NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|550795092|ref|WP_022650583|]
View 

MULTISPECIES: methylthioribulose 1-phosphate dehydratase [Enterobacter]

Protein Classification

methylthioribulose-1-phosphate dehydratase( domain architecture ID 10013153)

methylthioribulose-1-phosphate dehydratase catalyzes the formation of diketo methylthiopentyl phosphate from methylribulose phosphate in the methionine salvage pathway

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
1-203 6.09e-139

methylthioribulose 1-phosphate dehydratase;


:

Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 386.21  E-value: 6.09e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   1 MTDNLQLTHLVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHT 80
Cdd:PRK09220   1 MTLEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  81 LIYRLFPEANAVLHVHTVNATVLSRLVNEAELKITGFEMQKSLTGQTTHRDTVAIPVFDNDQDIDALASRIAHYAQERPL 160
Cdd:PRK09220  81 QLYRLFPEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQPL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 550795092 161 NYGFLLRGHGLTCWGRDVAEARRHLEGLEFLFECEMRLRQWER 203
Cdd:PRK09220 161 RYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLLEA 203
 
Name Accession Description Interval E-value
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
1-203 6.09e-139

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 386.21  E-value: 6.09e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   1 MTDNLQLTHLVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHT 80
Cdd:PRK09220   1 MTLEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  81 LIYRLFPEANAVLHVHTVNATVLSRLVNEAELKITGFEMQKSLTGQTTHRDTVAIPVFDNDQDIDALASRIAHYAQERPL 160
Cdd:PRK09220  81 QLYRLFPEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQPL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 550795092 161 NYGFLLRGHGLTCWGRDVAEARRHLEGLEFLFECEMRLRQWER 203
Cdd:PRK09220 161 RYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLLEA 203
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 10-200 5.99e-94

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: 272.22  E-value: 5.99e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   10 LVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFpEA 89
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-GA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   90 NAVLHVHTVNATVLSRLVNE-AELKITGFEMQKSLTGQTTHRDTVAIPVFDNDQDIDALASRIAHYAQERPLNYGFLLRG 168
Cdd:TIGR03328  80 GAVLHTHSVEATVLSRLYPSnGGFELEGYEMLKGLPGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRG 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 550795092  169 HGLTCWGRDVAEARRHLEGLEFLFECEMRLRQ 200
Cdd:TIGR03328 160 HGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 10-200 1.24e-54

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: 172.71  E-value: 1.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  10 LVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFPEA 89
Cdd:COG0235   10 LAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHLAIYRARPDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  90 NAVLHVHTVNATVLSRLvneaELKITGFEMQKSLTGqttHRDtvaIPVFD-NDQDIDALASRIAHYAQERPlnyGFLLRG 168
Cdd:COG0235   90 GAVVHTHSPYATALSAL----GEPLPPLEQTEAAAF---LGD---VPVVPyAGPGTEELAEAIAEALGDRP---AVLLRN 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 550795092 169 HGLTCWGRDVAEARRHLEGLEFLFECEMRLRQ 200
Cdd:COG0235  157 HGVVVWGKDLAEAFDRAEVLEEAARIQLLALA 188
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-195 3.04e-51

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: 163.58  E-value: 3.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092    10 LVEACRWIGAKGWAPATGGNMSVR-QDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSG--RKPSAETGLHTLIYRLF 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARvGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGggPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092    87 PEANAVLHVHTVNATVLSRLVNEAELKITgfEMQKSLTGQTTHRDTVAIPVFDNDQDIDALASRIAHYAQERPlnyGFLL 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPT--EQAAAFLGGEIPYAPYAGPGTELAEEGAELAEALAEALPDRP---AVLL 155

                          170       180
                   ....*....|....*....|....*....
gi 550795092   167 RGHGLTCWGRDVAEARRHLEGLEFLFECE 195
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQ 184
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-194 9.94e-49

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: 156.94  E-value: 9.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092    9 HLVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFPE 88
Cdd:pfam00596   2 ELAAAGRLLARRGLVEGTGGNISVRLPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRARPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   89 ANAVLHVHTVNATVLSRLvnEAELKITGFEMQKSLTGQtthrdtvaIPVFDNDQ-DIDALASRIAHYAQERplNYGFLLR 167
Cdd:pfam00596  82 AGAVVHTHSPYATALSLA--KEGLPPITQEAADFLGGD--------IPIIPYYTpGTEELGERIAEALGGD--RKAVLLR 149

