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Conserved domains on  [gi|446849302|ref|WP_000926558|]
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MULTISPECIES: L-fuculose-phosphate aldolase [Bacillus]

Protein Classification

class II aldolase/adducin head domain-containing protein; L-fuculose-phosphate aldolase( domain architecture ID 10012826)

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| 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
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-213 5.46e-144

L-fuculose-phosphate aldolase;


:

Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 399.89  E-value: 5.46e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   1 MLLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMH 80
Cdd:PRK06833   1 MLLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  81 LIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIAFAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGLI 160
Cdd:PRK06833  81 LIFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIAVAGPNVRCAEYATFGTKELAENAFEAMEDRRAVLLANHGLL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446849302 161 AGANNIKMAFTVAEEIEFCAQIYYQTKSVGEPKLLPEDEMENLAKKFEGYGQQ 213
Cdd:PRK06833 161 AGANNLKNAFNIAEEIEFCAEIYYQTKSIGEPKLLPEDEMENMAEKFKTYGQR 213
 
Name Accession Description Interval E-value
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-213 5.46e-144

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 399.89  E-value: 5.46e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   1 MLLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMH 80
Cdd:PRK06833   1 MLLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  81 LIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIAFAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGLI 160
Cdd:PRK06833  81 LIFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIAVAGPNVRCAEYATFGTKELAENAFEAMEDRRAVLLANHGLL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446849302 161 AGANNIKMAFTVAEEIEFCAQIYYQTKSVGEPKLLPEDEMENLAKKFEGYGQQ 213
Cdd:PRK06833 161 AGANNLKNAFNIAEEIEFCAEIYYQTKSIGEPKLLPEDEMENMAEKFKTYGQR 213
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-208 4.80e-79

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: 235.11  E-value: 4.80e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   1 MLLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREqGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMH 80
Cdd:COG0235    1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  81 LIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIA-FAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGL 159
Cdd:COG0235   80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAaAFLGDVPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446849302 160 IAGANNIKMAFTVAEEIEFCAQIYYQTKSVGEPKLLPEDEMENLAKKFE 208
Cdd:COG0235  160 VVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLVLSDEEIDKLARKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-184 1.44e-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: 197.38  E-value: 1.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302    8 EEIVAYGKKMISSGLTKGTGGNISIFnREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLIYYRKR 87
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVR-LPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   88 EDINALVHTHSPYAKTIASLGWELPAVSYLIA-FAGPNVRCAPYETFGTKQLAEAAFEGMI-DRRAVLLANHGLIAGANN 165
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAAdFLGGDIPIIPYYTPGTEELGERIAEALGgDRKAVLLRNHGLLVWGKT 159

                         170
                  ....*....|....*....
gi 446849302  166 IKMAFTVAEEIEFCAQIYY 184
Cdd:pfam00596 160 LEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-184 3.01e-57

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: 178.99  E-value: 3.01e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302    10 IVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGE--RKPSSELDMHLIYYRKR 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGggPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302    88 EDINALVHTHSPYAKTIASLGWELPAV--SYLIAFAGPNVRCAPYETFGT------KQLAEAAFEGMIDRRAVLLANHGL 159
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLptEQAAAFLGGEIPYAPYAGPGTelaeegAELAEALAEALPDRPAVLLRNHGL 160

                          170       180
                   ....*....|....*....|....*
gi 446849302   160 IAGANNIKMAFTVAEEIEFCAQIYY 184
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 9-207 1.03e-47

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: 155.60  E-value: 1.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   9 EIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGErKPSSELDMHLIYYRKRE 88
Cdd:cd00398    6 KIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGK-KPSSETPLHLALYRARP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  89 DINALVHTHSPYAKTIASLGWE-LPAVSYLIAFAGPN-VRCAPYETF--GTKQLAEAAFEGMIDRRAVLLANHGLIAGAN 164
Cdd:cd00398   85 DIGCIVHTHSTHATAVSQLKEGlIPAGHTACAVYFTGdIPCTPYMTPetGEDEIGTQRALGFPNSKAVLLRNHGLFAWGP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446849302 165 NIKMAFTVAEEIEFCAQIYYQTKSVGEPK-LLPEDEMENLAKKF 207
Cdd:cd00398  165 TLDEAFHLAVVLEVAAEIQLKALSMGGQLpPISLELLNKEYLRK 208
FucA_Meth NF040649
L-fuculose phosphate aldolase;
25-184 6.45e-26

