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Conserved domains on  [gi|739110591|ref|WP_036980336|]
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MULTISPECIES: class II aldolase/adducin family protein [Pseudoalteromonas]

Protein Classification

class II aldolase/adducin family protein( domain architecture ID 10012869)

class II aldolase/adducin family protein similar to L-fuculose phosphate aldolase, which catalyzes the reversible aldol cleavage of L-fuculose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 5-254 1.46e-138

aldolase II superfamily protein; Provisional


:

Pssm-ID: 235916  Cd Length: 252  Bit Score: 389.59  E-value: 1.46e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   5 PQLDLKNKVSEQEWQLRVDLAACYRLVDHFRWGDLIYTHLSARLPGTD-HYLVNAFGLTFDEITASNLVKVDLNGRIIDD 83
Cdd:PRK07044   2 QPAAVPARVSPAEWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEhHFLINPYGLLFDEITASNLVKIDLDGNVVDD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  84 TPFDINPAGFTIHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPLSQYSMFSLPSLSYHGYEGLAVNDDERKRLQTDL 163
Cdd:PRK07044  82 SPYPVNPAGFTIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFYGRLAYHDYEGIALDLDEGERLVADL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591 164 GSTNHMLLVNHGGLTVGPTVGDAFMRFYDLQRACEIQLAIQSSAQEAIAVPQAIIDNIYNQAnVVHSGSTGGQLAWPAML 243
Cdd:PRK07044 162 GDKPAMLLRNHGLLTVGRTVAEAFLLMYTLERACEIQVAAQAGGGELVLPPPEVAERTARQS-LFDPGAGAGELAWPALL 240

                        250
                 ....*....|.
gi 739110591 244 RKAYRLDPSFA 254
Cdd:PRK07044 241 RKLDRIDPGYR 251
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 5-254 1.46e-138

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 389.59  E-value: 1.46e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   5 PQLDLKNKVSEQEWQLRVDLAACYRLVDHFRWGDLIYTHLSARLPGTD-HYLVNAFGLTFDEITASNLVKVDLNGRIIDD 83
Cdd:PRK07044   2 QPAAVPARVSPAEWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEhHFLINPYGLLFDEITASNLVKIDLDGNVVDD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  84 TPFDINPAGFTIHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPLSQYSMFSLPSLSYHGYEGLAVNDDERKRLQTDL 163
Cdd:PRK07044  82 SPYPVNPAGFTIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFYGRLAYHDYEGIALDLDEGERLVADL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591 164 GSTNHMLLVNHGGLTVGPTVGDAFMRFYDLQRACEIQLAIQSSAQEAIAVPQAIIDNIYNQAnVVHSGSTGGQLAWPAML 243
Cdd:PRK07044 162 GDKPAMLLRNHGLLTVGRTVAEAFLLMYTLERACEIQVAAQAGGGELVLPPPEVAERTARQS-LFDPGAGAGELAWPALL 240

                        250
                 ....*....|.
gi 739110591 244 RKAYRLDPSFA 254
Cdd:PRK07044 241 RKLDRIDPGYR 251
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 15-224 3.83e-63

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: 196.59  E-value: 3.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  15 EQEWQLRVDLAACYRLVDHFRWGDLIYTHLSARLPGtDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTpfDINPAGFT 94
Cdd:COG0235    1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD--LKPSSETP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  95 IHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPLSQ-YSMFSLPSLSYHGYEGLAvNDDERKRLQTDLGSTNHMLLVN 173
Cdd:COG0235   78 LHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQtEAAAFLGDVPVVPYAGPG-TEELAEAIAEALGDRPAVLLRN 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739110591 174 HGGLTVGPTVGDAFMRFYDLQRACEIQLAIQsSAQEAIAVPQAIIDNIYNQ 224
Cdd:COG0235  157 HGVVVWGKDLAEAFDRAEVLEEAARIQLLAL-ALGGPLVLSDEEIDKLARK 206
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 24-201 1.55e-53

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: 171.28  E-value: 1.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591    24 LAACYRLVDHFRWGDLIYTHLSARLPGTDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTPFDINPAGFTIHSAIHEVR 103
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   104 EDAHCVIHLHTKETIAVATQKE--GLLPLSQYSMFSLPSLSYHGYEGLAVNDDER-----KRLQTDLGSTNHMLLVNHGG 176
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKplPLLPTEQAAAFLGGEIPYAPYAGPGTELAEEgaelaEALAEALPDRPAVLLRNHGL 160

