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Conserved domains on  [gi|2292704562|ref|WP_258759137|]
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methylthioribulose 1-phosphate dehydratase [Cytobacillus firmus]

Protein Classification

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

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

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
1-204 2.74e-135

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


The actual alignment was detected with superfamily member PRK06754:

Pssm-ID: 469663 [Multi-domain]  Cd Length: 208  Bit Score: 377.47  E-value: 2.74e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   1 MSRVGEKWNELADIKEELAERDWFMGTSGNLAIKVSSHPLQFLVTASGKDKRKRTDEDFLLVDEYGHPAGETHLKPSAET 80
Cdd:PRK06754    1 MKQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEETELKPSAET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  81 LLHSEIYRRTKAECSLHVHTIDNNVISEIYGDQAAVTFKGQELIKAFDKWEEDAVLEIPIIPNHAHIPTLAKCFSSHIHE 160
Cdd:PRK06754   81 LLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKALGIWEENAEIHIPIIENHADIPTLAEEFAKHIQG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2292704562 161 DAGAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLAYKP 204
Cdd:PRK06754  161 DSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQG 204
 
Name Accession Description Interval E-value
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
1-204 2.74e-135

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 377.47  E-value: 2.74e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   1 MSRVGEKWNELADIKEELAERDWFMGTSGNLAIKVSSHPLQFLVTASGKDKRKRTDEDFLLVDEYGHPAGETHLKPSAET 80
Cdd:PRK06754    1 MKQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEETELKPSAET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  81 LLHSEIYRRTKAECSLHVHTIDNNVISEIYGDQAAVTFKGQELIKAFDKWEEDAVLEIPIIPNHAHIPTLAKCFSSHIHE 160
Cdd:PRK06754   81 LLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKALGIWEENAEIHIPIIENHADIPTLAEEFAKHIQG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2292704562 161 DAGAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLAYKP 204
Cdd:PRK06754  161 DSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQG 204
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
11-200 5.42e-75

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: 224.45  E-value: 5.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  11 LADIKEELAERDWFMGTSGNLAIKVSshPLQFLVTASGKDKRKRTDEDFLLVDEYGHPAgETHLKPSAETLLHSEIYRRT 90
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPV-SGGLKPSAETLLHTQLYRLT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  91 KAECSLHVHTIDNNVISEIYGDQAAVTFKGQELIKAFDK-WEEDAVLEIPIIPNHAHIPTLAKCFSSHI--HEDAGAVLI 167
Cdd:TIGR03328  78 GAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGLPGiTTHEDTLVVPIIENTQDIARLADSVAPALnaYPDVPGVLI 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2292704562 168 RNHGITVWGKTSFEAKKILEASEFLFRYQLRLL 200
Cdd:TIGR03328 158 RGHGLYAWGRDWEEAKRHLEALEFLFECELEML 190
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
9-197 1.46e-40

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: 136.14  E-value: 1.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   9 NELADIKEELAERDWFMGTSGNLAIKVSSHplQFLVTASGKDKRKRTDEDFLLVDEYGHPAgETHLKPSAETLLHSEIYR 88
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGD--GFLITPSGVDFGELTPEDLVVVDLDGNVV-EGGLKPSSETPLHLAIYR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  89 -RTKAECSLHVHTIDNNVISEIygdqaavtfkgQELIKAFDKWEEDAV-LEIPIIPNHAH-IPTLAKCFSSHIHEDAGAV 165
Cdd:pfam00596  78 aRPDAGAVVHTHSPYATALSLA-----------KEGLPPITQEAADFLgGDIPIIPYYTPgTEELGERIAEALGGDRKAV 146
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2292704562 166 LIRNHGITVWGKTSFEAKKILEASEFLFRYQL 197
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
10-201 3.52e-37