                         170       180
                  ....*....|....*....|....*..
gi 550795092  168 GHGLTCWGRDVAEARRHLEGLEFLFEC 194
Cdd:pfam00596 150 NHGLLVWGKTLEEAFYLAEELERAAEI 176
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 10-200 1.72e-22

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: 90.12  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  10 LVEACRWIGAKGWAPATGGNMSVRQDEHLCWL-SESGKDKGSLTTADFLQVEIATNRApSGRKPSAETGLHTLIYRLFPE 88
Cdd:cd00398    7 IIAACLLLDLYGWVTGTGGNVSARDRDRGYFLiTPSGVDYEEMTASDLVVVDAQGKVV-EGKKPSSETPLHLALYRARPD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  89 ANAVLHVHTVNATVLSrLVNEAELKITGFEMQKSLTGqtthrdtvAIPVFDNDQDIDALASRIAHYAQERPLNYGFLLRG 168
Cdd:cd00398   86 IGCIVHTHSTHATAVS-QLKEGLIPAGHTACAVYFTG--------DIPCTPYMTPETGEDEIGTQRALGFPNSKAVLLRN 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 550795092 169 HGLTCWGRDVAEARRHLEGLEFLFECEMRLRQ 200
Cdd:cd00398  157 HGLFAWGPTLDEAFHLAVVLEVAAEIQLKALS 188
 
Name Accession Description Interval E-value
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
1-203 6.09e-139

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 386.21  E-value: 6.09e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   1 MTDNLQLTHLVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHT 80
Cdd:PRK09220   1 MTLEELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  81 LIYRLFPEANAVLHVHTVNATVLSRLVNEAELKITGFEMQKSLTGQTTHRDTVAIPVFDNDQDIDALASRIAHYAQERPL 160
Cdd:PRK09220  81 QLYRLFPEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQPL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 550795092 161 NYGFLLRGHGLTCWGRDVAEARRHLEGLEFLFECEMRLRQWER 203
Cdd:PRK09220 161 RYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLLEA 203
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 10-200 5.99e-94

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: 272.22  E-value: 5.99e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   10 LVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFpEA 89
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-GA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   90 NAVLHVHTVNATVLSRLVNE-AELKITGFEMQKSLTGQTTHRDTVAIPVFDNDQDIDALASRIAHYAQERPLNYGFLLRG 168
Cdd:TIGR03328  80 GAVLHTHSVEATVLSRLYPSnGGFELEGYEMLKGLPGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRG 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 550795092  169 HGLTCWGRDVAEARRHLEGLEFLFECEMRLRQ 200
Cdd:TIGR03328 160 HGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 10-200 1.24e-54

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: 172.71  E-value: 1.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  10 LVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFPEA 89
Cdd:COG0235   10 LAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHLAIYRARPDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  90 NAVLHVHTVNATVLSRLvneaELKITGFEMQKSLTGqttHRDtvaIPVFD-NDQDIDALASRIAHYAQERPlnyGFLLRG 168
Cdd:COG0235   90 GAVVHTHSPYATALSAL----GEPLPPLEQTEAAAF---LGD---VPVVPyAGPGTEELAEAIAEALGDRP---AVLLRN 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 550795092 169 HGLTCWGRDVAEARRHLEGLEFLFECEMRLRQ 200
Cdd:COG0235  157 HGVVVWGKDLAEAFDRAEVLEEAARIQLLALA 188
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-195 3.04e-51

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: 163.58  E-value: 3.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092    10 LVEACRWIGAKGWAPATGGNMSVR-QDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSG--RKPSAETGLHTLIYRLF 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARvGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGggPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092    87 PEANAVLHVHTVNATVLSRLVNEAELKITgfEMQKSLTGQTTHRDTVAIPVFDNDQDIDALASRIAHYAQERPlnyGFLL 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPT--EQAAAFLGGEIPYAPYAGPGTELAEEGAELAEALAEALPDRP---AVLL 155

                          170       180
                   ....*....|....*....|....*....
gi 550795092   167 RGHGLTCWGRDVAEARRHLEGLEFLFECE 195
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQ 184
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-194 9.94e-49

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: 156.94  E-value: 9.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092    9 HLVEACRWIGAKGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFPE 88
Cdd:pfam00596   2 ELAAAGRLLARRGLVEGTGGNISVRLPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRARPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   89 ANAVLHVHTVNATVLSRLvnEAELKITGFEMQKSLTGQtthrdtvaIPVFDNDQ-DIDALASRIAHYAQERplNYGFLLR 167
Cdd:pfam00596  82 AGAVVHTHSPYATALSLA--KEGLPPITQEAADFLGGD--------IPIIPYYTpGTEELGERIAEALGGD--RKAVLLR 149

