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Conserved domains on  [gi|318037609|ref|NP_001186985|]
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N-acetylneuraminate lyase isoform 3 [Homo sapiens]

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

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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 ...
 8-284 4.91e-126

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: 360.47  E-value: 4.91e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   8 LQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGA 87
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKV-TLIAHVGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  88 LSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIldKIP 167
Cdd:cd00954   80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELF--EIP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 168 TFQGLKFSDTDLLDFGQCVDQNrQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQF 247
Cdd:cd00954  157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 318037609 248 CIQRFINFVVKLE-NSKLKVSKNQRTLPLGTTNFPFLH 284
Cdd:cd00954  236 VINDVITVLIKNGlYPTLKAILRLMGLDAGPCRLPLRK 273
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 8-284 4.91e-126

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: 360.47  E-value: 4.91e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   8 LQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGA 87
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKV-TLIAHVGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  88 LSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIldKIP 167
Cdd:cd00954   80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELF--EIP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 168 TFQGLKFSDTDLLDFGQCVDQNrQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQF 247
Cdd:cd00954  157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 318037609 248 CIQRFINFVVKLE-NSKLKVSKNQRTLPLGTTNFPFLH 284
Cdd:cd00954  236 VINDVITVLIKNGlYPTLKAILRLMGLDAGPCRLPLRK 273
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 7-256 1.08e-70

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: 219.64  E-value: 1.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLI-DAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRV-PVIAGVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLDgiLDKI 166
Cdd:COG0329   79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLAR--LAEI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 167 PTFQGLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQ 246
Cdd:COG0329  155 PNIVGIKEASGDLDRIAELIRATG-DDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQ 233

                        250
                 ....*....|
gi 318037609 247 FCIQRFINFV 256
Cdd:COG0329  234 DRLLPLIRAL 243
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 6-258 4.88e-52

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 172.10  E-value: 4.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   6 KKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQ----VAEEwvTKGKDKLdqv 81
Cdd:PRK04147   2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  82 IIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLkPWTKDILINFLKEVAAAApALPFYYYHIPALTGVKIRAEELldG 161
Cdd:PRK04147  77 IAQVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLSLDQF--N 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 162 ILDKIPTFQGLKFSDTDLLDFGQCvdQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSL 241
Cdd:PRK04147 153 ELFTLPKVIGVKQTAGDLYQLERI--RKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQE 230

                        250
                 ....*....|....*..
gi 318037609 242 ALNYQFCIQRFINFVVK 258
Cdd:PRK04147 231 AQELQHECNDVIDLLIK 247
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 7-278 5.80e-49

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 164.08  E-value: 5.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609    7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLI-NKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRI-PVIAGVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDiLINFLKEVaAAAPALPFYYYHIPALTGVKIRAEELldGILDKI 166
Cdd:pfam00701  79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEG-LYQHFKAI-AEATDLPMILYNVPSRTGVDLTPETV--GRLATN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  167 PTFQGLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQ 246
Cdd:pfam00701 155 PNIVGIKEASGDLDRMINIKKEAG-PDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALIN 233

                         250       260       270
                  ....*....|....*....|....*....|...
gi 318037609  247 FCIQRFINFVVKLEN-SKLKVSKNQRTLPLGTT 278
Cdd:pfam00701 234 HKLLPLIKILFAEPNpIPIKTALELLGLVVGPT 266
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 10-243 5.47e-30

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: 114.35  E-value: 5.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   10 GLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGALS 89
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQI-ENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   90 LKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAApALPFYYYHIPALTGVKIRAEELLDgiLDKIPTF 169
Cdd:TIGR00674  79 TEEAISLTKFAEDVGADGFLVVTPYYNKP-TQEGLYQHFKAIAEEV-DLPIILYNVPSRTGVSLYPETVKR--LAEEPNI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318037609  170 QGLKFSDTDLLDFGQCVdQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLAL 243
Cdd:TIGR00674 155 VAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAR 227
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 8-284 4.91e-126

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: 360.47  E-value: 4.91e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   8 LQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGA 87
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKV-TLIAHVGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  88 LSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIldKIP 167
Cdd:cd00954   80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELF--EIP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 168 TFQGLKFSDTDLLDFGQCVDQNrQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQF 247
Cdd:cd00954  157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 318037609 248 CIQRFINFVVKLE-NSKLKVSKNQRTLPLGTTNFPFLH 284
Cdd:cd00954  236 VINDVITVLIKNGlYPTLKAILRLMGLDAGPCRLPLRK 273
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 7-256 1.08e-70

