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Conserved domains on  [gi|1811022935|ref|XP_032319467|]
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N-acetylneuraminate lyase isoform X2 [Camelus ferus]

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 ...
 8-248 4.54e-117

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: 337.74  E-value: 4.54e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGrNKLDQIVIHVGA 87
Cdd:cd00954     1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAA-KGKVTLIAHVGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  88 LSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIQekIP 167
Cdd:cd00954    80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELFE--IP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 168 TFQGLKFSDTDLLDFGQCVDQNrQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQE 247
Cdd:cd00954   157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235


                  .
gi 1811022935 248 K 248
Cdd:cd00954   236 V 236
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 8-248 4.54e-117

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: 337.74  E-value: 4.54e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGrNKLDQIVIHVGA 87
Cdd:cd00954     1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAA-KGKVTLIAHVGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  88 LSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIQekIP 167
Cdd:cd00954    80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELFE--IP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 168 TFQGLKFSDTDLLDFGQCVDQNrQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQE 247
Cdd:cd00954   157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235


                  .
gi 1811022935 248 K 248
Cdd:cd00954   236 V 236
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 7-248 4.76e-65

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: 205.39  E-value: 4.76e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   7 RLQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWV--TRGRNKldqIVIH 84
Cdd:COG0329     1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLID-AGVDGLVVLGTTGESATLTDEERKRVLEAVVeaAAGRVP---VIAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  85 VGALSLKESQELAQHAAKIGADGIAVIAPFFLKPwNKDILVNFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLDGIqe 164
Cdd:COG0329    77 VGSNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLA-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 165 KIPTFQGLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALN 244
Cdd:COG0329   153 EIPNIVGIKEASGDLDRIAELIRATGDD-FAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARA 231


                  ....
gi 1811022935 245 YQEK 248
Cdd:COG0329   232 LQDR 235
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 8-246 2.09e-48

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 162.86  E-value: 2.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCR----VAEEwvTRGRNKLdqiVI 83
Cdd:PRK04147    4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL---IA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  84 HVGALSLKESQELAQHAAKIGADGIAVIAPFFLkPWNKDILVNFLKEVAAAApALPFYYYHIPALTGVKIRaeelLDGIQ 163
Cdd:PRK04147   79 QVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLS----LDQFN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 164 E--KIPTFQGLKFSDTDLLDFGQCvdQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSS 241
Cdd:PRK04147  153 ElfTLPKVIGVKQTAGDLYQLERI--RKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQE 230


                  ....*
gi 1811022935 242 ALNYQ 246
Cdd:PRK04147  231 AQELQ 235
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 8-248 1.51e-43

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 150.21  E-value: 1.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVT--RGRNKLdqiVIHV 85
Cdd:pfam00701   2 FSGIITALVTPFDTDGTLDFAALRQLIDFLIN-KGVDGLVVGGTTGESFTLSTEEREQLVEITVNeaKGRIPV---IAGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  86 GALSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAaPALPFYYYHIPALTGVKIRAEElldgIQE- 164
Cdd:pfam00701  78 GSNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHF-KAIAEA-TDLPMILYNVPSRTGVDLTPET----VGRl 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 165 -KIPTFQGLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSAL 243
Cdd:pfam00701 152 aTNPNIVGIKEASGDLDRMINIKKEAGPD-FVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAA 230


                  ....*
gi 1811022935 244 NYQEK 248
Cdd:pfam00701 231 LINHK 235
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 10-248 1.50e-28

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: 110.50  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  10 GLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGRNKLdQIVIHVGALS 89
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIE-NGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  90 LKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAApALPFYYYHIPALTGVKIRAEELLDgiQEKIPTF 169
Cdd:TIGR00674  79 TEEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHF-KAIAEEV-DLPIILYNVPSRTGVSLYPETVKR--LAEEPNI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811022935 170 QGLKFSDTDLLDFGQCVdQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQEK 248
Cdd:TIGR00674 155 VAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQK 232
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 8-248 4.54e-117