                          170       180
                   ....*....|....*....|....*
gi 739110591   177 LTVGPTVGDAFMRFYDLQRACEIQL 201
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 23-201 3.14e-52

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: 167.72  E-value: 3.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   23 DLAACYRLVDHFRWGDLIYTHLSARLPGtDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTPfdiNP-AGFTIHSAIHE 101
Cdd:pfam00596   2 ELAAAGRLLARRGLVEGTGGNISVRLPG-DGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGL---KPsSETPLHLAIYR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  102 VREDAHCVIHLHTKETIAVATQKEGLLPLSQYS-MFSLPSLSYHGYEGLAvNDDERKRLQTDLGSTNHMLLV-NHGGLTV 179
Cdd:pfam00596  78 ARPDAGAVVHTHSPYATALSLAKEGLPPITQEAaDFLGGDIPIIPYYTPG-TEELGERIAEALGGDRKAVLLrNHGLLVW 156

                         170       180
                  ....*....|....*....|..
gi 739110591  180 GPTVGDAFMRFYDLQRACEIQL 201
Cdd:pfam00596 157 GKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 17-226 1.79e-30

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: 112.46  E-value: 1.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  17 EWQLRvDLAACYRLVDHFRWGDLIYTHLSARLPGTDHYLVNAFGLTFDEITASNLVKVDLNGRIID------DTPFdinp 90
Cdd:cd00398    1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEgkkpssETPL---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  91 agftiHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPLSQYsMFSLP---SLSYHGYEGLAVNDDERkRLQTDLGSTN 167
Cdd:cd00398   76 -----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHT-ACAVYftgDIPCTPYMTPETGEDEI-GTQRALGFPN 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739110591 168 H--MLLVNHGGLTVGPTVGDAFMRFYDLQRACEIQLAIQSSAQEAIAVPQAIIDNIYNQAN 226
Cdd:cd00398  149 SkaVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 44-135 1.28e-05

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: 44.56  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   44 LSARLPGtDHYLVNAFGLTFDEITASNLVKVDLNGRIID-------DTPfdinpagftIHSAIHEvREDAHCVIHLHTKE 116
Cdd:TIGR03328  21 LSARLDE-DEILITPSGVDKGRLTPEDFLVVDLQGKPVSgglkpsaETL---------LHTQLYR-LTGAGAVLHTHSVE 89

                          90       100
                  ....*....|....*....|..
gi 739110591  117 TIaVATQ---KEGLLPLSQYSM 135
Cdd:TIGR03328  90 AT-VLSRlypSNGGFELEGYEM 110
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 5-254 1.46e-138

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 389.59  E-value: 1.46e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   5 PQLDLKNKVSEQEWQLRVDLAACYRLVDHFRWGDLIYTHLSARLPGTD-HYLVNAFGLTFDEITASNLVKVDLNGRIIDD 83
Cdd:PRK07044   2 QPAAVPARVSPAEWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEhHFLINPYGLLFDEITASNLVKIDLDGNVVDD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  84 TPFDINPAGFTIHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPLSQYSMFSLPSLSYHGYEGLAVNDDERKRLQTDL 163
Cdd:PRK07044  82 SPYPVNPAGFTIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFYGRLAYHDYEGIALDLDEGERLVADL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591 164 GSTNHMLLVNHGGLTVGPTVGDAFMRFYDLQRACEIQLAIQSSAQEAIAVPQAIIDNIYNQAnVVHSGSTGGQLAWPAML 243
Cdd:PRK07044 162 GDKPAMLLRNHGLLTVGRTVAEAFLLMYTLERACEIQVAAQAGGGELVLPPPEVAERTARQS-LFDPGAGAGELAWPALL 240

                        250
                 ....*....|.
gi 739110591 244 RKAYRLDPSFA 254
Cdd:PRK07044 241 RKLDRIDPGYR 251
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 15-224 3.83e-63