                         170       180
                  ....*....|....*....|....*..
gi 550795092  168 GHGLTCWGRDVAEARRHLEGLEFLFEC 194
Cdd:pfam00596 150 NHGLLVWGKTLEEAFYLAEELERAAEI 176
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
10-200 1.01e-46

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 152.90  E-value: 1.01e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  10 LVEACRWIGAKGWAPATGGNMSVR-QDEHLCWL-SESGKDKGSLTTADFLQVEIATNRAPSGR-KPSAETGLHTLIYRLf 86
Cdd:PRK06754  11 LAEIKKELAARDWFPATSGNLSIKvSDDPLTFLvTASGKDKRKTTPEDFLLVDHDGKPVEETElKPSAETLLHTHIYNN- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  87 PEANAVLHVHTVNATVLSRLV-NEAELKITGFEMQKSLtGQTTHRDTVAIPVFDNDQDIDALASRIAHYAQerPLNYGFL 165
Cdd:PRK06754  90 TNAGCVLHVHTVDNNVISELYgDDGAVTFQGQEIIKAL-GIWEENAEIHIPIIENHADIPTLAEEFAKHIQ--GDSGAVL 166

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 550795092 166 LRGHGLTCWGRDVAEARRHLEGLEFLFECEMRLRQ 200
Cdd:PRK06754 167 IRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLS 201
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 10-200 1.72e-22

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: 90.12  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  10 LVEACRWIGAKGWAPATGGNMSVRQDEHLCWL-SESGKDKGSLTTADFLQVEIATNRApSGRKPSAETGLHTLIYRLFPE 88
Cdd:cd00398    7 IIAACLLLDLYGWVTGTGGNVSARDRDRGYFLiTPSGVDYEEMTASDLVVVDAQGKVV-EGKKPSSETPLHLALYRARPD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  89 ANAVLHVHTVNATVLSrLVNEAELKITGFEMQKSLTGqtthrdtvAIPVFDNDQDIDALASRIAHYAQERPLNYGFLLRG 168
Cdd:cd00398   86 IGCIVHTHSTHATAVS-QLKEGLIPAGHTACAVYFTG--------DIPCTPYMTPETGEDEIGTQRALGFPNSKAVLLRN 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 550795092 169 HGLTCWGRDVAEARRHLEGLEFLFECEMRLRQ 200
Cdd:cd00398  157 HGLFAWGPTLDEAFHLAVVLEVAAEIQLKALS 188
PRK08130 PRK08130
putative aldolase; Validated
 1-189 2.35e-11

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 60.27  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   1 MTDNLQLTHLVEACRWIGAKGWAPATGGNMSVRQDEHlCWL-SESGKDKGSLTTADFLQVEiATNRAPSGRKPSAETGLH 79
Cdd:PRK08130   1 MTEQALREEIVRLGRSLFQRGYTVGSAGNISARLDDG-GWLvTPTGSCLGRLDPARLSKVD-ADGNWLSGDKPSKEVPLH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  80 TLIYRLFPEANAVLHVHTVNATVLSRL--VNEAEL--KITGFEMQKslTGQTThrdtvAIPVF-DNDQDI-DALASRIAH 153
Cdd:PRK08130  79 RAIYRNNPECGAVVHLHSTHLTALSCLggLDPTNVlpPFTPYYVMR--VGHVP-----LIPYYrPGDPAIaEALAGLAAR 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 550795092 154 YAqerplnyGFLLRGHGLTCWGRDVAEARRHLEGLE 189
Cdd:PRK08130 152 YR-------AVLLANHGPVVWGSSLEAAVNATEELE 180
PRK06755 PRK06755
hypothetical protein; Validated
 45-198 2.02e-10

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 57.73  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  45 GKDKGSLTTADFLQVEIATNRA-PSGRKPSAETGLHTLIYRLfPEANAVLHVHTVNATVLSRLV-NEAELKITGFEMQKS 122
Cdd:PRK06755  48 GRDKGLFSEEDFIVVNCMCEPVfENEEKPAAESFMHADIYKK-SSAECILQVQTVDSHLISELYgEEGEVTFDKRSVERV 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550795092 123 LTGQTTHRDTvaIPVFDNDQDI-DALASRIAHYAQERPLnygFLLRGHGLTCWGRDVAEARRHLEGLEFLFECEMRL 198
Cdd:PRK06755 127 FGKEGITEMT--IPIVEDEKKFaDLLENNVPNFIEGGGV---VLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKL 198
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
26-106 1.84e-09

