314  165 EKALWVAHEVEVLAQWYL 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 3.43e-55

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: 173.98  E-value: 3.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314    10 IIDTCLEMTRLGLNQGTAGNISVR--YQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKL---PSSEWQFHLAVYQTR 84
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARvgEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpkPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314    85 PELNAVVHNHAINCTGVSILNKDIPAIHYMIAV-TGTNHVPCVPYATFGTWQ------LAEYVKQGIAKSKAILLQHHGM 157
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAaFLGGEIPYAPYAGPGTELaeegaeLAEALAEALPDRPAVLLRNHGL 160

                          170       180
                   ....*....|....*....|....*
gi 514062314   158 IAAEVNLEKALWVAHEVEVLAQWYL 182
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
 
Name Accession Description Interval E-value
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
1-215 4.71e-166

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 455.74  E-value: 4.71e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   1 MNRQTLARKIIDTCLEMTRLGLNQGTAGNISVRYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAV 80
Cdd:PRK08087   1 MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLPSSEWRFHMAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  81 YQTRPELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAA 160
Cdd:PRK08087  81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 514062314 161 EVNLEKALWVAHEVEVLAQWYLKLLATTPDVPVLSDEEIKVVLGKFSTYGLRVEE 215
Cdd:PRK08087 161 EVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE 215
fucA TIGR01086
L-fuculose phosphate aldolase; Members of this family are L-fuculose phosphate aldolase from ...
 2-215 7.37e-146

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: 404.71  E-value: 7.37e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314    2 NRQTLARKIIDTCLEMTRLGLNQGTAGNISVRYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAVY 81
Cdd:TIGR01086   1 NRAELSQQIIDTCLEMTRLGLNQGTAGNVSVRYKDGMLITPTGIPYEKLTTEHIVYVDGNGKHEEGKLPSSEWQFHLSVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   82 QTRPELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAAE 161
Cdd:TIGR01086  81 QTRPDANAVVHNHAIHCAAVSILNKSIPAIHYMVAASGTDHIPCVPYATFGSHKLASYVATGIKESKAILLQHHGLIACE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 514062314  162 VNLEKALWVAHEVEVLAQWYLKLLATTPDVPVLSDEEIKVVLGKFSTYGLRVEE 215
Cdd:TIGR01086 161 VNLEKALWLAHEVEVLASLYLKTLAITLEVPVLSKEQMAVVLGKFKTYGLRIEE 214
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 6-206 1.02e-83

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: 247.28  E-value: 1.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   6 LARKIIDTCLEMTRLGLNQGTAGNISVRYQD--GMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAVYQT 83
Cdd:cd00398    3 LKRKIIAACLLLDLYGWVTGTGGNVSARDRDrgYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKKPSSETPLHLALYRA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  84 RPELNAVVHNHAINCTGVSILNK-DIPAIHYMIAVTGTNHVPCVPYATF--GTWQLAEYVKQGIAKSKAILLQHHGMIAA 160
Cdd:cd00398   83 RPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPetGEDEIGTQRALGFPNSKAVLLRNHGLFAW 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 514062314 161 EVNLEKALWVAHEVEVLAQWYLKLLATTPDVPVLSDEEIKVVLGKF 206
Cdd:cd00398  163 GPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRK 208
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-207 6.65e-74

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: 222.40  E-value: 6.65e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   1 MNRQTLARKIIDTCLEMTRLGLNQGTAGNISVRYQDG-MLITPSGMPYEKMTEDDIVYVDNEGNFEAGKL-PSSEWQFHL 78
Cdd:COG0235    1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLkPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  79 AVYQTRPELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMI 158
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGVV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514062314 159 AAEVNLEKALWVAHEVEVLAQWYLKLLATTPdVPVLSDEEIKVVLGKFS 207
Cdd:COG0235  161 VWGKDLAEAFDRAEVLEEAARIQLLALALGG-PLVLSDEEIDKLARKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-182 8.83e-64

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: 195.46  E-value: 8.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314    8 RKIIDTCLEMTRLGLNQGTAGNISVR-YQDGMLITPSGMPYEKMTEDDIVYVDNEGN-FEAGKLPSSEWQFHLAVYQTRP 85
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNvVEGGLKPSSETPLHLAIYRARP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   86 ELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGI-AKSKAILLQHHGMIAAEVNL 164
Cdd:pfam00596  81 DAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEELGERIAEALgGDRKAVLLRNHGLLVWGKTL 160