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: 196.59  E-value: 3.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  15 EQEWQLRVDLAACYRLVDHFRWGDLIYTHLSARLPGtDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTpfDINPAGFT 94
Cdd:COG0235    1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD--LKPSSETP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  95 IHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPLSQ-YSMFSLPSLSYHGYEGLAvNDDERKRLQTDLGSTNHMLLVN 173
Cdd:COG0235   78 LHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQtEAAAFLGDVPVVPYAGPG-TEELAEAIAEALGDRPAVLLRN 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739110591 174 HGGLTVGPTVGDAFMRFYDLQRACEIQLAIQsSAQEAIAVPQAIIDNIYNQ 224
Cdd:COG0235  157 HGVVVWGKDLAEAFDRAEVLEEAARIQLLAL-ALGGPLVLSDEEIDKLARK 206
PRK06661 PRK06661
hypothetical protein; Provisional
 20-214 3.87e-54

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 174.25  E-value: 3.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  20 LRVDLAACYRLVDHFRWGDLIYTHLSARLPGTDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTPFDINPAGFTIHSAI 99
Cdd:PRK06661   3 IKYNLAAAYRIMAYLSLDDHTYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQYNKTGYFIHGSI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591 100 HEVREDAHCVIHLHTKETIAVATQKEGLLPLSQYSMFSLPSLSYHGYEGLAVNDD-ERKRLQTDLGSTNHMLLVNHGGLT 178
Cdd:PRK06661  83 YKTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDRISYHNYNSLALDADkQSSRLVNDLKQNYVMLLRNHGAIT 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 739110591 179 VGPTVGDAFMRFYDLQRACEIQLAIQSSAQEAIAVP 214
Cdd:PRK06661 163 CGKTIHEAMFYTYHLEQACKTQCLLNSTKKQELIIP 198
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 24-201 1.55e-53

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: 171.28  E-value: 1.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591    24 LAACYRLVDHFRWGDLIYTHLSARLPGTDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTPFDINPAGFTIHSAIHEVR 103
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   104 EDAHCVIHLHTKETIAVATQKE--GLLPLSQYSMFSLPSLSYHGYEGLAVNDDER-----KRLQTDLGSTNHMLLVNHGG 176
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKplPLLPTEQAAAFLGGEIPYAPYAGPGTELAEEgaelaEALAEALPDRPAVLLRNHGL 160

                          170       180
                   ....*....|....*....|....*
gi 739110591   177 LTVGPTVGDAFMRFYDLQRACEIQL 201
Cdd:smart01007 161 LVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 23-201 3.14e-52

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: 167.72  E-value: 3.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   23 DLAACYRLVDHFRWGDLIYTHLSARLPGtDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTPfdiNP-AGFTIHSAIHE 101
Cdd:pfam00596   2 ELAAAGRLLARRGLVEGTGGNISVRLPG-DGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGL---KPsSETPLHLAIYR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  102 VREDAHCVIHLHTKETIAVATQKEGLLPLSQYS-MFSLPSLSYHGYEGLAvNDDERKRLQTDLGSTNHMLLV-NHGGLTV 179
Cdd:pfam00596  78 ARPDAGAVVHTHSPYATALSLAKEGLPPITQEAaDFLGGDIPIIPYYTPG-TEELGERIAEALGGDRKAVLLrNHGLLVW 156

                         170       180
                  ....*....|....*....|..
gi 739110591  180 GPTVGDAFMRFYDLQRACEIQL 201
Cdd:pfam00596 157 GKTLEEAFYLAEELERAAEIQL 178
PRK06486 PRK06486
aldolase;
14-224 1.55e-41

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 142.93  E-value: 1.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  14 SEQEWQLRVDLAACYRLVDHFRWGDLIYTHLSARLPG-TDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTPfDINPAG 92
Cdd:PRK06486  21 SDAVAQARVDLAACFRAAARHGLEEGICNHFSAVLPGhDDLFLVNPYGYAFSEITASDLLICDFDGNVLAGRG-EPEATA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  93 FTIHSAIHEVREDAHCVIHLHTKETIAVA-TQKEGLLPLSQYSMfslpslSYHG-------YEGLAVNDDERKRLQTDLG 164
Cdd:PRK06486 100 FFIHARIHRAIPRAKAAFHTHMPYATALSlTEGRPLTTLGQTAL------KFYGrtavdedYNGLALDAAEGDRIARAMG 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591 165 STNHMLLVNHGGLTVGPTVGDAFMRFYDLQRACEIQLAIQSSAQEAIAVPQAIIDNIYNQ 224
Cdd:PRK06486 174 DADIVFLKNHGVMVCGPRIAEAWDDLYYLERACEVQVLAMSTGRPLVPVDPAIAAAVARQ 233
PRK06208 PRK06208
class II aldolase/adducin family protein;
13-217 4.38e-38