L-fuculose phosphate aldolase;


Pssm-ID: 468616  Cd Length: 179  Bit Score: 98.65  E-value: 6.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  25 GTGGNISIfnREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGerKPSSELDMHLIYYRKREDINALVHTHSPYAKTI 104
Cdd:NF040649  21 GSGGNVSI--REDDLIYITPTGSILGFLKEEDIAIVDLDGNIIKG--KPTSELNMHLKIYRKRKDINAIIHTHSLYSTAL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302 105 ASLGWELPAVSYLIAFAGPNVRCAPYETFGTKQLAEAAFEGmiDRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYY 184
Cdd:NF040649  97 SILDKKIELLTPEAKIFLKKIGYVDYLEAGSLELAEEVSKR--DEDVIILKNHGIVCLGKDLIEAYIKTEVLEEIAKLNL 174
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 10-189 4.09e-24

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 94.25  E-value: 4.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   10 IVAYGKKMISSGLTKGTGGNISIFNREQGLVaISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLIYYRKReD 89
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLDEDEIL-ITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-G 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   90 INALVHTHSPYAkTIASLGW------ELPAVSYLIAFAG-------------PNvrcapyeTFGTKQLAEA---AFEGMI 147
Cdd:TIGR03328  79 AGAVLHTHSVEA-TVLSRLYpsnggfELEGYEMLKGLPGitthedtlvvpiiEN-------TQDIARLADSvapALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446849302  148 DRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYYQTKSV 189
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
 
Name Accession Description Interval E-value
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-213 5.46e-144

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 399.89  E-value: 5.46e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   1 MLLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMH 80
Cdd:PRK06833   1 MLLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  81 LIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIAFAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGLI 160
Cdd:PRK06833  81 LIFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIAVAGPNVRCAEYATFGTKELAENAFEAMEDRRAVLLANHGLL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446849302 161 AGANNIKMAFTVAEEIEFCAQIYYQTKSVGEPKLLPEDEMENLAKKFEGYGQQ 213
Cdd:PRK06833 161 AGANNLKNAFNIAEEIEFCAEIYYQTKSIGEPKLLPEDEMENMAEKFKTYGQR 213
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-208 4.80e-79

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: 235.11  E-value: 4.80e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   1 MLLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREqGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMH 80
Cdd:COG0235    1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  81 LIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIA-FAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGL 159
Cdd:COG0235   80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAaAFLGDVPVVPYAGPGTEELAEAIAEALGDRPAVLLRNHGV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446849302 160 IAGANNIKMAFTVAEEIEFCAQIYYQTKSVGEPKLLPEDEMENLAKKFE 208
Cdd:COG0235  160 VVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLVLSDEEIDKLARKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-184 1.44e-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: 197.38  E-value: 1.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302    8 EEIVAYGKKMISSGLTKGTGGNISIFnREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLIYYRKR 87
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVR-LPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   88 EDINALVHTHSPYAKTIASLGWELPAVSYLIA-FAGPNVRCAPYETFGTKQLAEAAFEGMI-DRRAVLLANHGLIAGANN 165
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAAdFLGGDIPIIPYYTPGTEELGERIAEALGgDRKAVLLRNHGLLVWGKT 159

                         170
                  ....*....|....*....
gi 446849302  166 IKMAFTVAEEIEFCAQIYY 184
Cdd:pfam00596 160 LEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-184 3.01e-57