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 55.14  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  26 TGGNMSV-RQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFPEANAVLHVHTVNATVLS 104
Cdd:PRK06833  26 TGGNISIfNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMHLIFYRNREDINAIVHTHSPYATTLA 105


                 ..
gi 550795092 105 RL 106
Cdd:PRK06833 106 CL 107
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 26-181 1.51e-08

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 52.81  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  26 TGGNMSVRQDEH-LCWLSESGKDKGSLTTADFLQVEIATNRAPSG-RKPSAETGLHTLIYRLFPEANAVLHVHTVNATVL 103
Cdd:PRK13213  25 TWGNVSGIDREHgLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGdKKPSSDTDTHLVLYRAFAEIGGIVHTHSRHATIW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092 104 SrlvneaelkitgfEMQKSLTG-QTTHRDTVAIPV----------FDNDQDIDALASRIAHYAQE--RPLNY-GFLLRGH 169
Cdd:PRK13213 105 A-------------QAGKSLSAlGTTHADYFYGPIpctrlmteaeITGDYEHETGKVIVETFAEQglRAADIpAVLVNGH 171

                        170
                 ....*....|..
gi 550795092 170 GLTCWGRDVAEA 181
Cdd:PRK13213 172 GPFAWGSNAANA 183
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
44-181 2.30e-08

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 52.14  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  44 SGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFPEANAVLHVHTVNATVLSrlvnEAELKITGFemqksl 123
Cdd:PRK08193  44 SGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHLVLYKAFPEIGGIVHTHSRHATAWA----QAGRDIPAL------ 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550795092 124 tGqTTHRDTV--AIPVFD--NDQDIDA-----LASRIAHYAQERPLNY----GFLLRGHGLTCWGRDVAEA 181
Cdd:PRK08193 114 -G-TTHADYFygDIPCTRkmTDEEINGeyeweTGKVIVETFEKRGIDPaavpGVLVHSHGPFTWGKDAEDA 182
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 26-105 2.41e-08

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 52.13  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  26 TGGNMS-VRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSG-RKPSAETGLHTLIYRLFPEANAVLHVHTVNATVL 103
Cdd:PRK12347  25 TWGNVSaVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGsKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIW 104


                 ..
gi 550795092 104 SR 105
Cdd:PRK12347 105 SQ 106
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 26-102 4.02e-08

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 51.55  E-value: 4.02e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550795092  26 TGGNMSVR-QDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFPEANAVLHVHTVNATV 102
Cdd:PRK06557  31 TSGNVSARdPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLKPSSDTASHLYVYRHMPDVGGVVHTHSTYATA 108
PRK08333 PRK08333
aldolase;
10-114 4.98e-08

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 50.98  E-value: 4.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  10 LVEACRWIGAKGWAPATGGNMSVRQDEhLCWLSESGKDKGSLTTADFLQVEIATNRApSGRKPSAETGLHTLIYRLFPEA 89
Cdd:PRK08333   8 LVKYSKLAHERGLTAAFGGNLSIRVGN-LVFIKATGSVMDELTREQVAVIDLNGNQL-SSVRPSSEYRLHLAVYRNRPDV 85

                         90       100
                 ....*....|....*....|....*
gi 550795092  90 NAVLHVHTVNATVLSRLVnEAELKI 114
Cdd:PRK08333  86 RAIAHLHPPYSIVASTLL-EEELPI 109
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 20-104 5.36e-08

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 51.18  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  20 KGWAPATGGNMSVRQDEHLCWLSESGKDKGSLTTADFLQVEIATN--RAPSGRKPSAETGLHTLIYRLFPEANAVLHVHT 97
Cdd:PRK05874  21 RGLVEGTAGNISARRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAvlHAKDGRSPSTELNLHLACYRAFDDIGSVIHSHP 100


                 ....*..
gi 550795092  98 VNATVLS 104
Cdd:PRK05874 101 VWATMFA 107
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
10-106 9.22e-08

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 50.51  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  10 LVEACRWIGAKGWAPATGGNMSVR-QDEHLcwLSESGKDKGSLTTADFLQVEiATNRAPSGRKPSAETGLHTLIYRLFPE 88
Cdd:PRK08087  10 IIDTCLEMTRLGLNQGTAGNVSVRyQDGML--ITPTGIPYEKLTESHIVFVD-GNGKHEEGKLPSSEWRFHMAAYQTRPD 86