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 134.35  E-value: 4.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  13 VSEQEWQLRVDLAACYRLVDHFRWGDLIYTHLSARLPG-TDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTPFdINPA 91
Cdd:PRK06208  36 VAEERLHRKQRLAAAFRLFARFGFDEGLAGHITARDPElPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDRP-LNRA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  92 GFTIHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPLSQYS-MFSLPSLSYHGYEGLAVNDDERKRLQTDLGSTNHML 170
Cdd:PRK06208 115 AFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDAcAFYEDHALFDDFTGVVVDTSEGRRIAAALGTHKAVI 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 739110591 171 LVNHGGLTVGPTVGDAFMRFYDLQRACEIQLAIqssaqEAIAVPQAI 217
Cdd:PRK06208 195 LQNHGLLTVGPSVDAAAWWFIALERACQTQLLA-----EAAGPPQPI 236
PRK07490 PRK07490
hypothetical protein; Provisional
 17-217 6.55e-33

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 119.82  E-value: 6.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  17 EWQLRVDLAACYRLVDHFRWGDLIYTHLSARL-PGTDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDTPFDINPAGFTI 95
Cdd:PRK07490   8 EEQIRVDLAAAFRWIARLGMHEAVANHFSAAVsADGKQFLLNPKWKHFSRIRASDLLLLDADDPSTAERPDVPDATAWAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  96 HSAIHEVREDAHCVIHLHTKETIAVATQKEG-LLPLSQYSMFSLPSLSY-HGYEGLAvNDDERKRLQTDLGSTNHMLLVN 173
Cdd:PRK07490  88 HGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTARFFNRVAVdTLYGGMA-LEEEGERLAGLLGDKRRLLMGN 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 739110591 174 HGGLTVGPTVGDAFMRFYDLQRACEIQLAIQSSAQEAIAVPQAI 217
Cdd:PRK07490 167 HGVLVTGDTVAEAFDDLYYFERACQTYITALSTGQPLRVLSDAV 210
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 17-226 1.79e-30

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: 112.46  E-value: 1.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  17 EWQLRvDLAACYRLVDHFRWGDLIYTHLSARLPGTDHYLVNAFGLTFDEITASNLVKVDLNGRIID------DTPFdinp 90
Cdd:cd00398    1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEgkkpssETPL---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  91 agftiHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPLSQYsMFSLP---SLSYHGYEGLAVNDDERkRLQTDLGSTN 167
Cdd:cd00398   76 -----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHT-ACAVYftgDIPCTPYMTPETGEDEI-GTQRALGFPN 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739110591 168 H--MLLVNHGGLTVGPTVGDAFMRFYDLQRACEIQLAIQSSAQEAIAVPQAIIDNIYNQAN 226
Cdd:cd00398  149 SkaVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 6-202 7.28e-18

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 80.45  E-value: 7.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   6 QLDLKNKVSEQEWQLRVDLA-ACYRLVDHFRWGDLIyTHLSARLPGTDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDT 84
Cdd:PRK07090  17 QRQMDNELKDSGWTLRQKLAlTCRILFDAGHDSGLA-GQITARAEAPGTYYTQRLGLGFDEITASNLLLVDEDLNVLDGE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  85 PFDiNPAGfTIHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLpLSQYSMFSLpslsyhgYE---------GLAVNDDE 155
Cdd:PRK07090  96 GMP-NPAN-RFHSWIYRARPDVNCIIHTHPPHVAALSMLEVPLV-VSHMDTCPL-------YDdcaflkdwpGVPVGNEE 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 739110591 156 RKRLQTDLGSTNHMLLVNHGGLTVGPTVGDAFMRFYDLQRACEIQLA 202
Cdd:PRK07090 166 GEIISAALGDKRAILLSHHGQLVAGKSIEEACVLALLIERAARLQLL 212
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 19-224 2.22e-10

