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Conserved domains on  [gi|1601516519|emb|VGM85510|]
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N-acetylneuraminate lyase [Streptococcus pneumoniae]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 7-296 2.23e-118

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member cd00954:

Pssm-ID: 473867 [Multi-domain]  Cd Length: 288  Bit Score: 341.98  E-value: 2.23e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   7 YEGVIPAFYACYDDQGEVSPERTRALVQYFIDK-GVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACN 85
Cdd:cd00954     1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  86 NTKDSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAAPNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIG 165
Cdd:cd00954    81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 166 VKNSSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAI 245
Cdd:cd00954   161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1601516519 246 IGKLTSahGNMYGVIKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAAAAL 296
Cdd:cd00954   241 ITVLIK--NGLYPTLKAILRL-MGLDAGPCRLPLRKVTEKALAKAKELAAK 288
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 7-296 2.23e-118

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: 341.98  E-value: 2.23e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   7 YEGVIPAFYACYDDQGEVSPERTRALVQYFIDK-GVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACN 85
Cdd:cd00954     1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  86 NTKDSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAAPNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIG 165
Cdd:cd00954    81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 166 VKNSSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAI 245
Cdd:cd00954   161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1601516519 246 IGKLTSahGNMYGVIKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAAAAL 296
Cdd:cd00954   241 ITVLIK--NGLYPTLKAILRL-MGLDAGPCRLPLRKVTEKALAKAKELAAK 288
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 6-295 3.50e-84

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: 255.08  E-value: 3.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   6 KYEGVIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACN 85
Cdd:COG0329     1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  86 NTKDSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAAPnTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIG 165
Cdd:COG0329    81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 166 VKNSSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAI 245
Cdd:COG0329   160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1601516519 246 IgKLTSAHGNMyGVIKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAAAA 295
Cdd:COG0329   240 I-RALFAEGNP-APVKAALAL-LGLPSGPVRLPLLPLSEEERAELRAALK 286
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 5-295 4.89e-71

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 221.41  E-value: 4.89e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   5 KKYEGVIPAFYACYDDQGEVSPERTRALVQYFIDK-GVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVA 83
Cdd:PRK04147    2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  84 CNNTKDSMELARHAESLGVDAIATIPPIY--FRLPEysVAKYWNDISSAAPNtDYVIYNIPQLAGVALTPSLYTEMLKNP 161
Cdd:PRK04147   82 SVNTAEAQELAKYATELGYDAISAVTPFYypFSFEE--ICDYYREIIDSADN-PMIVYNIPALTGVNLSLDQFNELFTLP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 162 RVIGVKNSSmpvQDIQTFVSLGGE--DHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQ 239
Cdd:PRK04147  159 KVIGVKQTA---GDLYQLERIRKAfpDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQ 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1601516519 240 YAINAIIGKLTSAhgNMYGVIKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAAAA 295
Cdd:PRK04147  236 HECNDVIDLLIKN--GVYPGLKEILHY-MGVDAGLCRKPFKPVDEKYLPALKALAA 288
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 6-294 4.02e-57

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 185.65  E-value: 4.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   6 KYEGVIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACN 85
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  86 NTKDSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDIsSAAPNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIG 165
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAI-AEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 166 VKNSSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAI 245
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1601516519 246 IGKLTSAhGNMYGvIKEVLKInEGLNIGS-VRSPLTPVTEEDRPVVEAAA 294
Cdd:pfam00701 240 IKILFAE-PNPIP-IKTALEL-LGLVVGPtCRLPLTPLSEEERPELEAIL 286
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 9-293 1.05e-34

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: 127.06  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   9 GVIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACNNTK 88
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  89 DSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAApNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIGVKN 168
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEV-DLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 169 SSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYainaiigK 248
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQ-------K 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1601516519 249 LTSAHGNMYGV-----IKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAA 293
Cdd:TIGR00674 233 LMPLHKALFIEtnpipVKTALAL-LGLIEGELRLPLTELSEEHRNKLRDV 281
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 7-296 2.23e-118

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: 341.98  E-value: 2.23e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   7 YEGVIPAFYACYDDQGEVSPERTRALVQYFIDK-GVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACN 85
Cdd:cd00954     1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  86 NTKDSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAAPNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIG 165
Cdd:cd00954    81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 166 VKNSSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAI 245
Cdd:cd00954   161 VKFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1601516519 246 IGKLTSahGNMYGVIKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAAAAL 296
Cdd:cd00954   241 ITVLIK--NGLYPTLKAILRL-MGLDAGPCRLPLRKVTEKALAKAKELAAK 288
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 6-295 3.50e-84

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: 255.08  E-value: 3.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   6 KYEGVIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACN 85
Cdd:COG0329     1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  86 NTKDSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAAPnTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIG 165
Cdd:COG0329    81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 166 VKNSSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAI 245
Cdd:COG0329   160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1601516519 246 IgKLTSAHGNMyGVIKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAAAA 295
Cdd:COG0329   240 I-RALFAEGNP-APVKAALAL-LGLPSGPVRLPLLPLSEEERAELRAALK 286
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 10-293 2.10e-73