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: 178.99  E-value: 3.01e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302    10 IVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGE--RKPSSELDMHLIYYRKR 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGggPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302    88 EDINALVHTHSPYAKTIASLGWELPAV--SYLIAFAGPNVRCAPYETFGT------KQLAEAAFEGMIDRRAVLLANHGL 159
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLptEQAAAFLGGEIPYAPYAGPGTelaeegAELAEALAEALPDRPAVLLRNHGL 160

                          170       180
                   ....*....|....*....|....*
gi 446849302   160 IAGANNIKMAFTVAEEIEFCAQIYY 184
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
8-211 1.15e-51

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 166.07  E-value: 1.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   8 EEIVAYGKKMISSGLTKGTGGNISIfnREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGeRKPSSELDMHLIYYRKR 87
Cdd:PRK08087   8 RQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEG-KLPSSEWRFHMAAYQTR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  88 EDINALVHTHSPYAKTIASLGWELPAVSYLIAFAGPN-VRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGLIAGANNI 166
Cdd:PRK08087  85 PDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNsIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446849302 167 KMAFTVAEEIEFCAQIYYQTKSVGEP-KLLPEDEMENLAKKFEGYG 211
Cdd:PRK08087 165 EKALWLAHEVEVLAQLYLKTLAITDPvPVLSDEEIAVVLEKFKTYG 210
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 9-207 1.03e-47

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: 155.60  E-value: 1.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   9 EIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGErKPSSELDMHLIYYRKRE 88
Cdd:cd00398    6 KIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGK-KPSSETPLHLALYRARP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  89 DINALVHTHSPYAKTIASLGWE-LPAVSYLIAFAGPN-VRCAPYETF--GTKQLAEAAFEGMIDRRAVLLANHGLIAGAN 164
Cdd:cd00398   85 DIGCIVHTHSTHATAVSQLKEGlIPAGHTACAVYFTGdIPCTPYMTPetGEDEIGTQRALGFPNSKAVLLRNHGLFAWGP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446849302 165 NIKMAFTVAEEIEFCAQIYYQTKSVGEPK-LLPEDEMENLAKKF 207
Cdd:cd00398  165 TLDEAFHLAVVLEVAAEIQLKALSMGGQLpPISLELLNKEYLRK 208
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 3-212 6.25e-44

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 146.31  E-value: 6.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   3 LQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLI 82
Cdd:PRK06557   8 VEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLKPSSDTASHLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  83 YYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIA--FAGPnVRCAPYETFGTKQLAEAAFEGMIDRR--AVLLANHG 158
Cdd:PRK06557  88 VYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMAdeFGGP-IPVGPFALIGDEAIGKGIVETLKGGRspAVLMQNHG 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446849302 159 LIAGANNIKMAFTVAEEIEFCAQIYYQTKSVGEPKLLPEDEMENLAKKFEG-YGQ 212
Cdd:PRK06557 167 VFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIPIPQEEIDRLYDRYQNvYGQ 221
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 10-204 2.21e-36

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 127.07  E-value: 2.21e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  10 IVAYGKKMISSGLTKGTGGNISIfNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGE--RKPSSELDMHLIYYRKR 87
Cdd:PRK05874  11 VLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHAKdgRSPSTELNLHLACYRAF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  88 EDINALVHTHSPYAKTIASLGWELPA-VSYLIAFAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGLIAGANNI 166
Cdd:PRK05874  90 DDIGSVIHSHPVWATMFAVAHEPIPAcIDEFAIYCGGDVRCTEYAASGTPEVGRNAVRALEGRAAALIANHGLVAVGPRP 169

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446849302 167 KMAFTVAEEIEFCAQIYYQTKSVGEPKLLPEDEMENLA 204
Cdd:PRK05874 170 DQVLRVTALVERTAQIVWGARALGGPVPIPEDVCRNFT 207
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
21-158 1.16e-33

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 119.94  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  21 GLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLIYYRKREDINALVHTHSPY 100
Cdd:PRK08193  20 GLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHLVLYKAFPEIGGIVHTHSRH 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446849302 101 AKTIASLGWELPAVSYLIA--FAGPnVRCAP----------YE---------TFGTKQLAEAAFEGmidrraVLLANHG 158
Cdd:PRK08193 100 ATAWAQAGRDIPALGTTHAdyFYGD-IPCTRkmtdeeingeYEwetgkviveTFEKRGIDPAAVPG------VLVHSHG 171
PRK08130 PRK08130
putative aldolase; Validated
 4-207 9.38e-31

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 112.28  E-value: 9.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   4 QKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVaISPSGLEYYETKPEDVVILNLDGEVVEGErKPSSELDMHLIY 83
Cdd:PRK08130   4 QALREEIVRLGRSLFQRGYTVGSAGNISARLDDGGWL-VTPTGSCLGRLDPARLSKVDADGNWLSGD-KPSKEVPLHRAI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  84 YRKREDINALVHTHSPYAKTIASL-GWE----LPAVS-YLIAFAGpNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANH 157
Cdd:PRK08130  82 YRNNPECGAVVHLHSTHLTALSCLgGLDptnvLPPFTpYYVMRVG-HVPLIPYYRPGDPAIAEALAGLAARYRAVLLANH 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446849302 158 GLIAGANNIKMAFTVAEEIEFCAQIYYQTKSVGePKLLPEDEMENLAKKF 207
Cdd:PRK08130 161 GPVVWGSSLEAAVNATEELEETAKLILLLGGRP-PRYLTDEEIAELRSTF 209
PRK08333 PRK08333
aldolase;
7-185 4.25e-29

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 107.22  E-value: 4.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   7 REEIVAYGKKMISSGLTKGTGGNISIfnREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERkPSSELDMHLIYYRK 86
Cdd:PRK08333   5 KAQLVKYSKLAHERGLTAAFGGNLSI--RVGNLVFIKATGSVMDELTREQVAVIDLNGNQLSSVR-PSSEYRLHLAVYRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  87 REDINALVHTHSPYAKTIAS-LGWELPAVSYLIAFAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGLIAGANN 165
Cdd:PRK08333  82 RPDVRAIAHLHPPYSIVASTlLEEELPIITPEAELYLKKIPILPFRPAGSVELAEQVAEAMKEYDAVIMERHGIVTVGRS 161

                        170       180
                 ....*....|....*....|
gi 446849302 166 IKMAFTVAEEIEFCAQIYYQ 185
Cdd:PRK08333 162 LREAFYKAELVEESAKLWYL 181
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 3-113 7.49e-29

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 107.58  E-value: 7.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   3 LQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLI 82
Cdd:PRK12348   1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLE 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446849302  83 YYRKREDINALVHTHSPYAKTIASLGWELPA 113
Cdd:PRK12348  81 LYRRYPSLGGIVHTHSTHATAWAQAGLAIPA 111
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-128 2.25e-26

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 101.45  E-value: 2.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   1 MLLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMH 80
Cdd:PRK13145   1 KNLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLNPSSDLPTH 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446849302  81 LIYYRKREDINALVHTHSPYAKTIASLGWELP--AVSYLIAFAGPnVRCA 128
Cdd:PRK13145  81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPfyGTTHADYFYGP-IPCA 129
FucA_Meth NF040649
L-fuculose phosphate aldolase;
25-184 6.45e-26

L-fuculose phosphate aldolase;


Pssm-ID: 468616  Cd Length: 179  Bit Score: 98.65  E-value: 6.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  25 GTGGNISIfnREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGerKPSSELDMHLIYYRKREDINALVHTHSPYAKTI 104
Cdd:NF040649  21 GSGGNVSI--REDDLIYITPTGSILGFLKEEDIAIVDLDGNIIKG--KPTSELNMHLKIYRKRKDINAIIHTHSLYSTAL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302 105 ASLGWELPAVSYLIAFAGPNVRCAPYETFGTKQLAEAAFEGmiDRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYY 184
Cdd:NF040649  97 SILDKKIELLTPEAKIFLKKIGYVDYLEAGSLELAEEVSKR--DEDVIILKNHGIVCLGKDLIEAYIKTEVLEEIAKLNL 174
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-114 2.46e-24