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 58.87  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  19 QLRVDLAACYRLVDhfRWGDLIYT--HLSARLPGTDHYLVNAFGLTFDEITASNLVKVDLNGRIIDDtpfDINPAGFTI- 95
Cdd:PRK06557  10 KLREEVCKLHLELP--KYGLVVWTsgNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEG---DLKPSSDTAs 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  96 HSAIHEVREDAHCVIHLH-TKETIAVATQKE-------------GLLPLSQYSMfslpslsyhgyeglaVNDDE--RKRL 159
Cdd:PRK06557  85 HLYVYRHMPDVGGVVHTHsTYATAWAARGEPipcvltamadefgGPIPVGPFAL---------------IGDEAigKGIV 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739110591 160 QTDLGSTN-HMLLVNHGGLTVGPTVGDAF---MRFYDLQRACEIQLAIqssaQEAIAVPQAIIDNIYNQ 224
Cdd:PRK06557 150 ETLKGGRSpAVLMQNHGVFTIGKDAEDAVkaaVMVEEVARTVHIARQL----GEPIPIPQEEIDRLYDR 214
PRK08333 PRK08333
aldolase;
52-189 2.72e-09

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 55.21  E-value: 2.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  52 DHYLVNAFGLTFDEITASNLVKVDLNGRIIDDtpfdINPAG-FTIHSAIHEVREDAHCVIHLHTKETIAVATQKEGLLPL 130
Cdd:PRK08333  34 NLVFIKATGSVMDELTREQVAVIDLNGNQLSS----VRPSSeYRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPI 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739110591 131 ----SQYSMFSLPSLSYH--GYEGLAVNDDERkrlqtdLGSTNHMLLVNHGGLTVGPTVGDAFMR 189
Cdd:PRK08333 110 itpeAELYLKKIPILPFRpaGSVELAEQVAEA------MKEYDAVIMERHGIVTVGRSLREAFYK 168
PRK08130 PRK08130
putative aldolase; Validated
 41-186 4.74e-06

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 46.02  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  41 YTH-----LSARLPGtDHYLVNAFGLTFDEITASNLVKVDLNGRIID-DTPFDINPagftIHSAIHEVREDAHCVIHLHT 114
Cdd:PRK08130  22 YTVgsagnISARLDD-GGWLVTPTGSCLGRLDPARLSKVDADGNWLSgDKPSKEVP----LHRAIYRNNPECGAVVHLHS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591 115 keTIAVA-------TQKEGLLPLSQYSMF---SLPSLSYHGYEGLAVNDDERKRlqtdLGSTNHMLLVNHGGLTVGPTVG 184
Cdd:PRK08130  97 --THLTAlsclgglDPTNVLPPFTPYYVMrvgHVPLIPYYRPGDPAIAEALAGL----AARYRAVLLANHGPVVWGSSLE 170


                 ..
gi 739110591 185 DA 186
Cdd:PRK08130 171 AA 172
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
60-187 6.10e-06

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 45.90  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591  60 GLTFDEITASNLVKVDLNGRIIDDTpfDINPAGFTIHSAIHEVREDAHCVIHLHTKETIAVATQKEGL------------ 127
Cdd:PRK06833  46 GIDYFEIKPEDIVIMDLDGKVVEGE--RKPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGWELpavhyliavagp 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739110591 128 -LPLSQYSMFSLPSLSYHGYEGLavndDERKRLqtdlgstnhmLLVNHGGLTVGPTVGDAF 187
Cdd:PRK06833 124 nVRCAEYATFGTKELAENAFEAM----EDRRAV----------LLANHGLLAGANNLKNAF 170
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 44-135 1.28e-05

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: 44.56  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739110591   44 LSARLPGtDHYLVNAFGLTFDEITASNLVKVDLNGRIID-------DTPfdinpagftIHSAIHEvREDAHCVIHLHTKE 116
Cdd:TIGR03328  21 LSARLDE-DEILITPSGVDKGRLTPEDFLVVDLQGKPVSgglkpsaETL---------LHTQLYR-LTGAGAVLHTHSVE 89

                          90       100
                  ....*....|....*....|..
gi 739110591  117 TIaVATQ---KEGLLPLSQYSM 135
Cdd:TIGR03328  90 AT-VLSRlypSNGGFELEGYEM 110
 
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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