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: 219.64  E-value: 1.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLI-DAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRV-PVIAGVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLDgiLDKI 166
Cdd:COG0329   79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLAR--LAEI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 167 PTFQGLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQ 246
Cdd:COG0329  155 PNIVGIKEASGDLDRIAELIRATG-DDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQ 233

                        250
                 ....*....|
gi 318037609 247 FCIQRFINFV 256
Cdd:COG0329  234 DRLLPLIRAL 243
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 11-258 2.82e-69

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: 215.87  E-value: 2.82e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  11 LVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGALSL 90
Cdd:cd00408    1 VIPALVTPFTADGEVDLDALRRLVEFLI-EAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRV-PVIAGVGANST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  91 KESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAaPALPFYYYHIPALTGVKIRAEELLDgiLDKIPTFQ 170
Cdd:cd00408   79 REAIELARHAEEAGADGVLVVPPYYNKP-SQEGIVAHFKAVADA-SDLPVILYNIPGRTGVDLSPETIAR--LAEHPNIV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 171 GLKFSDTDLLDFGQCVDQNRQQqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQFCIQ 250
Cdd:cd00408  155 GIKDSSGDLDRLTRLIALLGPD-FAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLL 233


                 ....*...
gi 318037609 251 RFINFVVK 258
Cdd:cd00408  234 PLIEALFK 241
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 6-258 4.88e-52

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 172.10  E-value: 4.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   6 KKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQ----VAEEwvTKGKDKLdqv 81
Cdd:PRK04147   2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  82 IIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLkPWTKDILINFLKEVAAAApALPFYYYHIPALTGVKIRAEELldG 161
Cdd:PRK04147  77 IAQVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLSLDQF--N 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 162 ILDKIPTFQGLKFSDTDLLDFGQCvdQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSL 241
Cdd:PRK04147 153 ELFTLPKVIGVKQTAGDLYQLERI--RKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQE 230

                        250
                 ....*....|....*..
gi 318037609 242 ALNYQFCIQRFINFVVK 258
Cdd:PRK04147 231 AQELQHECNDVIDLLIK 247
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 7-278 5.80e-49

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 164.08  E-value: 5.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609    7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLI-NKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRI-PVIAGVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDiLINFLKEVaAAAPALPFYYYHIPALTGVKIRAEELldGILDKI 166
Cdd:pfam00701  79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEG-LYQHFKAI-AEATDLPMILYNVPSRTGVDLTPETV--GRLATN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  167 PTFQGLKFSDTDLLDFGQCVDQNRqQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQ 246
Cdd:pfam00701 155 PNIVGIKEASGDLDRMINIKKEAG-PDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALIN 233

                         250       260       270
                  ....*....|....*....|....*....|...
gi 318037609  247 FCIQRFINFVVKLEN-SKLKVSKNQRTLPLGTT 278
Cdd:pfam00701 234 HKLLPLIKILFAEPNpIPIKTALELLGLVVGPT 266
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 8-247 1.07e-37

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: 134.54  E-value: 1.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   8 LQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGA 87
Cdd:cd00950    1 FGGSITALVTPFKDDGSVDFDALERLIEFQI-ENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRV-PVIAGTGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  88 LSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLdgILDKIP 167
Cdd:cd00950   79 NNTAEAIELTKRAEKAGADAALVVTPYYNKP-SQEGLYAHFKAIAEATD-LPVILYNVPGRTGVNIEPETVL--RLAEHP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 168 TFQGLKFSDTDlLDFGQCVDQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQF 247
Cdd:cd00950  155 NIVGIKEATGD-LDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHR 233
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 10-243 5.47e-30

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: 114.35  E-value: 5.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   10 GLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVGALS 89
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQI-ENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   90 LKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAApALPFYYYHIPALTGVKIRAEELLDgiLDKIPTF 169
Cdd:TIGR00674  79 TEEAISLTKFAEDVGADGFLVVTPYYNKP-TQEGLYQHFKAIAEEV-DLPIILYNVPSRTGVSLYPETVKR--LAEEPNI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318037609  170 QGLKFSDTDLLDFGQCVdQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLAL 243
Cdd:TIGR00674 155 VAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAR 227
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 12-249 1.68e-25

