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Conserved domains on  [gi|501066199|ref|WP_012117414|]
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MULTISPECIES: methylthioribulose 1-phosphate dehydratase [Bacillus amyloliquefaciens group]

Protein Classification

methylthioribulose 1-phosphate dehydratase( domain architecture ID 10012806)

methylthioribulose 1-phosphate dehydratase catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P)

CATH:  3.40.225.10
EC:  4.2.1.109
Gene Ontology:  GO:0046570|GO:0008270
PubMed:  15102328

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
1-209 4.94e-144

methylthioribulose 1-phosphate dehydratase;


:

Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 399.43  E-value: 4.94e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   1 MAAKEERWRELAEVKRELAERDWFPATSGNLSIKVSDGPLTFLVTASGKDKRKETDEDFLLIDEYGKPAETgHSLKPSAE 80
Cdd:PRK06754   1 MKQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEE-TELKPSAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  81 TLLHTYLYQKTDAGCCLHVHTVNNNVISELYGDEKQITFQGQEMIKALGLWEENASVTVPIIDNPAHIPALAENFAHHAA 160
Cdd:PRK06754  80 TLLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKALGIWEENAEIHIPIIENHADIPTLAEEFAKHIQ 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 501066199 161 AGSGAVLIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLRPQLVK 209
Cdd:PRK06754 160 GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQGGVSK 208
 
Name Accession Description Interval E-value
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
1-209 4.94e-144

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 399.43  E-value: 4.94e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   1 MAAKEERWRELAEVKRELAERDWFPATSGNLSIKVSDGPLTFLVTASGKDKRKETDEDFLLIDEYGKPAETgHSLKPSAE 80
Cdd:PRK06754   1 MKQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEE-TELKPSAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  81 TLLHTYLYQKTDAGCCLHVHTVNNNVISELYGDEKQITFQGQEMIKALGLWEENASVTVPIIDNPAHIPALAENFAHHAA 160
Cdd:PRK06754  80 TLLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKALGIWEENAEIHIPIIENHADIPTLAEEFAKHIQ 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 501066199 161 AGSGAVLIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLRPQLVK 209
Cdd:PRK06754 160 GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQGGVSK 208
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 11-203 6.04e-91

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: 264.51  E-value: 6.04e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   11 LAEVKRELAERDWFPATSGNLSIKVSdgPLTFLVTASGKDKRKETDEDFLLIDEYGKPAETGhsLKPSAETLLHTYLYQK 90
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGG--LKPSAETLLHTQLYRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   91 TDAGCCLHVHTVNNNVISELYGDEKQITFQGQEMIKAL-GLWEENASVTVPIIDNPAHIPALAENFAHHAAAGSGA--VL 167
Cdd:TIGR03328  77 TGAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGLpGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVpgVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 501066199  168 IRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSL 203
Cdd:TIGR03328 157 IRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-198 2.48e-45

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: 148.46  E-value: 2.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199    9 RELAEVKRELAERDWFPATSGNLSIKVSDGplTFLVTASGKDKRKETDEDFLLIDEYGKPAETGhsLKPSAETLLHTYLY 88
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGD--GFLITPSGVDFGELTPEDLVVVDLDGNVVEGG--LKPSSETPLHLAIY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   89 QK-TDAGCCLHVHTVNNNVISELygdEKQITFQGQEMIKALGLweenasvTVPIIDN-PAHIPALAENFAHHAAAGSGAV 166
Cdd:pfam00596  77 RArPDAGAVVHTHSPYATALSLA---KEGLPPITQEAADFLGG-------DIPIIPYyTPGTEELGERIAEALGGDRKAV 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 501066199  167 LIRNHGITAWGRTAFEAKRVLEAYEFLFSCHL 198
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 5-208 9.08e-45

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: 147.67  E-value: 9.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   5 EERWRELAEVKRELAERDWFPATSGNLSIKVSDGplTFLVTASGKDKRKETDEDFLLIDEYGKPAETGHslKPSAETLLH 84
Cdd:COG0235    4 EELREELAAAGRRLARRGLVDGTAGNISVRLDDD--RFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL--KPSSETPLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  85 TYLYQK-TDAGCCLHVHTVNNNVISELyGDEkqitFQGQEMIKALGLWEEnasvtVPIID-NPAHIPALAENFAHHAAAG 162
Cdd:COG0235   80 LAIYRArPDVGAVVHTHSPYATALSAL-GEP----LPPLEQTEAAAFLGD-----VPVVPyAGPGTEELAEAIAEALGDR 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 501066199 163 SGaVLIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLRPQLV 208
Cdd:COG0235  150 PA-VLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV 194
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 11-198 1.45e-43

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: 143.93  E-value: 1.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199    11 LAEVKRELAERDWFPATSGNLSIKVSDgPLTFLVTASGKDKRKETDEDFLLIDEYGKPAETGHSLKPSAETLLHTYLYQK 90
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGE-EDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGPKPSSETPLHLAIYRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199    91 T-DAGCCLHVHTVNNNVISELygdEKQITFQGQEMIKALGLWE-ENASVTVPIIDNPAHIPALAENFaHHAAAGSGAVLI 168
Cdd:smart01007  80 RpDVGAVVHTHSPYATALAAL---GKPLPLLPTEQAAAFLGGEiPYAPYAGPGTELAEEGAELAEAL-AEALPDRPAVLL 155

                          170       180       190
                   ....*....|....*....|....*....|
gi 501066199   169 RNHGITAWGRTAFEAKRVLEAYEFLFSCHL 198
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 9-207 3.06e-18

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: 78.95  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   9 RELAEVKRELAERDWFPATSGNLSIKVSDGPLtFLVTASGKDKRKETDEDFLLIDEYGKPAETGhslKPSAETLLHTYLY 88
Cdd:cd00398    5 RKIIAACLLLDLYGWVTGTGGNVSARDRDRGY-FLITPSGVDYEEMTASDLVVVDAQGKVVEGK---KPSSETPLHLALY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  89 Q-KTDAGCCLHVHTVNNNVISELygdekqitfqGQEMIKALGlweenasvTVPIIDNPAHIPALA-----------ENFA 156
Cdd:cd00398   81 RaRPDIGCIVHTHSTHATAVSQL----------KEGLIPAGH--------TACAVYFTGDIPCTPymtpetgedeiGTQR 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501066199 157 HHAAAGSGAVLIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLRPQL 207
Cdd:cd00398  143 ALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQL 193
 
Name Accession Description Interval E-value
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
1-209 4.94e-144

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 399.43  E-value: 4.94e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   1 MAAKEERWRELAEVKRELAERDWFPATSGNLSIKVSDGPLTFLVTASGKDKRKETDEDFLLIDEYGKPAETgHSLKPSAE 80
Cdd:PRK06754   1 MKQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEE-TELKPSAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  81 TLLHTYLYQKTDAGCCLHVHTVNNNVISELYGDEKQITFQGQEMIKALGLWEENASVTVPIIDNPAHIPALAENFAHHAA 160
Cdd:PRK06754  80 TLLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKALGIWEENAEIHIPIIENHADIPTLAEEFAKHIQ 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 501066199 161 AGSGAVLIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLRPQLVK 209
Cdd:PRK06754 160 GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQGGVSK 208
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 11-203 6.04e-91

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: 264.51  E-value: 6.04e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   11 LAEVKRELAERDWFPATSGNLSIKVSdgPLTFLVTASGKDKRKETDEDFLLIDEYGKPAETGhsLKPSAETLLHTYLYQK 90
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGG--LKPSAETLLHTQLYRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   91 TDAGCCLHVHTVNNNVISELYGDEKQITFQGQEMIKAL-GLWEENASVTVPIIDNPAHIPALAENFAHHAAAGSGA--VL 167
Cdd:TIGR03328  77 TGAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGLpGITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVpgVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 501066199  168 IRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSL 203
Cdd:TIGR03328 157 IRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
5-206 1.68e-58

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 182.83  E-value: 1.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   5 EERWRELAEVKRELAERDWFPATSGNLSIKVSDGplTFLVTASGKDKRKETDEDFLLIDEYGKPAETGHslKPSAETLLH 84
Cdd:PRK09220   4 EELLQQLIAAGRWIGARGWVPATSGNMSVRLDEQ--HCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGR--KPSAETLLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  85 TYLY-QKTDAGCCLHVHTVNNNVISELygdEKQ--ITFQGQEMIKAL-GLWEENASVTVPIIDNPAHIPALAENFAHHAA 160
Cdd:PRK09220  80 TQLYrLFPEIGAVLHTHSVNATVLSRV---EKSdaLVLEGYELQKAFaGQTTHETAVVVPIFDNDQDIARLAARVAPYLD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 501066199 161 AGSGAV--LIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLRPQ 206
Cdd:PRK09220 157 AQPLRYgyLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLLEAK 204
PRK06755 PRK06755
hypothetical protein; Validated
 6-204 1.27e-46

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 152.88  E-value: 1.27e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   6 ERWRELAEVKRELAERDWFPATSGNLSIKVSDGPLTFLVTASGKDKRKETDEDFLLIDEYGKPAETGHSlKPSAETLLHT 85
Cdd:PRK06755   6 KKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCEPVFENEE-KPAAESFMHA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  86 YLYQKTDAGCCLHVHTVNNNVISELYGDEKQITFQGQEMIKALGLwEENASVTVPIIDNPAHIPALAENFAHHAAAGSGA 165
Cdd:PRK06755  85 DIYKKSSAECILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGK-EGITEMTIPIVEDEKKFADLLENNVPNFIEGGGV 163

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 501066199 166 VLIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLR 204
Cdd:PRK06755 164 VLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIK 202
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-198 2.48e-45

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: 148.46  E-value: 2.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199    9 RELAEVKRELAERDWFPATSGNLSIKVSDGplTFLVTASGKDKRKETDEDFLLIDEYGKPAETGhsLKPSAETLLHTYLY 88
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGD--GFLITPSGVDFGELTPEDLVVVDLDGNVVEGG--LKPSSETPLHLAIY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   89 QK-TDAGCCLHVHTVNNNVISELygdEKQITFQGQEMIKALGLweenasvTVPIIDN-PAHIPALAENFAHHAAAGSGAV 166
Cdd:pfam00596  77 RArPDAGAVVHTHSPYATALSLA---KEGLPPITQEAADFLGG-------DIPIIPYyTPGTEELGERIAEALGGDRKAV 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 501066199  167 LIRNHGITAWGRTAFEAKRVLEAYEFLFSCHL 198
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 5-208 9.08e-45

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: 147.67  E-value: 9.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   5 EERWRELAEVKRELAERDWFPATSGNLSIKVSDGplTFLVTASGKDKRKETDEDFLLIDEYGKPAETGHslKPSAETLLH 84
Cdd:COG0235    4 EELREELAAAGRRLARRGLVDGTAGNISVRLDDD--RFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL--KPSSETPLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  85 TYLYQK-TDAGCCLHVHTVNNNVISELyGDEkqitFQGQEMIKALGLWEEnasvtVPIID-NPAHIPALAENFAHHAAAG 162
Cdd:COG0235   80 LAIYRArPDVGAVVHTHSPYATALSAL-GEP----LPPLEQTEAAAFLGD-----VPVVPyAGPGTEELAEAIAEALGDR 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 501066199 163 SGaVLIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLRPQLV 208
Cdd:COG0235  150 PA-VLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV 194
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 11-198 1.45e-43

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: 143.93  E-value: 1.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199    11 LAEVKRELAERDWFPATSGNLSIKVSDgPLTFLVTASGKDKRKETDEDFLLIDEYGKPAETGHSLKPSAETLLHTYLYQK 90
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGE-EDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGPKPSSETPLHLAIYRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199    91 T-DAGCCLHVHTVNNNVISELygdEKQITFQGQEMIKALGLWE-ENASVTVPIIDNPAHIPALAENFaHHAAAGSGAVLI 168
Cdd:smart01007  80 RpDVGAVVHTHSPYATALAAL---GKPLPLLPTEQAAAFLGGEiPYAPYAGPGTELAEEGAELAEAL-AEALPDRPAVLL 155

                          170       180       190
                   ....*....|....*....|....*....|
gi 501066199   169 RNHGITAWGRTAFEAKRVLEAYEFLFSCHL 198
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 9-207 3.06e-18

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: 78.95  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   9 RELAEVKRELAERDWFPATSGNLSIKVSDGPLtFLVTASGKDKRKETDEDFLLIDEYGKPAETGhslKPSAETLLHTYLY 88
Cdd:cd00398    5 RKIIAACLLLDLYGWVTGTGGNVSARDRDRGY-FLITPSGVDYEEMTASDLVVVDAQGKVVEGK---KPSSETPLHLALY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  89 Q-KTDAGCCLHVHTVNNNVISELygdekqitfqGQEMIKALGlweenasvTVPIIDNPAHIPALA-----------ENFA 156
Cdd:cd00398   81 RaRPDIGCIVHTHSTHATAVSQL----------KEGLIPAGH--------TACAVYFTGDIPCTPymtpetgedeiGTQR 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501066199 157 HHAAAGSGAVLIRNHGITAWGRTAFEAKRVLEAYEFLFSCHLKLLSLRPQL 207
Cdd:cd00398  143 ALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQL 193
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 16-102 2.97e-07

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 49.26  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  16 RELAERDWFPATSGNLSIKVSDGPLtfLVTASGKDKRKETDEDFLLIDEYGKPAETGHSLKPSAETLLHTYLYQK-TDAG 94
Cdd:PRK05874  16 KDMLRRGLVEGTAGNISARRSDGNV--VITPSSVDYAEMLLHDLVLVDAGGAVLHAKDGRSPSTELNLHLACYRAfDDIG 93


                 ....*...
gi 501066199  95 CCLHVHTV 102
Cdd:PRK05874  94 SVIHSHPV 101
PRK08660 PRK08660
aldolase;
8-183 3.00e-07

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 48.80  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   8 WRELAEVKRELAERDWFPATSGNLSIKVSDGpltFLVTASGK--DKRKETDEDFLLIDEYGkpaetghSLKP--SAETLL 83
Cdd:PRK08660   2 WQEFARIGKKLFAHGLVSSHFGNISVRTGDG---LLITRTGSmlDEITEGDVIEVGIDDDG-------SVDPlaSSETPV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  84 HTYLYQKTDAGCCLHVHTVNNNVISELygdEKQITFQGQEMIKALGlweenasvTVPIIDNPAHIPALAENfAHHAAAGS 163
Cdd:PRK08660  72 HRAIYRRTSAKAIVHAHPPYAVALSLL---EDEIVPLDSEGLYFLG--------TIPVVGGDIGSGELAEN-VARALSEH 139

                        170       180
                 ....*....|....*....|
gi 501066199 164 GAVLIRNHGITAWGRTAFEA 183
Cdd:PRK08660 140 KGVVVRGHGTFAIGKTLEEA 159
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 10-101 5.16e-07

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 48.47  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  10 ELAEVKRELAERD----------WfpaTSGNLSIKVSDGPLtFLVTASGKDKRKETDEDFLLIDEYGKPAETghSLKPSA 79
Cdd:PRK06557   7 MVEKLREEVCKLHlelpkyglvvW---TSGNVSARDPGTDL-VVIKPSGVSYDDLTPEDMVVVDLDGNVVEG--DLKPSS 80

                         90       100
                 ....*....|....*....|...
gi 501066199  80 ETLLHTYLYQK-TDAGCCLHVHT 101
Cdd:PRK06557  81 DTASHLYVYRHmPDVGGVVHTHS 103
PRK08333 PRK08333
aldolase;
9-183 2.36e-03

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 37.49  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199   9 RELAEVKRELAERDWFPATSGNLSIKVsdGPLTFlVTASGKDKRKETDEDFLLIDEYGKPAEtghSLKPSAETLLHTYLY 88
Cdd:PRK08333   6 AQLVKYSKLAHERGLTAAFGGNLSIRV--GNLVF-IKATGSVMDELTREQVAVIDLNGNQLS---SVRPSSEYRLHLAVY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  89 Q-KTDAGCCLHVHTVNNNVISELYGDE-KQITFQGQEMIKalglweenasvTVPIID-NPAHIPALAENfAHHAAAGSGA 165
Cdd:PRK08333  80 RnRPDVRAIAHLHPPYSIVASTLLEEElPIITPEAELYLK-----------KIPILPfRPAGSVELAEQ-VAEAMKEYDA 147

                        170
                 ....*....|....*...
gi 501066199 166 VLIRNHGITAWGRTAFEA 183
Cdd:PRK08333 148 VIMERHGIVTVGRSLREA 165
PRK07490 PRK07490
hypothetical protein; Provisional
 10-110 8.51e-03

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 36.24  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066199  10 ELAEVKRELAERDWFPATSGNLSIKVSDGPLTFLVTASGKDKRKETDEDFLLID-EYGKPAETGHSLKPSAETLlHTYLY 88
Cdd:PRK07490  14 DLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLDaDDPSTAERPDVPDATAWAI-HGQIH 92

                         90       100
                 ....*....|....*....|...
gi 501066199  89 QKT-DAGCCLHVHTVNNNVISEL 110
Cdd:PRK07490  93 RRLpHARCVMHVHSVYATALACL 115
 
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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