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: 227.05  E-value: 2.10e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  10 VIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACNNTKD 89
Cdd:cd00408     1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  90 SMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDIsSAAPNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIGVKNS 169
Cdd:cd00408    81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAV-ADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 170 SMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAIIGKL 249
Cdd:cd00408   160 SGDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1601516519 250 tsAHGNMYGVIKEVLKINeGLNIGSVRSPLTPVTEEDRPVVEAA 293
Cdd:cd00408   240 --FKEGNPAPVKAALALL-GLDAGPVRLPLVPLSEEERAKLEAL 280
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 5-295 4.89e-71

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 221.41  E-value: 4.89e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   5 KKYEGVIPAFYACYDDQGEVSPERTRALVQYFIDK-GVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVA 83
Cdd:PRK04147    2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  84 CNNTKDSMELARHAESLGVDAIATIPPIY--FRLPEysVAKYWNDISSAAPNtDYVIYNIPQLAGVALTPSLYTEMLKNP 161
Cdd:PRK04147   82 SVNTAEAQELAKYATELGYDAISAVTPFYypFSFEE--ICDYYREIIDSADN-PMIVYNIPALTGVNLSLDQFNELFTLP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 162 RVIGVKNSSmpvQDIQTFVSLGGE--DHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQ 239
Cdd:PRK04147  159 KVIGVKQTA---GDLYQLERIRKAfpDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQ 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1601516519 240 YAINAIIGKLTSAhgNMYGVIKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAAAA 295
Cdd:PRK04147  236 HECNDVIDLLIKN--GVYPGLKEILHY-MGVDAGLCRKPFKPVDEKYLPALKALAA 288
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 6-294 4.02e-57

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 185.65  E-value: 4.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   6 KYEGVIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACN 85
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  86 NTKDSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDIsSAAPNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIG 165
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAI-AEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 166 VKNSSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAI 245
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1601516519 246 IGKLTSAhGNMYGvIKEVLKInEGLNIGS-VRSPLTPVTEEDRPVVEAAA 294
Cdd:pfam00701 240 IKILFAE-PNPIP-IKTALEL-LGLVVGPtCRLPLTPLSEEERPELEAIL 286
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 9-293 1.05e-34

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: 127.06  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   9 GVIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACNNTK 88
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  89 DSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAApNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIGVKN 168
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEV-DLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 169 SSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYainaiigK 248
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQ-------K 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1601516519 249 LTSAHGNMYGV-----IKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAA 293
Cdd:TIGR00674 233 LMPLHKALFIEtnpipVKTALAL-LGLIEGELRLPLTELSEEHRNKLRDV 281
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 8-293 3.28e-34

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: 125.68  E-value: 3.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   8 EGVIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACNNT 87
Cdd:cd00950     2 GGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  88 KDSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAA--PntdYVIYNIPQLAGVALTPSLYTEMLKNPRVIG 165
Cdd:cd00950    82 AEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATdlP---VILYNVPGRTGVNIEPETVLRLAEHPNIVG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 166 VKNSSMPVQDIQTFVSLGGEDHIVFNGPDEQFLGGRLMGARAGIGGTYGAMPELFLKLNQLIADKDLETARELQYAINAI 245
Cdd:cd00950   159 IKEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPL 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1601516519 246 IgKLTSAHGNMYGViKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEAA 293
Cdd:cd00950   239 I-KALFAEPNPIPV-KAALAL-LGLISGELRLPLVPLSEELRAKLRAA 283
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 22-287 7.65e-32

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: 119.41  E-value: 7.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  22 GEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKgklTIIAHVACNNTKDSMELARHAESLG 101
Cdd:cd00953    15 NKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD---KVIFQVGSLNLEESIELARAAKSFG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 102 VDAIATIPPIYF-RLPEYSVAKYWNDISSAAPNtdyVIYNIPQLAGVALTPSLYTEMLKNPR-VIGVKNSSMPVQDIQTF 179
Cdd:cd00953    92 IYAIASLPPYYFpGIPEEWLIKYFTDISSPYPT---FIYNYPKATGYDINARMAKEIKKAGGdIIGVKDTNEDISHMLEY 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 180 VSLgGEDHIVFNGPDEQFLGgrlmGARAGIGGTYGA----MPELFLKLNQLIADKDletARELQYAINAIIGklTSAHGN 255
Cdd:cd00953   169 KRL-VPDFKVYSGPDSLIFS----ALRSGLDGSVAAasnyLPEVFVKIKDHVAIED---AFKLQFLINEVLD--ASRKYG 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1601516519 256 MYGVIKEVLKINEGLNIGSVRSPLTPVTEEDR 287
Cdd:cd00953   239 SWSANYSLVKIFQGYDAGEPRPPFYPLDEEEE 270
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 24-295 1.94e-20

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: 89.43  E-value: 1.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  24 VSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACNNTKDSMELARHAESLGVD 103
Cdd:cd00952    26 VDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGAD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 104 AIATIPPIYFRLPEYSVAKYWNDISSAAPNTDYVIYNIPQLAGVALTPSLYTEMLKNPRVIGVK---NSSMPVQDIQTFv 180
Cdd:cd00952   106 GTMLGRPMWLPLDVDTAVQFYRDVAEAVPEMAIAIYANPEAFKFDFPRAAWAELAQIPQVVAAKylgDIGALLSDLAAV- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 181 slggEDHIVFNGPDEQFLGGRLMGARAGIGG-TYGAM--PELFLKLNQLIADKDLETARELQYAINAIIGKLtSAHGNM- 256
Cdd:cd00952   185 ----KGRMRLLPLEDDYYAAARLFPEEVTAFwSSGAAcgPAPVTALRDAVATGDWTDARALTDRMRWAAEPL-FPRGDFs 259

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1601516519 257 ----YGVIKEVLKINEG--LNIGSVRSPLTPVTEedrPVVEAAAA 295
Cdd:cd00952   260 efskYNIALEKARFDAAgyMRAGPARPPYNTAPE---AYLEGARE 301
PLN02417 PLN02417
dihydrodipicolinate synthase
 9-293 1.40e-15

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 75.06  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519   9 GVIPAFYACYDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVACNNTK 88
Cdd:PLN02417    4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  89 DSMELARHAESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAAPNtdyVIYNIPQLAGVALTPSLYTEMLKNPRVIGVKN 168
Cdd:PLN02417   84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMGPT---IIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 169 SsmpVQD--IQTFVslgGEDHIVFNGPDEQFLGGRL-MGARAGIGGTYGAMPELFLKL-----NQLIADKDLETARELQY 240
Cdd:PLN02417  161 C---TGNdrVKQYT---EKGILLWSGNDDECHDARWdYGADGVISVTSNLVPGLMHKLmfagkNKELNDKLLPLMDWLFC 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1601516519 241 AINAIIGKLTSAhgnMYGVIKEVLkineglnigsvRSPLTPVTEEDRPVVEAA 293
Cdd:PLN02417  235 EPNPIGLNTALA---QLGLIRPVF-----------RLPYVPLDLAKRAEFVAL 273
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 18-292 3.12e-11

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: 62.72  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  18 YDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHvACNNTKDSMELARHA 97
Cdd:cd00951    12 FDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAG-AGYGTATAIAYAQAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  98 ESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAAP------NTDYVIYNIPQLAGVAltpslytemLKNPRVIGVKNSSM 171
Cdd:cd00951    91 EKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDlgvivyNRANAVLTADSLARLA---------ERCPNLVGFKDGVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 172 PVQDIQTFVSLGGEDHIVFNG-PD-EQFlggrlMGARAGIG-GTYGA-----MPELFLKLNQLIADKDLETARELQ---- 239
Cdd:cd00951   162 DIELMRRIVAKLGDRLLYLGGlPTaEVF-----ALAYLAMGvPTYSSavfnfVPEIALAFYAAVRAGDHATVKRLLrdff 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1601516519 240 YAINAIigkltSAHGNMYGV--IKEVLKInEGLNIGSVRSPLTPVTEEDRPVVEA 292
Cdd:cd00951   237 LPYVDI-----RNRRKGYAVsiVKAGARL-VGRDAGPVRPPLTDLTEEELAQLTA 285
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 18-297 9.27e-11

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 61.37  E-value: 9.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  18 YDDQGEVSPERTRALVQYFIDKGVQGLYVNGSSGECIYQSVEDRKLILEEVMAVAKGKLTIIAHVAcNNTKDSMELARHA 97
Cdd:PRK03620   19 FDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAG-GGTAQAIEYAQAA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519  98 ESLGVDAIATIPPIYFRLPEYSVAKYWNDISSAAP------NTDYVIYNIPQLAGVALtpslytemlKNPRVIGVKNSSM 171
Cdd:PRK03620   98 ERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDlgvivyNRDNAVLTADTLARLAE---------RCPNLVGFKDGVG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 172 PVQDIQTFVSLGGEDHIVFNG-PD-EQFlggrlMGARAGIG-GTYG-AM----PELFLKLNQLIADKDLETARELQ---- 239
Cdd:PRK03620  169 DIELMQRIVRALGDRLLYLGGlPTaEVF-----AAAYLALGvPTYSsAVfnfvPEIALAFYRALRAGDHATVDRLLddff 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601516519 240 YAINAIIGKltsAHGnmYGV--IKEVLKInEGLNIGSVRSPLTPVTEEDrpvVEAAAALI 297
Cdd:PRK03620  244 LPYVALRNR---KKG--YAVsiVKAGARL-VGLDAGPVRAPLTDLTPEE---LAELAALI 294
 
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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