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: 128.41  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  10 ELADIKEELAERDWFMGTSGNLAIKVSSHplQFLVTASGKDKRKRTDEDFLLVDEYGHPAgETHLKPSAETLLHSEIYR- 88
Cdd:COG0235     9 ELAAAGRRLARRGLVDGTAGNISVRLDDD--RFLITPSGVDFGELTPEDLVVVDLDGNVV-EGDLKPSSETPLHLAIYRa 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  89 RTKAECSLHVHTIDNNVISeiygdQAAVTFKGQELIKAfdkweeDAVL-EIPIIPnHAHIPT------LAKCFsshihED 161
Cdd:COG0235    86 RPDVGAVVHTHSPYATALS-----ALGEPLPPLEQTEA------AAFLgDVPVVP-YAGPGTeelaeaIAEAL-----GD 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2292704562 162 AGAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLA 201
Cdd:COG0235   149 RPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA 188
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
11-197 3.73e-33

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: 117.35  E-value: 3.73e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   11 LADIKEELAERDWFMGTSGNLAIKVSsHPLQFLVTASGKDKRKRTDEDFLLVDEYGHP-AGETHLKPSAETLLHSEIYR- 88
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVvEGGGGPKPSSETPLHLAIYRa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   89 RTKAECSLHVHTIDNNVIS------EIYGDQAAVTFKGQELikafdkweEDAVLEIPIIPNHAHIPTLAKCFSSHIhEDA 162
Cdd:smart01007  80 RPDVGAVVHTHSPYATALAalgkplPLLPTEQAAAFLGGEI--------PYAPYAGPGTELAEEGAELAEALAEAL-PDR 150
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2292704562  163 GAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQL 197
Cdd:smart01007 151 PAVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
9-201 8.44e-14

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: 67.39  E-value: 8.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   9 NELADIKEELAERDWFMGTSGNLAIKVSSHPLqFLVTASGKDKRKRTDEDFLLVDEYG-HPAGEthlKPSAETLLHSEIY 87
Cdd:cd00398     5 RKIIAACLLLDLYGWVTGTGGNVSARDRDRGY-FLITPSGVDYEEMTASDLVVVDAQGkVVEGK---KPSSETPLHLALY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  88 R-RTKAECSLHVHTIDnnviseiygdQAAVTFKGQELIKAfdkWEEDAVL----EIPIIPNHAhIPTLAKCFSSHIHE-- 160
Cdd:cd00398    81 RaRPDIGCIVHTHSTH----------ATAVSQLKEGLIPA---GHTACAVyftgDIPCTPYMT-PETGEDEIGTQRALgf 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2292704562 161 -DAGAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLA 201
Cdd:cd00398   147 pNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALS 188
 
Name Accession Description Interval E-value
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
1-204 2.74e-135

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 377.47  E-value: 2.74e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   1 MSRVGEKWNELADIKEELAERDWFMGTSGNLAIKVSSHPLQFLVTASGKDKRKRTDEDFLLVDEYGHPAGETHLKPSAET 80
Cdd:PRK06754    1 MKQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEETELKPSAET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  81 LLHSEIYRRTKAECSLHVHTIDNNVISEIYGDQAAVTFKGQELIKAFDKWEEDAVLEIPIIPNHAHIPTLAKCFSSHIHE 160
Cdd:PRK06754   81 LLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKALGIWEENAEIHIPIIENHADIPTLAEEFAKHIQG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2292704562 161 DAGAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLAYKP 204
Cdd:PRK06754  161 DSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQG 204
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
11-200 5.42e-75

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: 224.45  E-value: 5.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  11 LADIKEELAERDWFMGTSGNLAIKVSshPLQFLVTASGKDKRKRTDEDFLLVDEYGHPAgETHLKPSAETLLHSEIYRRT 90
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPV-SGGLKPSAETLLHTQLYRLT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  91 KAECSLHVHTIDNNVISEIYGDQAAVTFKGQELIKAFDK-WEEDAVLEIPIIPNHAHIPTLAKCFSSHI--HEDAGAVLI 167
Cdd:TIGR03328  78 GAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGLPGiTTHEDTLVVPIIENTQDIARLADSVAPALnaYPDVPGVLI 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2292704562 168 RNHGITVWGKTSFEAKKILEASEFLFRYQLRLL 200
Cdd:TIGR03328 158 RGHGLYAWGRDWEEAKRHLEALEFLFECELEML 190
PRK06755 PRK06755
hypothetical protein; Validated
6-203 3.93e-55

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 174.45  E-value: 3.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   6 EKWNELADIKEELAERDWFMGTSGNLAIKVSSHPLQFLVTASGKDKRKRTDEDFLLVDEYGHPAGETHLKPSAETLLHSE 85
Cdd:PRK06755    6 KKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCEPVFENEEKPAAESFMHAD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  86 IYRRTKAECSLHVHTIDNNVISEIYGDQAAVTFKGQELIKAFDKwEEDAVLEIPIIPNHAHIPTLAKCFSSHIHEDAGAV 165
Cdd:PRK06755   86 IYKKSSAECILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGK-EGITEMTIPIVEDEKKFADLLENNVPNFIEGGGVV 164
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2292704562 166 LIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLAYK 203
Cdd:PRK06755  165 LVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIK 202
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
10-203 6.82e-42

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 140.46  E-value: 6.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  10 ELADIKEELAERDWFMGTSGNLAIKVSSHplQFLVTASGKDKRKRTDEDFLLVDEYGHPAGETHlKPSAETLLHSEIYRR 89
Cdd:PRK09220    9 QLIAAGRWIGARGWVPATSGNMSVRLDEQ--HCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGR-KPSAETLLHTQLYRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  90 -TKAECSLHVHTIDNNVISeIYGDQAAVTFKGQELIKAFD--KWEEDAVlEIPIIPNHAHIPTLAKCFSSHI--HEDAGA 164
Cdd:PRK09220   86 fPEIGAVLHTHSVNATVLS-RVEKSDALVLEGYELQKAFAgqTTHETAV-VVPIFDNDQDIARLAARVAPYLdaQPLRYG 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2292704562 165 VLIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLAYK 203
Cdd:PRK09220  164 YLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLLE 202
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
9-197 1.46e-40

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: 136.14  E-value: 1.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   9 NELADIKEELAERDWFMGTSGNLAIKVSSHplQFLVTASGKDKRKRTDEDFLLVDEYGHPAgETHLKPSAETLLHSEIYR 88
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGD--GFLITPSGVDFGELTPEDLVVVDLDGNVV-EGGLKPSSETPLHLAIYR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  89 -RTKAECSLHVHTIDNNVISEIygdqaavtfkgQELIKAFDKWEEDAV-LEIPIIPNHAH-IPTLAKCFSSHIHEDAGAV 165
Cdd:pfam00596  78 aRPDAGAVVHTHSPYATALSLA-----------KEGLPPITQEAADFLgGDIPIIPYYTPgTEELGERIAEALGGDRKAV 146
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2292704562 166 LIRNHGITVWGKTSFEAKKILEASEFLFRYQL 197
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
10-201 3.52e-37

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: 128.41  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  10 ELADIKEELAERDWFMGTSGNLAIKVSSHplQFLVTASGKDKRKRTDEDFLLVDEYGHPAgETHLKPSAETLLHSEIYR- 88
Cdd:COG0235     9 ELAAAGRRLARRGLVDGTAGNISVRLDDD--RFLITPSGVDFGELTPEDLVVVDLDGNVV-EGDLKPSSETPLHLAIYRa 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  89 RTKAECSLHVHTIDNNVISeiygdQAAVTFKGQELIKAfdkweeDAVL-EIPIIPnHAHIPT------LAKCFsshihED 161
Cdd:COG0235    86 RPDVGAVVHTHSPYATALS-----ALGEPLPPLEQTEA------AAFLgDVPVVP-YAGPGTeelaeaIAEAL-----GD 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2292704562 162 AGAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLA 201
Cdd:COG0235   149 RPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA 188
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
11-197 3.73e-33

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: 117.35  E-value: 3.73e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   11 LADIKEELAERDWFMGTSGNLAIKVSsHPLQFLVTASGKDKRKRTDEDFLLVDEYGHP-AGETHLKPSAETLLHSEIYR- 88
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVvEGGGGPKPSSETPLHLAIYRa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   89 RTKAECSLHVHTIDNNVIS------EIYGDQAAVTFKGQELikafdkweEDAVLEIPIIPNHAHIPTLAKCFSSHIhEDA 162
Cdd:smart01007  80 RPDVGAVVHTHSPYATALAalgkplPLLPTEQAAAFLGGEI--------PYAPYAGPGTELAEEGAELAEALAEAL-PDR 150
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2292704562  163 GAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQL 197
Cdd:smart01007 151 PAVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
9-201 8.44e-14

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: 67.39  E-value: 8.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   9 NELADIKEELAERDWFMGTSGNLAIKVSSHPLqFLVTASGKDKRKRTDEDFLLVDEYG-HPAGEthlKPSAETLLHSEIY 87
Cdd:cd00398     5 RKIIAACLLLDLYGWVTGTGGNVSARDRDRGY-FLITPSGVDYEEMTASDLVVVDAQGkVVEGK---KPSSETPLHLALY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  88 R-RTKAECSLHVHTIDnnviseiygdQAAVTFKGQELIKAfdkWEEDAVL----EIPIIPNHAhIPTLAKCFSSHIHE-- 160
Cdd:cd00398    81 RaRPDIGCIVHTHSTH----------ATAVSQLKEGLIPA---GHTACAVyftgDIPCTPYMT-PETGEDEIGTQRALgf 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2292704562 161 -DAGAVLIRNHGITVWGKTSFEAKKILEASEFLFRYQLRLLA 201
Cdd:cd00398   147 pNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALS 188
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
10-184 1.06e-04

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 41.53  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  10 ELADIKEELAERDWFMGTSGNLAIKVSSHPLqFLVTASGKDKRKRTDEDFLLVDEYGHPAgETHLKPSAETLLHSEIYR- 88
Cdd:PRK06557   14 EVCKLHLELPKYGLVVWTSGNVSARDPGTDL-VVIKPSGVSYDDLTPEDMVVVDLDGNVV-EGDLKPSSDTASHLYVYRh 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  89 RTKAECSLHVHTidnnviseIYGDQAAVTfkGQE----LIKAFDKWEEdavlEIPIIPnHAHIPT--LAKCFSSHIHED- 161
Cdd:PRK06557   92 MPDVGGVVHTHS--------TYATAWAAR--GEPipcvLTAMADEFGG----PIPVGP-FALIGDeaIGKGIVETLKGGr 156
                         170       180
                  ....*....|....*....|...
gi 2292704562 162 AGAVLIRNHGITVWGKTSFEAKK 184
Cdd:PRK06557  157 SPAVLMQNHGVFTIGKDAEDAVK 179
PRK08333 PRK08333
aldolase;
29-182 1.15e-03

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 38.27  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562  29 GNLAIKVSSHplqFLVTASGKDKRKRTDEDFLLVDEYGHPAgeTHLKPSAETLLHSEIYR-RTKAECSLHVHTIDNNVIS 107
Cdd:PRK08333   26 GNLSIRVGNL---VFIKATGSVMDELTREQVAVIDLNGNQL--SSVRPSSEYRLHLAVYRnRPDVRAIAHLHPPYSIVAS 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2292704562 108 EIYGDQAAVTFKGQELIkafdkweedaVLEIPIIP-NHAHIPTLAKCFSSHIhEDAGAVLIRNHGITVWGKTSFEA 182
Cdd:PRK08333  101 TLLEEELPIITPEAELY----------LKKIPILPfRPAGSVELAEQVAEAM-KEYDAVIMERHGIVTVGRSLREA 165
PRK08660 PRK08660
aldolase;
8-99 4.28e-03

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 36.86  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2292704562   8 WNELADIKEELAERDWFMGTSGNLAIKVSShplQFLVTASGKDKRKRTDEDFLLVDEygHPAGETHLKPSAETLLHSEIY 87
Cdd:PRK08660    2 WQEFARIGKKLFAHGLVSSHFGNISVRTGD---GLLITRTGSMLDEITEGDVIEVGI--DDDGSVDPLASSETPVHRAIY 76
                          90
                  ....*....|..
gi 2292704562  88 RRTKAECSLHVH 99
Cdd:PRK08660   77 RRTSAKAIVHAH 88
 
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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