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 96.04  E-value: 2.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   2 LLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNL-DGEVVEGERKPSSELDMH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIaSGKVVEGSKKPSSDTPTH 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446849302  81 LIYYRKREDINALVHTHSPYAKTIASLGWELPAV 114
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAW 114
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 10-189 4.09e-24

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 94.25  E-value: 4.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   10 IVAYGKKMISSGLTKGTGGNISIFNREQGLVaISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLIYYRKReD 89
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLDEDEIL-ITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-G 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   90 INALVHTHSPYAkTIASLGW------ELPAVSYLIAFAG-------------PNvrcapyeTFGTKQLAEA---AFEGMI 147
Cdd:TIGR03328  79 AGAVLHTHSVEA-TVLSRLYpsnggfELEGYEMLKGLPGitthedtlvvpiiEN-------TQDIARLADSvapALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446849302  148 DRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYYQTKSV 189
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-191 9.24e-23

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 91.71  E-value: 9.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   2 LLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNL-DGEVVEGERKPSSELDMH 80
Cdd:PRK13213   1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLaTGKVVEGDKKPSSDTDTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  81 LIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIA--FAGPnVRC----------APYETFGTKQLAEA-AFEGM- 146
Cdd:PRK13213  81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHAdyFYGP-IPCtrlmteaeitGDYEHETGKVIVETfAEQGLr 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446849302 147 -IDRRAVLLANHGLIAGANNIKMAF---TVAEEIEFCAQIYYQ-TKSVGE 191
Cdd:PRK13213 160 aADIPAVLVNGHGPFAWGSNAANAVhnaVVLEEIAYMNLFTHQlTPGVGD 209
PRK06357 PRK06357
hypothetical protein; Provisional
 1-187 3.98e-22

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 89.83  E-value: 3.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   1 MLLQKEREEIVAYGKKMISSGLTKGTGGNISI---FNREQGLVAISP---SGLEYYETKPEDVVILNLD-GEVVEGERKP 73
Cdd:PRK06357   1 MLFQKEREDLAKVVKTMFDRKETNAAGGNISVrmtAEKNKEYIIMTPtlmSEAKLCDLSPYQILVVDLNtGEVIEGVGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  74 SSELDMHLIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIAFAGPnVRCAPYETFGTKQLAEAAFEGMIDRR--- 150
Cdd:PRK06357  81 TREINMHEAAYVANPKIKCVYHSHAKESMFWATLGLEMPNLTEATQKLGK-IPTLPFAPATSPELAEIVRKHLIELGdka 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446849302 151 ---AVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYYQTK 187
Cdd:PRK06357 160 vpsAFLLNSHGIVITDTSLHKAYDILETIEWNAYIAYQAT 199
PRK08660 PRK08660
aldolase;
8-187 3.01e-16

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 73.45  E-value: 3.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   8 EEIVAYGKKMISSGLTKGTGGNISIfnREQGLVAISPSGLEYYETKPEDVVI--LNLDGEVvegERKPSSELDMHLIYYR 85
Cdd:PRK08660   3 QEFARIGKKLFAHGLVSSHFGNISV--RTGDGLLITRTGSMLDEITEGDVIEvgIDDDGSV---DPLASSETPVHRAIYR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  86 kREDINALVHTHSPYAkTIASLGWEL--PAVSYLIAFAG--PNVRcapyETFGTKQLAEAAFEGMIDRRAVLLANHGLIA 161
Cdd:PRK08660  78 -RTSAKAIVHAHPPYA-VALSLLEDEivPLDSEGLYFLGtiPVVG----GDIGSGELAENVARALSEHKGVVVRGHGTFA 151

                        170       180
                 ....*....|....*....|....*.
gi 446849302 162 GANNIKMAFTVAEEIEFCAQIYYQTK 187
Cdd:PRK08660 152 IGKTLEEAYIYTSQLEHSCKVLYLVR 177
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
8-178 1.37e-14

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 69.20  E-value: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   8 EEIVAYGKKMISSGLTKGTGGNISIfNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLIYYRKR 87
Cdd:PRK09220   8 QQLIAAGRWIGARGWVPATSGNMSV-RLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHTQLYRLF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  88 EDINALVHTHSPYAkTIASL----------GWELpavsyLIAFAGPnvrcAPYET------FGTKQ----LA---EAAFE 144
Cdd:PRK09220  87 PEIGAVLHTHSVNA-TVLSRveksdalvleGYEL-----QKAFAGQ----TTHETavvvpiFDNDQdiarLAarvAPYLD 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446849302 145 GMIDRRAVLLANHGLIAGANNIKMAFTVAEEIEF 178
Cdd:PRK09220 157 AQPLRYGYLIRGHGLYCWGRDMAEARRHLEGLEF 190
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 46-198 1.11e-13

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 67.74  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  46 GLEYYETKPEDVVILNLDGEVVEGERKPSSELDMHLIYYRKREDINALVHTHSPYAKTIASLGWELpAVSYLIAfagpnv 125
Cdd:PRK07090  71 GLGFDEITASNLLLVDEDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSMLEVPL-VVSHMDT------ 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302 126 rCAPYEtfgtkqlaEAAF------------EGMI------DRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYYQTK 187
Cdd:PRK07090 144 -CPLYD--------DCAFlkdwpgvpvgneEGEIisaalgDKRAILLSHHGQLVAGKSIEEACVLALLIERAARLQLLAM 214

                        170
                 ....*....|.
gi 446849302 188 SVGEPKLLPED 198
Cdd:PRK07090 215 AAGPIKPIPPE 225
PRK03634 PRK03634
rhamnulose-1-phosphate aldolase; Provisional
 38-207 1.43e-10

rhamnulose-1-phosphate aldolase; Provisional


Pssm-ID: 179615 [Multi-domain]  Cd Length: 274  Bit Score: 59.23  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  38 GLVAISPSGLEYyetkpedVVILNLDGEVvegerKPSSELDMHL---IYYRKREDIN--ALVHTHSPyaktiaslgwELP 112
Cdd:PRK03634  91 GVIRIDSDGAGY-------HILWGLTNGG-----KPTSELPAHLmshIARLKATNGKdrVIMHCHAT----------NLI 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302 113 AVSYL-------------------IAFAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGLIAGANNIKMAFTVA 173
Cdd:PRK03634 149 ALTYVleldeavftrtlwemstecLVVFPDGVGIVPWMVPGTDEIGQATAEKMQKHDLVLWPKHGVFGSGPTLDEAFGLI 228

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446849302 174 EEIEFCAQIYYQTKSVG-EPKLLPEDEMENLAKKF 207
Cdd:PRK03634 229 DTAEKSAEIYVKVLSMGgMKQTITDEELIALGERF 263
PRK06208 PRK06208
class II aldolase/adducin family protein;
42-198 2.45e-10

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 58.46  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  42 ISPSGLEYYETKPEDVVILNLDGEVVEGERkPSSE--LDMHLIYYRKREDINALVHTHSPYAKTIASLGWELPAVSylia 119
Cdd:PRK06208  80 VNPLGVHFSQIKVSDLLLVDHDGEVVEGDR-PLNRaaFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDPIT---- 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302 120 fagpNVRCAPYE------TFGTKQLAEAafEG-MI-----DRRAVLLANHGLI--------AGANNIKMaftvaeeiEFC 179
Cdd:PRK06208 155 ----QDACAFYEdhalfdDFTGVVVDTS--EGrRIaaalgTHKAVILQNHGLLtvgpsvdaAAWWFIAL--------ERA 220

                        170
                 ....*....|....*....
gi 446849302 180 AQIYYQTKSVGEPKLLPED 198
Cdd:PRK06208 221 CQTQLLAEAAGPPQPIDHE 239
PRK07490 PRK07490
hypothetical protein; Provisional
 42-210 4.71e-09