                         90
                 ....*....|....*...
gi 550795092  89 ANAVLHVHTVNATVLSRL 106
Cdd:PRK08087  87 ANAVVHNHAVHCTAVSIL 104
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 26-181 5.85e-07

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 48.26  E-value: 5.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  26 TGGNMS-VRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAETGLHTLIYRLFPEANAVLHVHTVNATVLS 104
Cdd:PRK12348  24 TWGNVSaIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLELYRRYPSLGGIVHTHSTHATAWA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092 105 rlvnEAELKITGFemqksltgQTTHRDTV--AIPVFD--NDQDIDALASR------IAHYAQERPLNY-GFLLRGHGLTC 173
Cdd:PRK12348 104 ----QAGLAIPAL--------GTTHADYFfgDIPCTRglSEEEVQGEYELntgkviIETLGNAEPLHTpGIVVYQHGPFA 171


                 ....*...
gi 550795092 174 WGRDVAEA 181
Cdd:PRK12348 172 WGKDAHDA 179
PRK08660 PRK08660
aldolase;
28-181 7.64e-06

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 44.56  E-value: 7.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  28 GNMSVRQDEHLcWLSESGKDKGSLTTADFLQVEIaTNRAPSGRKPSAETGLHTLIYRLFPeANAVLHVHTVNATVLSRLv 107
Cdd:PRK08660  23 GNISVRTGDGL-LITRTGSMLDEITEGDVIEVGI-DDDGSVDPLASSETPVHRAIYRRTS-AKAIVHAHPPYAVALSLL- 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550795092 108 nEAELKITGFEMQKSLTgqtthrdtvAIPVFDNDQDIDALASRIAHYAQERplnYGFLLRGHGLTCWGRDVAEA 181
Cdd:PRK08660  99 -EDEIVPLDSEGLYFLG---------TIPVVGGDIGSGELAENVARALSEH---KGVVVRGHGTFAIGKTLEEA 159
PRK07490 PRK07490
hypothetical protein; Provisional
 10-201 4.42e-04

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 40.09  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  10 LVEACRWIGAKGWAPATGGNMS--VRQDEHLCWLSESGKDKGSLTTADFLQVEIATNRAPSGRKPSAET--GLHTLIYRL 85
Cdd:PRK07490  15 LAAAFRWIARLGMHEAVANHFSaaVSADGKQFLLNPKWKHFSRIRASDLLLLDADDPSTAERPDVPDATawAIHGQIHRR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  86 FPEANAVLHVHTVNATVLSRLVNEAELKITgfemqksltgQTTHRdtvaipvFDNDQDIDAL---------ASRIAHYAQ 156
Cdd:PRK07490  95 LPHARCVMHVHSVYATALACLADPTLPPID----------QNTAR-------FFNRVAVDTLyggmaleeeGERLAGLLG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 550795092 157 ERPLnygFLLRGHGLTCWGRDVAEARRHLegleFLFE--CEMRLRQW 201
Cdd:PRK07490 158 DKRR---LLMGNHGVLVTGDTVAEAFDDL----YYFEraCQTYITAL 197
PRK06661 PRK06661
hypothetical protein; Provisional
 78-186 2.49e-03

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 37.50  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092  78 LHTLIYRLFPEANAVLHVHTVNATVLSRLvNEAELKITGFemqksltgqtthrdtvAIPVFDNDQ---------DIDALA 148
Cdd:PRK06661  78 IHGSIYKTRPDISAIFHYHTPASIAVSAL-KCGLLPISQW----------------ALHFYDRISyhnynslalDADKQS 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 550795092 149 SRIAHYAQErplNYGFLLRGHGLTCWGRDVAEA---RRHLE 186
Cdd:PRK06661 141 SRLVNDLKQ---NYVMLLRNHGAITCGKTIHEAmfyTYHLE 178
PRK06208 PRK06208
class II aldolase/adducin family protein;
9-106 5.66e-03

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 36.89  E-value: 5.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550795092   9 HLVEACRWIGAKGWAPATGGNMSVRQDEH--LCWLSESGKDKGSLTTADFLQV----EIATNRAPSGRkpsAETGLHTLI 82
Cdd:PRK06208  46 RLAAAFRLFARFGFDEGLAGHITARDPELpdHFWVNPLGVHFSQIKVSDLLLVdhdgEVVEGDRPLNR---AAFAIHSAI 122

                         90       100
                 ....*....|....*....|....
gi 550795092  83 YRLFPEANAVLHVHTVNATVLSRL 106
Cdd:PRK06208 123 HEARPDVVAAAHTHSTYGKAWSTL 146
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH