NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1313375691|dbj|GBE53970|]
View 

4-hydroxy-tetrahydrodipicolinate synthase [archaeon BMS3Bbin15]

Protein Classification

dihydrodipicolinate synthase family protein( domain architecture ID 10001092)

dihydrodipicolinate synthase family protein belongs to the pyruvate-dependent class I aldolases, similar to 4-hydroxy-tetrahydrodipicolinate synthase which catalyzes a key step in lysine biosynthesis, the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residu

CATH:  3.20.20.70
EC:  4.-.-.-
Gene Ontology:  GO:0071704|GO:0016829
PubMed:  9047371

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 2-288 4.29e-102

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


:

Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 299.76  E-value: 4.29e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   2 KLKGIYCPMITPF-KNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGATSM 78
Cdd:COG0329     1 KFRGVIPALVTPFdADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAgrVPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:COG0329    81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIV 237
Cdd:COG0329   161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAgDLAEARALQDRLLPLI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKKMEV 288
Cdd:COG0329   241 RALFAEGNPAPVKAALALLGLPSG-PVRLPLLPLSEEERAELRAALKELGL 290
 
Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 2-288 4.29e-102

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 299.76  E-value: 4.29e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   2 KLKGIYCPMITPF-KNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGATSM 78
Cdd:COG0329     1 KFRGVIPALVTPFdADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAgrVPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:COG0329    81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIV 237
Cdd:COG0329   161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAgDLAEARALQDRLLPLI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKKMEV 288
Cdd:COG0329   241 RALFAEGNPAPVKAALALLGLPSG-PVRLPLLPLSEEERAELRAALKELGL 290
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 6-283 2.51e-94

Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.


Pssm-ID: 188630 [Multi-domain]  Cd Length: 281  Bit Score: 279.82  E-value: 2.51e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   6 IYCPMITPFKNGG-IDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMRMEE 82
Cdd:cd00408     1 VIPALVTPFTADGeVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVagRVPVIAGVGANSTRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  83 ALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIKDTS 162
Cdd:cd00408    81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 163 GDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIVKIMD 241
Cdd:cd00408   161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAgDLEEARALQDRLLPLIEALF 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1313375691 242 TGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLL 283
Cdd:cd00408   241 KEGNPAPVKAALALLGLDAG-PVRLPLVPLSEEERAKLEALL 281
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 5-285 2.81e-73

4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129757 [Multi-domain]  Cd Length: 285  Bit Score: 226.44  E-value: 2.81e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   5 GIYCPMITPFK-NGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMRME 81
Cdd:TIGR00674   1 GVITALITPFKeDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVngRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  82 EALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIKDT 161
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 162 SGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNIVKIM 240
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNAlEGDFAEAREIHQKLMPLHKAL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1313375691 241 DTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEG-ELRLPLTELSEEHRNKLRDVLKD 284
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 2-284 2.33e-72

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 224.17  E-value: 2.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   2 KLKGIYCPMITPFKN-GGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDT--TSLPVIAGATSM 78
Cdd:pfam00701   1 KFSGIITALVTPFDTdGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEakGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNIV 237
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALkNGDLATAALINHKLLPLI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGDDVRAPLLNLTSEEKDTVDGLLK 284
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILK 287
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 1-285 3.32e-39

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 138.97  E-value: 3.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   1 MKLKGIYCPMITPF-KNGGIDLEGLEKNIAF-LEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGAT 76
Cdd:PRK04147    2 KNLKGVYAALLTPFdEDGQIDEQGLRRLVRFnIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKgkVKLIAQVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  77 SMRMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNII 156
Cdd:PRK04147   82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 157 GIKDTSGDMKKFQVIVNLVPeDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMN 235
Cdd:PRK04147  162 GVKQTAGDLYQLERIRKAFP-DKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAgDIQEAQELQHECND 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 236 IV-KIMDTGTFPaGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:PRK04147  241 VIdLLIKNGVYP-GLKEILHYMGVDAG-LCRKPFKPVDEKYLPALKALAAK 289
 
Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 2-288 4.29e-102

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 299.76  E-value: 4.29e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   2 KLKGIYCPMITPF-KNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGATSM 78
Cdd:COG0329     1 KFRGVIPALVTPFdADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAgrVPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:COG0329    81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIV 237
Cdd:COG0329   161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAgDLAEARALQDRLLPLI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKKMEV 288
Cdd:COG0329   241 RALFAEGNPAPVKAALALLGLPSG-PVRLPLLPLSEEERAELRAALKELGL 290
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 6-283 2.51e-94

Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.


Pssm-ID: 188630 [Multi-domain]  Cd Length: 281  Bit Score: 279.82  E-value: 2.51e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   6 IYCPMITPFKNGG-IDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMRMEE 82
Cdd:cd00408     1 VIPALVTPFTADGeVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVagRVPVIAGVGANSTRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  83 ALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIKDTS 162
Cdd:cd00408    81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 163 GDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIVKIMD 241
Cdd:cd00408   161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAgDLEEARALQDRLLPLIEALF 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1313375691 242 TGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLL 283
Cdd:cd00408   241 KEGNPAPVKAALALLGLDAG-PVRLPLVPLSEEERAKLEALL 281
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 3-280 1.25e-80

Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.


Pssm-ID: 188637 [Multi-domain]  Cd Length: 284  Bit Score: 245.10  E-value: 1.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   3 LKGIYCPMITPFKNGG-IDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMR 79
Cdd:cd00950     1 FGGSITALVTPFKDDGsVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVngRVPVIAGTGSNN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  80 MEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIK 159
Cdd:cd00950    81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 160 DTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMNIVK 238
Cdd:cd00950   161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAgDLEKARELHRKLLPLIK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1313375691 239 IMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVD 280
Cdd:cd00950   241 ALFAEPNPIPVKAALALLGLISG-ELRLPLVPLSEELRAKLR 281
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 5-285 2.81e-73

4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129757 [Multi-domain]  Cd Length: 285  Bit Score: 226.44  E-value: 2.81e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   5 GIYCPMITPFK-NGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGATSMRME 81
Cdd:TIGR00674   1 GVITALITPFKeDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVngRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  82 EALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGIKDT 161
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 162 SGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNIVKIM 240
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNAlEGDFAEAREIHQKLMPLHKAL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1313375691 241 DTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:TIGR00674 241 FIETNPIPVKTALALLGLIEG-ELRLPLTELSEEHRNKLRDVLKD 284
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 2-284 2.33e-72

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 224.17  E-value: 2.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   2 KLKGIYCPMITPFKN-GGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDT--TSLPVIAGATSM 78
Cdd:pfam00701   1 KFSGIITALVTPFDTdGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEakGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIGI 158
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 159 KDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNIV 237
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALkNGDLATAALINHKLLPLI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1313375691 238 KIMDTGTFPAGLKYAMNMLDIAGGDDVRAPLLNLTSEEKDTVDGLLK 284
Cdd:pfam00701 241 KILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILK 287
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 3-285 4.53e-50

N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases.


Pssm-ID: 188641 [Multi-domain]  Cd Length: 288  Bit Score: 167.10  E-value: 4.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   3 LKGIYCPMITPF-KNGGIDLEGLEKNIAFL-EKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGATSM 78
Cdd:cd00954     1 LKGLIAALLTPFdENGEINEDVLRAIVDYLiEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKgkVTLIAHVGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  79 RMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLS-SHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNIIG 157
Cdd:cd00954    81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIaAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 158 IKDTSGDMKKFQVIVNLVPEDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTW-ERDIDRAVGLQKLLMNI 236
Cdd:cd00954   161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFnAGDIDTARELQHVINDV 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1313375691 237 VKIMDTGTFPAGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:cd00954   241 ITVLIKNGLYPTLKAILRLMGLDAG-PCRLPLRKVTEKALAKAKELAAK 288
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 1-285 3.32e-39

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 138.97  E-value: 3.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   1 MKLKGIYCPMITPF-KNGGIDLEGLEKNIAF-LEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGAT 76
Cdd:PRK04147    2 KNLKGVYAALLTPFdEDGQIDEQGLRRLVRFnIEKQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKgkVKLIAQVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  77 SMRMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNIPVFTGNPFLPPLVKRLSVLDNII 156
Cdd:PRK04147   82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 157 GIKDTSGDMKKFQVIVNLVPeDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRTWER-DIDRAVGLQKLLMN 235
Cdd:PRK04147  162 GVKQTAGDLYQLERIRKAFP-DKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAgDIQEAQELQHECND 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 236 IV-KIMDTGTFPaGLKYAMNMLDIAGGdDVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:PRK04147  241 VIdLLIKNGVYP-GLKEILHYMGVDAG-LCRKPFKPVDEKYLPALKALAAK 289
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 9-287 4.66e-34

KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases.


Pssm-ID: 188640  Cd Length: 279  Bit Score: 124.80  E-value: 4.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   9 PMITPFKNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTSlPVIAGATSMRMEEALEIIA 88
Cdd:cd00953     7 PVITPFTGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD-KVIFQVGSLNLEESIELAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  89 YSADMGAEAALVAPPYYF-RTSQEGLFSYYSNLSSHstLPIILYNIPVFTGNPFLPPLVKRL-SVLDNIIGIKDTSGDMK 166
Cdd:cd00953    86 AAKSFGIYAIASLPPYYFpGIPEEWLIKYFTDISSP--YPTFIYNYPKATGYDINARMAKEIkKAGGDIIGVKDTNEDIS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 167 KFQVIVNLVPeDFSCLIGADHLLLPALVTGASGAILGSSNLVPDIPVGIYRtwERDIDRAVGLQKLLMNIVKIMDT-GTF 245
Cdd:cd00953   164 HMLEYKRLVP-DFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKD--HVAIEDAFKLQFLINEVLDASRKyGSW 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1313375691 246 PAGLKYAMNMLDIAGGDDvRAPLLNLTSEEKDTvdgLLKKME 287
Cdd:cd00953   241 SANYSLVKIFQGYDAGEP-RPPFYPLDEEEEEK---LRKEVN 278
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 11-286 7.30e-31

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 117.22  E-value: 7.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  11 ITPFK-NGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTT--SLPVIAGA---TSMrmeeAL 84
Cdd:PRK03620   16 VTPFDaDGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTagRVPVIAGAgggTAQ----AI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  85 EIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYN--IPVFTgnpflPPLVKRLS-VLDNIIGIKDT 161
Cdd:PRK03620   92 EYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNrdNAVLT-----ADTLARLAeRCPNLVGFKDG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 162 SGDMKKFQVIVNLVPEDFSCLIGadhllLP-ALVTGASGAILG----SS---NLVPDIPVGIYRTWERDIDRAVG--LQK 231
Cdd:PRK03620  167 VGDIELMQRIVRALGDRLLYLGG-----LPtAEVFAAAYLALGvptySSavfNFVPEIALAFYRALRAGDHATVDrlLDD 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1313375691 232 LLMNIVKIMDTGtfpAGlkYAMNM----LDIAGGD--DVRAPLLNLTSEEKDTVDGLLKKM 286
Cdd:PRK03620  242 FFLPYVALRNRK---KG--YAVSIvkagARLVGLDagPVRAPLTDLTPEELAELAALIAKG 297
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 11-285 2.87e-29

5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH); 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH), which is member of dihydrodipicolinate synthase (DHDPS) family that comprises several pyruvate-dependent class I aldolases. The enzyme is involved in glucarate metabolism, and its mechanism presumbly involves a Schiff-base intermediate similar to members of DHDPS family. While in the case of Pseudomonas sp. 5-dehydro-4-deoxy-D-glucarate is degraded by KDGDH to 2,5-dioxopentanoate, in certain species of Enterobacteriaceae it is degraded instead to pyruvate and glycerate.


Pssm-ID: 188638  Cd Length: 289  Bit Score: 112.42  E-value: 2.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  11 ITPFK-NGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVIAGA---TSMrmeeAL 84
Cdd:cd00951     9 VTHFDaDGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAgrVPVLAGAgygTAT----AI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  85 EIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSSHSTLPIILYNipvfTGNPFLPP-LVKRLS-VLDNIIGIKDTS 162
Cdd:cd00951    85 AYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN----RANAVLTAdSLARLAeRCPNLVGFKDGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 163 GDMKKFQVIVNLVPEDFSCLIGAD------HLLLPALVTGASGAIlgsSNLVPDIPVGIYRTWeRDIDRAVGLQKLLMNI 236
Cdd:cd00951   161 GDIELMRRIVAKLGDRLLYLGGLPtaevfaLAYLAMGVPTYSSAV---FNFVPEIALAFYAAV-RAGDHATVKRLLRDFF 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1313375691 237 VKIMDTGTFPAGlkYAMNM----LDIAGGD--DVRAPLLNLTSEEKDTVDGLLKK 285
Cdd:cd00951   237 LPYVDIRNRRKG--YAVSIvkagARLVGRDagPVRPPLTDLTEEELAQLTALIKT 289
PLN02417 PLN02417
dihydrodipicolinate synthase
 1-285 5.48e-28

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 108.96  E-value: 5.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   1 MKLkGIYCPMITPF-KNGGIDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDT--TSLPVIAGATS 77
Cdd:PLN02417    1 KKL-RLITAIKTPYlPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCfgGKIKVIGNTGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  78 MRMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSnlsshSTL---PIILYNIPVFTGNPFLPPLVKRLSVLDN 154
Cdd:PLN02417   80 NSTREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFE-----TVLdmgPTIIYNVPGRTGQDIPPEVIFKIAQHPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691 155 IIGIKDTSGDMKkfqvIVNLVPEDFSCLIGADHLLLPA-LVTGASGAILGSSNLVPDIpvgiyrtwERDIDRAV---GLQ 230
Cdd:PLN02417  155 FAGVKECTGNDR----VKQYTEKGILLWSGNDDECHDArWDYGADGVISVTSNLVPGL--------MHKLMFAGknkELN 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1313375691 231 KLLMNIVKIMDTGTFPAGLKYAMNMLDIAggDDV-RAPLLNLTSEEKDTVDGLLKK 285
Cdd:PLN02417  223 DKLLPLMDWLFCEPNPIGLNTALAQLGLI--RPVfRLPYVPLDLAKRAEFVALVKA 276
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 3-203 1.20e-12

Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA); Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). HBPHA catalyzes HBP to salicyaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. CBPHA is homologous to HBPHA and catalyzes the cleavage of CBP to 2-carboxylbenzaldehyde and pyruvate during the degradation of phenanthrene. They are member of the DHDPS family of Schiff-base-dependent class I aldolases.


Pssm-ID: 188639  Cd Length: 309  Bit Score: 67.09  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691   3 LKGIYCPMITPFKNGG--------IDLEGLEKNIAFLEKKEVTGLVPLGSAGEFSGLSIKERKEVIKKVLDTTS--LPVI 72
Cdd:cd00952     2 IKGVWAIVPTPSKPDAsdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAgrVPVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313375691  73 AGATSMRMEEALEIIAYSADMGAEAALVAPPYYFRTSQEGLFSYYSNLSshSTLP---IILY-NIPVFTGnPFLPPLVKR 148
Cdd:cd00952    82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVA--EAVPemaIAIYaNPEAFKF-DFPRAAWAE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1313375691 149 LSVLDNIIGIKDTS------GDMKKFQVIVNLVPEDFSCLIGAdhLLLPALVTGA--SGAILG 203
Cdd:cd00952   159 LAQIPQVVAAKYLGdigallSDLAAVKGRMRLLPLEDDYYAAA--RLFPEEVTAFwsSGAACG 219
 
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