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 54.73  E-value: 4.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  42 ISPSGLEYYETKPEDVVILNL-DGEVVEGERKP-SSELDMHLIYYRKREDINALVHTHSPYAKTIASLGW-ELPAVSYLI 118
Cdd:PRK07490  48 LNPKWKHFSRIRASDLLLLDAdDPSTAERPDVPdATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADpTLPPIDQNT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302 119 A-FAGPNVRCAPYETFGTKQLAEAAFEGMIDRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYYQTKSVGEP-KLLP 196
Cdd:PRK07490 128 ArFFNRVAVDTLYGGMALEEEGERLAGLLGDKRRLLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALSTGQPlRVLS 207

                        170
                 ....*....|....
gi 446849302 197 EDEMENLAKKFEGY 210
Cdd:PRK07490 208 DAVAEKTARDWEDY 221
PRK06661 PRK06661
hypothetical protein; Provisional
 11-206 7.38e-09

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 54.07  E-value: 7.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  11 VAYGKKMISS-GLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKPSSELD--MHLIYYRKR 87
Cdd:PRK06661   7 LAAAYRIMAYlSLDDHTYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQYNKTGyfIHGSIYKTR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  88 EDINALVHTHSPYAKTIASLGWELPAVSyliAFAGPNVRCAPYETFGTKQLaEAAFEG------MIDRRAVLLANHGLIA 161
Cdd:PRK06661  87 PDISAIFHYHTPASIAVSALKCGLLPIS---QWALHFYDRISYHNYNSLAL-DADKQSsrlvndLKQNYVMLLRNHGAIT 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446849302 162 GANNIKMAFTVAEEIEFCAQIYYQTKSVGEPKL-LPEDEMENLAKK 206
Cdd:PRK06661 163 CGKTIHEAMFYTYHLEQACKTQCLLNSTKKQELiIPSVEICKKTVK 208
PRK06486 PRK06486
aldolase;
37-198 6.52e-07

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 48.55  E-value: 6.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  37 QGLVAISPSGLEYYETKPEDVVILNLDGEVVEGERKP-SSELDMHLIYYRKREDINALVHTHSPYAkTIASLGWELPAVs 115
Cdd:PRK06486  59 DDLFLVNPYGYAFSEITASDLLICDFDGNVLAGRGEPeATAFFIHARIHRAIPRAKAAFHTHMPYA-TALSLTEGRPLT- 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302 116 yliaFAGPNV-----RCAPYETFgtKQLAEAAFEG------MIDRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYY 184
Cdd:PRK06486 137 ----TLGQTAlkfygRTAVDEDY--NGLALDAAEGdriaraMGDADIVFLKNHGVMVCGPRIAEAWDDLYYLERACEVQV 210

                        170
                 ....*....|....
gi 446849302 185 QTKSVGEPkLLPED 198
Cdd:PRK06486 211 LAMSTGRP-LVPVD 223
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
1-178 6.14e-05

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 42.35  E-value: 6.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302   1 MLLQKEREEIVAYGKKMISSGLTKGTGGNISI-FNREQGLVAISPSGLEYYETKPEDVVILNLDGEVVEGER-KPSSELD 78
Cdd:PRK06754   2 KQLQRRWNELAEIKKELAARDWFPATSGNLSIkVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEETElKPSAETL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446849302  79 MHLIYYrKREDINALVHTHSPYAKTIASLGWELPAVSY----LI-AFA----GPNVRCAPYETFG-TKQLAEaAFEGMI- 147
Cdd:PRK06754  82 LHTHIY-NNTNAGCVLHVHTVDNNVISELYGDDGAVTFqgqeIIkALGiweeNAEIHIPIIENHAdIPTLAE-EFAKHIq 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446849302 148 -DRRAVLLANHGLIAGANNIKMAFTVAEEIEF 178
Cdd:PRK06754 160 gDSGAVLIRNHGITVWGRDAFEAKKHLEAYEF 191
 
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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