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Conserved domains on  [gi|489192550|ref|WP_003101895|]
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MULTISPECIES: dihydrodipicolinate synthase family protein [Pseudomonas]

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

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List of domain hits

Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
5-292 4.83e-110

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: 320.18  E-value: 4.83e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   5 IHGIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLT 84
Cdd:COG0329    2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  85 TAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMV 164
Cdd:COG0329   82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVGI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 165 KESTGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLL 244
Cdd:COG0329  161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489192550 245 DFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:COG0329  241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
 
Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
5-292 4.83e-110

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: 320.18  E-value: 4.83e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   5 IHGIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLT 84
Cdd:COG0329    2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  85 TAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMV 164
Cdd:COG0329   82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVGI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 165 KESTGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLL 244
Cdd:COG0329  161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489192550 245 DFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:COG0329  241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
8-289 2.11e-99

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: 292.91  E-value: 2.11e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   8 IIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTAK 87
Cdd:cd00408    1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  88 TVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKES 167
Cdd:cd00408   81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLA-EHPNIVGIKDS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 168 TGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDFI 247
Cdd:cd00408  160 SGDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489192550 248 LRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLL 289
Cdd:cd00408  240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
7-292 1.41e-62

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: 199.09  E-value: 1.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550    7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTA 86
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   87 KTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVREVdNVTMVKE 166
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  167 STGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDF 246
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 489192550  247 ILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
7-292 6.45e-60

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 192.58  E-value: 6.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550    7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTA 86
Cdd:pfam00701   4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   87 KTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKE 166
Cdd:pfam00701  84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLA-TNPNIVGIKE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  167 STGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDF 246
Cdd:pfam00701 163 ASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 489192550  247 ILRRGLPTTIKAGLGLSGLEVGA-PRLPVQALDTEGCRYLQGLLEEL 292
Cdd:pfam00701 243 LFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
7-293 2.97e-34

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 126.08  E-value: 2.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSdLTTA 86
Cdd:PRK03620  10 GLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAG-GGTA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  87 KTVRRAQFAESLGAEAVMVLPiSYwkLNEAE---VFQHYRAVGEAIGVPVMLYNNpGTSgiDMSVELILRIVREVDNVTM 163
Cdd:PRK03620  89 QAIEYAQAAERAGADGILLLP-PY--LTEAPqegLAAHVEAVCKSTDLGVIVYNR-DNA--VLTADTLARLAERCPNLVG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 164 VKESTGDIQRMHKLRLLGEGRVPFYNGCnPLAlEAFVAGAKG-----WCSAAPNLIPTLNGQLYQAVLDGDLEKARAL-- 236
Cdd:PRK03620 163 FKDGVGDIELMQRIVRALGDRLLYLGGL-PTA-EVFAAAYLAlgvptYSSAVFNFVPEIALAFYRALRAGDHATVDRLld 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489192550 237 -FYrqLPLLDfiLRRGLP----TTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEELR 293
Cdd:PRK03620 241 dFF--LPYVA--LRNRKKgyavSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGG 298
 
Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
5-292 4.83e-110

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: 320.18  E-value: 4.83e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   5 IHGIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLT 84
Cdd:COG0329    2 FRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSNS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  85 TAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMV 164
Cdd:COG0329   82 TAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVGI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 165 KESTGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLL 244
Cdd:COG0329  161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489192550 245 DFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:COG0329  241 RALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKEL 288
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
8-289 2.11e-99

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: 292.91  E-value: 2.11e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   8 IIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTAK 87
Cdd:cd00408    1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  88 TVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKES 167
Cdd:cd00408   81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLA-EHPNIVGIKDS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 168 TGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDFI 247
Cdd:cd00408  160 SGDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489192550 248 LRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLL 289
Cdd:cd00408  240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
13-286 2.75e-78

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: 239.32  E-value: 2.75e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  13 ITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTAKTVRRA 92
Cdd:cd00950    9 VTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNTAEAIELT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  93 QFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKESTGDIQ 172
Cdd:cd00950   89 KRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLA-EHPNIVGIKEATGDLD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 173 RMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDFILRRGL 252
Cdd:cd00950  168 RVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIKALFAEPN 247
                        250       260       270
                 ....*....|....*....|....*....|....
gi 489192550 253 PTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQ 286
Cdd:cd00950  248 PIPVKAALALLGLISGELRLPLVPLSEELRAKLR 281
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
7-292 1.41e-62

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: 199.09  E-value: 1.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550    7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTA 86
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   87 KTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVREVdNVTMVKE 166
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  167 STGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDF 246
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 489192550  247 ILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEEL 292
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
7-292 6.45e-60

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 192.58  E-value: 6.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550    7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTTA 86
Cdd:pfam00701   4 GIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSNSTS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   87 KTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVKE 166
Cdd:pfam00701  84 EAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLA-TNPNIVGIKE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  167 STGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLLDF 246
Cdd:pfam00701 163 ASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 489192550  247 ILRRGLPTTIKAGLGLSGLEVGA-PRLPVQALDTEGCRYLQGLLEEL 292
Cdd:pfam00701 243 LFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
7-280 2.91e-43

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: 149.38  E-value: 2.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   7 GIIGYTITPFAADGGLDLPALGRSIERLID-GGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTT 85
Cdd:cd00954    3 GLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLNL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  86 AKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGE-AIGVPVMLYNNPGTSGIDMSVELILrIVREVDNVTMV 164
Cdd:cd00954   83 KESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAaAASLPMIIYHIPALTGVNLTLEQFL-ELFEIPNVIGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 165 KESTGDIQRMHKLRLLGEGRVPFYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKARALFYRQLPLL 244
Cdd:cd00954  162 KFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDVI 241
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489192550 245 DFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTE 280
Cdd:cd00954  242 TVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEK 277
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
7-290 2.61e-36

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: 131.29  E-value: 2.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSdLTTA 86
Cdd:cd00951    3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAG-YGTA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  87 KTVRRAQFAESLGAEAVMVLPiSYWKLNEAE-VFQHYRAVGEAIGVPVMLYNNpGTSGIdmSVELILRIVREVDNVTMVK 165
Cdd:cd00951   82 TAIAYAQAAEKAGADGILLLP-PYLTEAPQEgLYAHVEAVCKSTDLGVIVYNR-ANAVL--TADSLARLAERCPNLVGFK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 166 ESTGDIQRMHKLRLLGEGRVPFYNGCnPLAlEAFVAGAKG-----WCSAAPNLIPTLNGQLYQAVLDGDLEKARAL---F 237
Cdd:cd00951  158 DGVGDIELMRRIVAKLGDRLLYLGGL-PTA-EVFALAYLAmgvptYSSAVFNFVPEIALAFYAAVRAGDHATVKRLlrdF 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489192550 238 YrqLPLLDFILRR-GLPTTI-KAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLE 290
Cdd:cd00951  236 F--LPYVDIRNRRkGYAVSIvKAGARLVGRDAGPVRPPLTDLTEEELAQLTALIK 288
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
7-293 2.97e-34

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 126.08  E-value: 2.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSdLTTA 86
Cdd:PRK03620  10 GLLSFPVTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAG-GGTA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  87 KTVRRAQFAESLGAEAVMVLPiSYwkLNEAE---VFQHYRAVGEAIGVPVMLYNNpGTSgiDMSVELILRIVREVDNVTM 163
Cdd:PRK03620  89 QAIEYAQAAERAGADGILLLP-PY--LTEAPqegLAAHVEAVCKSTDLGVIVYNR-DNA--VLTADTLARLAERCPNLVG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 164 VKESTGDIQRMHKLRLLGEGRVPFYNGCnPLAlEAFVAGAKG-----WCSAAPNLIPTLNGQLYQAVLDGDLEKARAL-- 236
Cdd:PRK03620 163 FKDGVGDIELMQRIVRALGDRLLYLGGL-PTA-EVFAAAYLAlgvptYSSAVFNFVPEIALAFYRALRAGDHATVDRLld 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489192550 237 -FYrqLPLLDfiLRRGLP----TTIKAGLGLSGLEVGAPRLPVQALDTEGCRYLQGLLEELR 293
Cdd:PRK03620 241 dFF--LPYVA--LRNRKKgyavSIVKAGARLVGLDAGPVRAPLTDLTPEELAELAALIAKGG 298
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
7-273 4.38e-32