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: 102.08  E-value: 1.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  12 VAATITPMTENgEINFSVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERRQVAEEWvtkgKDKLDQVIIHVGALSLK 91
Cdd:cd00953    5 ITPVITPFTGN-KIDKEKFKKHCENLISK-GIDYVFVAGTTGLGPSLSFQEKLELLKAY----SDITDKVIFQVGSLNLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  92 ESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFLKEVAAaapALPFYYYHIPALTGVKIRAeELLDGILDKIPTFQG 171
Cdd:cd00953   79 ESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISS---PYPTFIYNYPKATGYDINA-RMAKEIKKAGGDIIG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609 172 LK---FSDTDLLDFGQCVDqnrqqQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDfslALNYQFC 248
Cdd:cd00953  155 VKdtnEDISHMLEYKRLVP-----DFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAIED---AFKLQFL 226


                 .
gi 318037609 249 I 249
Cdd:cd00953  227 I 227
PLN02417 PLN02417
dihydrodipicolinate synthase
 7-238 3.70e-19

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 84.69  E-value: 3.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   7 KLQGLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLdQVIIHVG 86
Cdd:PLN02417   1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQI-ENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKI-KVIGNTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  87 ALSLKESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPALpfyYYHIPALTGVKIRAEELldGILDKI 166
Cdd:PLN02417  79 SNSTREAIHATEQGFAVGMHAALHINPYYGKT-SQEGLIKHFETVLDMGPTI---IYNVPGRTGQDIPPEVI--FKIAQH 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318037609 167 PTFQGLKfsdtdlldfgQCVDQNRQQQFA---FLF--GVDEQLLSA-LVMGATGAVGSTYNYLGKKTNQMLEAFEQKD 238
Cdd:PLN02417 153 PNFAGVK----------ECTGNDRVKQYTekgILLwsGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFAGKNKE 220
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 10-180 3.04e-08

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: 53.48  E-value: 3.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  10 GLVAATITPMTENGEINFSVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERRQVAEEWV--TKGKdkldqVIIHVGA 87
Cdd:cd00951    3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSY-GAAALFAAGGTGEFFSLTPDEYAQVVRAAVeeTAGR-----VPVLAGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  88 -LSLKESQELAQHAAEIGADGIaVIAPFFLKPWTKDILINFLKEVAAAAPaLPFYYYHipalTGVKIRAEELLDGILDKI 166
Cdd:cd00951   77 gYGTATAIAYAQAAEKAGADGI-LLLPPYLTEAPQEGLYAHVEAVCKSTD-LGVIVYN----RANAVLTADSLARLAERC 150

                        170
                 ....*....|....*.
gi 318037609 167 PTFQGLK--FSDTDLL 180
Cdd:cd00951  151 PNLVGFKdgVGDIELM 166
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 10-173 7.58e-08

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 52.51  E-value: 7.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  10 GLVAATITPMTENGEINFSVIGQYVDYLVkEQGVKNIFVNGTTGEGLSLSVSERRQV---AEEwVTKGKdkldqVIIHVG 86
Cdd:PRK03620  10 GLLSFPVTPFDADGSFDEAAYREHLEWLA-PYGAAALFAAGGTGEFFSLTPDEYSQVvraAVE-TTAGR-----VPVIAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609  87 A-LSLKESQELAQHAAEIGADGIAVIAPfFLKPWTKDILINFLKEVAAAAPaLPFYYYHipalTGVKIRAEELLDGILDK 165
Cdd:PRK03620  83 AgGGTAQAIEYAQAAERAGADGILLLPP-YLTEAPQEGLAAHVEAVCKSTD-LGVIVYN----RDNAVLTADTLARLAER 156


                 ....*...
gi 318037609 166 IPTFQGLK 173
Cdd:PRK03620 157 CPNLVGFK 164
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 8-146 2.37e-06

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: 48.21  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318037609   8 LQGLVAATITPMTENGE-------INFSVIGQYVDYLVKEqGVKNIFVNGTTGEGLSLSVSERR----QVAEewVTKGKd 76
Cdd:cd00952    2 IKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAA-GVDGILTMGTFGECATLTWEEKQafvaTVVE--TVAGR- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 318037609  77 kldqVIIHVGALSL--KESQELAQHAAEIGADGIAVIAPFFLKPwTKDILINFLKEVAAAAPALPFYYYHIP 146
Cdd:cd00952   78 ----VPVFVGATTLntRDTIARTRALLDLGADGTMLGRPMWLPL-DVDTAVQFYRDVAEAVPEMAIAIYANP 144
 
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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