                         170
                  ....*....|....*...
gi 514062314  165 EKALWVAHEVEVLAQWYL 182
Cdd:pfam00596 161 EEAFYLAEELERAAEIQL 178
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
8-212 6.65e-59

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 184.57  E-value: 6.65e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   8 RKIIDTclemtrlGLNQGTAGNISV--RYQDGMLITPSGMPYEKMTEDDIVYVDNEGNF-EAGKLPSSEWQFHLAVYQTR 84
Cdd:PRK06833  15 KKLISS-------GLTKGTGGNISIfnREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVvEGERKPSSELDMHLIFYRNR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  85 PELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNhVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAAEVNL 164
Cdd:PRK06833  88 EDINAIVHTHSPYATTLACLGWELPAVHYLIAVAGPN-VRCAEYATFGTKELAENAFEAMEDRRAVLLANHGLLAGANNL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 514062314 165 EKALWVAHEVEVLAQWYLKllATTPDVPV-LSDEEIKVVLGKFSTYGLR 212
Cdd:PRK06833 167 KNAFNIAEEIEFCAEIYYQ--TKSIGEPKlLPEDEMENMAEKFKTYGQR 213
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-182 3.43e-55

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: 173.98  E-value: 3.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314    10 IIDTCLEMTRLGLNQGTAGNISVR--YQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKL---PSSEWQFHLAVYQTR 84
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARvgEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpkPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314    85 PELNAVVHNHAINCTGVSILNKDIPAIHYMIAV-TGTNHVPCVPYATFGTWQ------LAEYVKQGIAKSKAILLQHHGM 157
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAaFLGGEIPYAPYAGPGTELaeegaeLAEALAEALPDRPAVLLRNHGL 160

                          170       180
                   ....*....|....*....|....*
gi 514062314   158 IAAEVNLEKALWVAHEVEVLAQWYL 182
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
PRK08130 PRK08130
putative aldolase; Validated
 16-206 1.79e-31

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 114.20  E-value: 1.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  16 EMTRL-------GLNQGTAGNISVRYQD-GMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAVYQTRPEL 87
Cdd:PRK08130   9 EIVRLgrslfqrGYTVGSAGNISARLDDgGWLVTPTGSCLGRLDPARLSKVDADGNWLSGDKPSKEVPLHRAIYRNNPEC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  88 NAVVHNHAINCTGVSIL-NKD----IPAI--HYMIAVtgtNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAA 160
Cdd:PRK08130  89 GAVVHLHSTHLTALSCLgGLDptnvLPPFtpYYVMRV---GHVPLIPYYRPGDPAIAEALAGLAARYRAVLLANHGPVVW 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 514062314 161 EVNLEKALWVAHEVEVLAqwylKLLATTPDVPV--LSDEEIKVVLGKF 206
Cdd:PRK08130 166 GSSLEAAVNATEELEETA----KLILLLGGRPPryLTDEEIAELRSTF 209
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 10-196 7.28e-31

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 112.81  E-value: 7.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  10 IIDTCLEMTRLGLNQGTAGNISVRYQDG-MLITPSGMPYEKMTEDDIVYVDNEGNF---EAGKLPSSEWQFHLAVYQTRP 85
Cdd:PRK05874  11 VLAAAKDMLRRGLVEGTAGNISARRSDGnVVITPSSVDYAEMLLHDLVLVDAGGAVlhaKDGRSPSTELNLHLACYRAFD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  86 ELNAVVHNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAAEVNLE 165
Cdd:PRK05874  91 DIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCTEYAASGTPEVGRNAVRALEGRAAALIANHGLVAVGPRPD 170

                        170       180       190
                 ....*....|....*....|....*....|.
gi 514062314 166 KALWVAHEVEVLAQWYLKLLATTPDVPVLSD 196
Cdd:PRK05874 171 QVLRVTALVERTAQIVWGARALGGPVPIPED 201
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 15-200 3.00e-29

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 108.56  E-value: 3.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  15 LEMTRLGLNQGTAGNISVRYQDG--MLITPSGMPYEKMTEDDIVYVDNEGNFEAGKL-PSSEWQFHLAVYQTRPELNAVV 91
Cdd:PRK06557  20 LELPKYGLVVWTSGNVSARDPGTdlVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLkPSSDTASHLYVYRHMPDVGGVV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  92 HNHAINCTGVSILNKDIPAIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIA--KSKAILLQHHGMIAAEVNLEKALW 169
Cdd:PRK06557 100 HTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGPFALIGDEAIGKGIVETLKggRSPAVLMQNHGVFTIGKDAEDAVK 179

                        170       180       190
                 ....*....|....*....|....*....|...
gi 514062314 170 VAHEVEVLAQ--WYLKLLAttpDVPVLSDEEIK 200
Cdd:PRK06557 180 AAVMVEEVARtvHIARQLG---EPIPIPQEEID 209
PRK08333 PRK08333
aldolase;
21-183 1.32e-26

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 100.67  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  21 GLNQGTAGNISVRYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAVYQTRPELNAVVHNH-AINCT 99
Cdd:PRK08333  19 GLTAAFGGNLSIRVGNLVFIKATGSVMDELTREQVAVIDLNGNQLSSVRPSSEYRLHLAVYRNRPDVRAIAHLHpPYSIV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314 100 GVSILNKDIPAIH-----YMiavtgtNHVPCVPYATFGTWQLAEYVKQGIAKSKAILLQHHGMIAAEVNLEKALWVAHEV 174
Cdd:PRK08333  99 ASTLLEEELPIITpeaelYL------KKIPILPFRPAGSVELAEQVAEAMKEYDAVIMERHGIVTVGRSLREAFYKAELV 172

                        170
                 ....*....|
gi 514062314 175 EVLAQ-WYLK 183
Cdd:PRK08333 173 EESAKlWYLK 182
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 4-125 6.26e-20

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 84.47  E-value: 6.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   4 QTLARKIIDTCLEMTRLGLNQGTAGNISV--RYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKL-PSSEWQFHLAV 80
Cdd:PRK12348   2 QKLKQQVFEANMDLPRYGLVTFTWGNVSAidRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYrPSSDTATHLEL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514062314  81 YQTRPELNAVVHNHAINCTGVSILNKDIPAIhymiavtGTNH-------VPC 125
Cdd:PRK12348  82 YRRYPSLGGIVHTHSTHATAWAQAGLAIPAL-------GTTHadyffgdIPC 126
PRK08660 PRK08660
aldolase;
21-175 5.34e-19

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 80.77  E-value: 5.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  21 GLNQGTAGNISVRYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQFHLAVYQTRPELnAVVHNHAINCTG 100
Cdd:PRK08660  16 GLVSSHFGNISVRTGDGLLITRTGSMLDEITEGDVIEVGIDDDGSVDPLASSETPVHRAIYRRTSAK-AIVHAHPPYAVA 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514062314 101 VSILNKDIPAI----HYMIAvtgtnHVPCVPyATFGTWQLAEYVKQGIAKSKAILLQHHGMIAAEVNLEKALWVAHEVE 175
Cdd:PRK08660  95 LSLLEDEIVPLdsegLYFLG-----TIPVVG-GDIGSGELAENVARALSEHKGVVVRGHGTFAIGKTLEEAYIYTSQLE 167
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
4-130 1.18e-18

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 81.03  E-value: 1.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   4 QTLARKIIDTCLEMTRLGLNQGTAGNISV--RYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKL-PSSEWQFHLAV 80
Cdd:PRK08193   3 EDLKQEVLEANLALPKHGLVTFTWGNVSAidRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLkPSSDTPTHLVL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 514062314  81 YQTRPELNAVVHNHAINCTGVSILNKDIPAIhymiavtGTNH-------VPCVPYAT 130
Cdd:PRK08193  83 YKAFPEIGGIVHTHSRHATAWAQAGRDIPAL-------GTTHadyfygdIPCTRKMT 132
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
1-106 1.31e-18

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 80.37  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   1 MNRQTLARKIIDTCLEMTRLGLNQGTAGNISVRYQDG-MLITPSGMPYEKMTEDDIVYVDNEGN-FEAGKLPSSEWQFHL 78
Cdd:PRK09220   1 MTLEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQhCAITVSGKDKGSLTAEDFLQVDIAGNaVPSGRKPSAETLLHT 80

                         90       100
                 ....*....|....*....|....*...
gi 514062314  79 AVYQTRPELNAVVHNHAINCTGVSILNK 106
Cdd:PRK09220  81 QLYRLFPEIGAVLHTHSVNATVLSRVEK 108
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 2-186 2.48e-14

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 69.66  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   2 NRQTLARKIIDTCLEMTRLGLNQGTAGNISVRY-QDGMLIT-PSGMPYEKMTEDDIVYVDNEGNFEAGK-LPSSEWQFHL 78
Cdd:PRK07090  27 SGWTLRQKLALTCRILFDAGHDSGLAGQITARAeAPGTYYTqRLGLGFDEITASNLLLVDEDLNVLDGEgMPNPANRFHS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  79 AVYQTRPELNAVVHNHAINCTGVSILnkDIP-AIHYMIAvtgtnhvpCVPY---ATFGTW-------QLAEYVKQGIAKS 147
Cdd:PRK07090 107 WIYRARPDVNCIIHTHPPHVAALSML--EVPlVVSHMDT--------CPLYddcAFLKDWpgvpvgnEEGEIISAALGDK 176

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 514062314 148 KAILLQHHGMIAAEVNLEKALWVAHEVEVLAQwyLKLLA 186
Cdd:PRK07090 177 RAILLSHHGQLVAGKSIEEACVLALLIERAAR--LQLLA 213
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 4-125 3.70e-14

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 68.69  E-value: 3.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   4 QTLARKIIDTCLEMTRLGLNQGTAGNISV--RYQDGMLITPSGMPYEKMTEDDIVYVD-NEGN-FEAGKLPSSEWQFHLA 79
Cdd:PRK12347   3 EQLKADVLAANLALPAHHLVTFTWGNVSAvdETRQLMVIKPSGVEYDVMTADDMVVVEiASGKvVEGSKKPSSDTPTHLA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 514062314  80 VYQTRPELNAVVHNHAINCTGVSILNKDIPAIhymiavtGTNH-------VPC 125
Cdd:PRK12347  83 LYRRYPEIGGIVHTHSRHATIWSQAGLDLPAW-------GTTHadyfygaIPC 128
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-126 7.75e-14

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 67.94  E-value: 7.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   1 MNRQTLARKIIDTCLEMTRLGLNQGTAGNISV--RYQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKL-PSSEWQFH 77
Cdd:PRK13145   1 KNLQEMRERVCAANKSLPKHGLVKFTWGNVSEvcRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLnPSSDLPTH 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 514062314  78 LAVYQTRPELNAVVHNHAINCTGVSILNKDIPaihymiaVTGTNH-------VPCV 126
Cdd:PRK13145  81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIP-------FYGTTHadyfygpIPCA 129
PRK06208 PRK06208
class II aldolase/adducin family protein;
19-199 3.65e-13

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 66.55  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  19 RLGLNQGTAGNISVR---YQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAGKLPSSEWQF--HLAVYQTRPELNAVVHN 93
Cdd:PRK06208  56 RFGFDEGLAGHITARdpeLPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDRPLNRAAFaiHSAIHEARPDVVAAAHT 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  94 HAINCTGVSILNKDIPAIHYMIAVTGTNHvpcVPYATFGTWQLAEYVKQGIAKS----KAILLQHHGMiaaevnlekaLW 169
Cdd:PRK06208 136 HSTYGKAWSTLGRPLDPITQDACAFYEDH---ALFDDFTGVVVDTSEGRRIAAAlgthKAVILQNHGL----------LT 202

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 514062314 170 VAHEVEVLAQWYL--------KLLATTPDVPVLSDEEI 199
Cdd:PRK06208 203 VGPSVDAAAWWFIaleracqtQLLAEAAGPPQPIDHET 240
PRK06661 PRK06661
hypothetical protein; Provisional
 17-199 4.20e-11

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 60.23  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  17 MTRLGLNQGTAGNISVRYQDG--MLITPSGMPYEKMTEDDIVYVDNEGNFEAGKlpssEWQF-------HLAVYQTRPEL 87
Cdd:PRK06661  14 MAYLSLDDHTYTHLSARPKNAdfYYIYPFGLRFEEVTTENLLKVSLDGQILEGE----EYQYnktgyfiHGSIYKTRPDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  88 NAVVHNHAINCTGVSILnKD--IP----AIHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQgiakSKAILLQHHGMIAAE 161
Cdd:PRK06661  90 SAIFHYHTPASIAVSAL-KCglLPisqwALHFYDRISYHNYNSLALDADKQSSRLVNDLKQ----NYVMLLRNHGAITCG 164

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 514062314 162 VNLEKALWVAHEVEVLAQWYLKLLATTPDVPVLSDEEI 199
Cdd:PRK06661 165 KTIHEAMFYTYHLEQACKTQCLLNSTKKQELIIPSVEI 202
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
25-192 6.82e-11

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 59.29  E-value: 6.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  25 GTAGNISVRYQDG---MLITPSGMPYEKMTEDDIVYVDNEGN-FEAGKL-PSSEWQFHLAVYQtRPELNAVVHNHAINCT 99
Cdd:PRK06754  26 ATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDFLLVDHDGKpVEETELkPSAETLLHTHIYN-NTNAGCVLHVHTVDNN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314 100 GVSILNKDIPAIHY----MIAVTG------TNHVPCVP-YATFGTwqLAEYVKQGI-AKSKAILLQHHGMIAAEVNLEKA 167
Cdd:PRK06754 105 VISELYGDDGAVTFqgqeIIKALGiweenaEIHIPIIEnHADIPT--LAEEFAKHIqGDSGAVLIRNHGITVWGRDAFEA 182

                        170       180
                 ....*....|....*....|....*
gi 514062314 168 LWVAHEVEVLAQWYLKLLATTPDVP 192
Cdd:PRK06754 183 KKHLEAYEFLFSYHIKLLSIQGGVS 207
PRK06357 PRK06357
hypothetical protein; Provisional
 28-175 8.20e-11

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 59.40  E-value: 8.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  28 GNISVRYQDG-----MLITPSGMP---YEKMTEDDIVYVD-NEGNFEAG--KLpSSEWQFHLAVYQTRPELNAVVHNHAI 96
Cdd:PRK06357  28 GNISVRMTAEknkeyIIMTPTLMSeakLCDLSPYQILVVDlNTGEVIEGvgRV-TREINMHEAAYVANPKIKCVYHSHAK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  97 NCTGVSILNKDIPaiHYMIAVTGTNHVPCVPYATFGTWQLAEYVKQGIAKSK------AILLQHHGMIAAEVNLEKALWV 170
Cdd:PRK06357 107 ESMFWATLGLEMP--NLTEATQKLGKIPTLPFAPATSPELAEIVRKHLIELGdkavpsAFLLNSHGIVITDTSLHKAYDI 184


                 ....*
gi 514062314 171 AHEVE 175
Cdd:PRK06357 185 LETIE 189
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 4-191 1.28e-09

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 56.27  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   4 QTLARKIIDTCLEMTRLGLNQGTAGNIS-VRYQDGML-ITPSGMPYEKMTEDDIVYVDNEGN--FEAGKLPSSEWQFHLA 79
Cdd:PRK13213   3 EQLKQQVFEANLALPKYKLVTFTWGNVSgIDREHGLVvIKPSGVEYDVMSVNDMVVVDLATGkvVEGDKKPSSDTDTHLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  80 VYQTRPELNAVVHNHAINCTGVSILNKDIPAIhymiavtGTNH-------VPCVPYAT-----------FGTWQLAEYVK 141
Cdd:PRK13213  83 LYRAFAEIGGIVHTHSRHATIWAQAGKSLSAL-------GTTHadyfygpIPCTRLMTeaeitgdyeheTGKVIVETFAE 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514062314 142 QGI--AKSKAILLQHHGMIAAEVNLEKALWVAHEVEVLAQWYLKLLATTPDV 191
Cdd:PRK13213 156 QGLraADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGV 207
PRK06486 PRK06486
aldolase;
7-104 4.74e-06

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 45.86  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314   7 ARKIIDTCLEM-TRLGLNQGTAGNISVR---YQDGMLITPSGMPYEKMTEDDIVYVDNEGNFEAG--KLPSSEWQFHLAV 80
Cdd:PRK06486  27 ARVDLAACFRAaARHGLEEGICNHFSAVlpgHDDLFLVNPYGYAFSEITASDLLICDFDGNVLAGrgEPEATAFFIHARI 106

                         90       100
                 ....*....|....*....|....
gi 514062314  81 YQTRPELNAVVHNHAINCTGVSIL 104
Cdd:PRK06486 107 HRAIPRAKAAFHTHMPYATALSLT 130
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 30-102 1.18e-04

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 41.76  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062314  30 ISVRYQDG---MLITPSGMPYEKMTEDDIVYVDNEGNfeagKLPSSEWQ-------FHLAVYQTRPELNAVVHNHAINCT 99
Cdd:PRK07044  41 ISARVPGEehhFLINPYGLLFDEITASNLVKIDLDGN----VVDDSPYPvnpagftIHSAIHAARPDAHCVMHTHTTAGV 116


                 ...
gi 514062314 100 GVS 102
Cdd:PRK07044 117 AVS 119
 
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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