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 120.10  E-value: 4.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   7 GIIGYTITPFAADGGLDLPALGRSIERLIDG-GVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTIVSVSDLTT 85
Cdd:PRK04147   6 GVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSVNT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  86 AKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAIGVPVMLYNNPGTSGIDMSVELILRIVrEVDNVTMVK 165
Cdd:PRK04147  86 AEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELF-TLPKVIGVK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 166 ESTGDIQRMHKLRllgeGRVP---FYNGCNPLALEAFVAGAKGWCSAAPNliptLNGQLYQAVLD----GDLEKARALFY 238
Cdd:PRK04147 165 QTAGDLYQLERIR----KAFPdklIYNGFDEMFASGLLAGADGAIGSTYN----VNGWRARQIFEaakaGDIQEAQELQH 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489192550 239 RQLPLLDFILRRGLPTTIKAGLGLSGLEVGAPRLP 273
Cdd:PRK04147 237 ECNDVIDLLIKNGVYPGLKEILHYMGVDAGLCRKP 271
PLN02417 PLN02417
dihydrodipicolinate synthase
7-280 5.72e-23

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 95.48  E-value: 5.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   7 GIIGYTITPFAADGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSdpeWDE---VVDFTLKTVAHRVPTIVSVSDL 83
Cdd:PLN02417   4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMS---WDEhimLIGHTVNCFGGKIKVIGNTGSN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  84 TTAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEaIGvPVMLYNNPGTSGIDMSVELILrIVREVDNVTM 163
Cdd:PLN02417  81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD-MG-PTIIYNVPGRTGQDIPPEVIF-KIAQHPNFAG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 164 VKESTGDiQRMHKLRllgEGRVPFYNGCNPLALEA-FVAGAKGWCSAAPNLIPTLNGQLYQAVLDGDLEKaralfyRQLP 242
Cdd:PLN02417 158 VKECTGN-DRVKQYT---EKGILLWSGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFAGKNKELND------KLLP 227
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489192550 243 LLDFILRRGLPTTIKAGLGLSGLEVGAPRLPVQALDTE 280
Cdd:PLN02417 228 LMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLA 265
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
8-280 1.91e-22

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: 93.99  E-value: 1.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   8 IIGYTITPFAaDGGLDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDfTLKTVAHRVptIVSVSDLTTAK 87
Cdd:cd00953    4 KITPVITPFT-GNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLK-AYSDITDKV--IFQVGSLNLEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  88 TVRRAQFAESLGAEAVMVLPISYW-KLNEAEVFQHYRAVGEAIgvPVMLYNNPGTSGIDMSVELILRIVREVDNVTMVKE 166
Cdd:cd00953   80 SIELARAAKSFGIYAIASLPPYYFpGIPEEWLIKYFTDISSPY--PTFIYNYPKATGYDINARMAKEIKKAGGDIIGVKD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 167 STGDIqrMHKL---RLLGEGRVpfYNGCNPLALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVldgDLEKARALFYRQLPL 243
Cdd:cd00953  158 TNEDI--SHMLeykRLVPDFKV--YSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHV---AIEDAFKLQFLINEV 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 489192550 244 LDFILRRGlptTIKAGLGL----SGLEVGAPRLPVQALDTE 280
Cdd:cd00953  231 LDASRKYG---SWSANYSLvkifQGYDAGEPRPPFYPLDEE 268
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
5-236 1.53e-21

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: 92.12  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550   5 IHGIIGYTITPFAADGG-------LDLPALGRSIERLIDGGVHAIAPLGSTGEGAYLSDPEWDEVVDFTLKTVAHRVPTI 77
Cdd:cd00952    2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550  78 VSVSDLTTAKTVRRAQFAESLGAEAVMVLPISYWKLNEAEVFQHYRAVGEAigVP---VMLYNNPGTSGIDMSvELILRI 154
Cdd:cd00952   82 VGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEA--VPemaIAIYANPEAFKFDFP-RAAWAE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192550 155 VREVDNVTMVKEsTGDIQRMHKLRLLGEGRVPFYngcnPL------ALEAFVAGAKGWCSAAPNLIPTLNGQLYQAVLDG 228
Cdd:cd00952  159 LAQIPQVVAAKY-LGDIGALLSDLAAVKGRMRLL----PLeddyyaAARLFPEEVTAFWSSGAACGPAPVTALRDAVATG 233

                 ....*...
gi 489192550 229 DLEKARAL 236
Cdd:cd00952  234 DWTDARAL 241
 
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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