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: 337.74  E-value: 4.54e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGrNKLDQIVIHVGA 87
Cdd:cd00954     1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEKQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAA-KGKVTLIAHVGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  88 LSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGIQekIP 167
Cdd:cd00954    80 LNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYY-REIIAAAASLPMIIYHIPALTGVNLTLEQFLELFE--IP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 168 TFQGLKFSDTDLLDFGQCVDQNrQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQE 247
Cdd:cd00954   157 NVIGVKFTATDLYDLERIRAAS-PEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235


                  .
gi 1811022935 248 K 248
Cdd:cd00954   236 V 236
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 7-248 4.76e-65

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: 205.39  E-value: 4.76e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   7 RLQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWV--TRGRNKldqIVIH 84
Cdd:COG0329     1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLID-AGVDGLVVLGTTGESATLTDEERKRVLEAVVeaAAGRVP---VIAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  85 VGALSLKESQELAQHAAKIGADGIAVIAPFFLKPwNKDILVNFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLDGIqe 164
Cdd:COG0329    77 VGSNSTAEAIELARHAEEAGADAVLVVPPYYNKP-TQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLA-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 165 KIPTFQGLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALN 244
Cdd:COG0329   153 EIPNIVGIKEASGDLDRIAELIRATGDD-FAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARA 231


                  ....
gi 1811022935 245 YQEK 248
Cdd:COG0329   232 LQDR 235
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 11-248 1.00e-63

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: 202.01  E-value: 1.00e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  11 LVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGRNKLdQIVIHVGALSL 90
Cdd:cd00408     1 VIPALVTPFTADGEVDLDALRRLVEFLIE-AGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRV-PVIAGVGANST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  91 KESQELAQHAAKIGADGIAVIAPFFLKPwNKDILVNFLKEVAAAaPALPFYYYHIPALTGVKIRAEELLDGIQekIPTFQ 170
Cdd:cd00408    79 REAIELARHAEEAGADGVLVVPPYYNKP-SQEGIVAHFKAVADA-SDLPVILYNIPGRTGVDLSPETIARLAE--HPNIV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811022935 171 GLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQEK 248
Cdd:cd00408   155 GIKDSSGDLDRLTRLIALLGPD-FAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDR 231
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 8-246 2.09e-48

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 162.86  E-value: 2.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEEQGVKNIFVNGTTGEGLSLSISERCR----VAEEwvTRGRNKLdqiVI 83
Cdd:PRK04147    4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKQGIDGLYVGGSTGEAFLLSTEEKKQvleiVAEE--AKGKVKL---IA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  84 HVGALSLKESQELAQHAAKIGADGIAVIAPFFLkPWNKDILVNFLKEVAAAApALPFYYYHIPALTGVKIRaeelLDGIQ 163
Cdd:PRK04147   79 QVGSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSA-DNPMIVYNIPALTGVNLS----LDQFN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 164 E--KIPTFQGLKFSDTDLLDFGQCvdQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSS 241
Cdd:PRK04147  153 ElfTLPKVIGVKQTAGDLYQLERI--RKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQE 230


                  ....*
gi 1811022935 242 ALNYQ 246
Cdd:PRK04147  231 AQELQ 235
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 8-248 1.51e-43

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 150.21  E-value: 1.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVT--RGRNKLdqiVIHV 85
Cdd:pfam00701   2 FSGIITALVTPFDTDGTLDFAALRQLIDFLIN-KGVDGLVVGGTTGESFTLSTEEREQLVEITVNeaKGRIPV---IAGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  86 GALSLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAaPALPFYYYHIPALTGVKIRAEElldgIQE- 164
Cdd:pfam00701  78 GSNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHF-KAIAEA-TDLPMILYNVPSRTGVDLTPET----VGRl 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 165 -KIPTFQGLKFSDTDLLDFGQCVDQNRQRqFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSAL 243
Cdd:pfam00701 152 aTNPNIVGIKEASGDLDRMINIKKEAGPD-FVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAA 230


                  ....*
gi 1811022935 244 NYQEK 248
Cdd:pfam00701 231 LINHK 235
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 8-248 6.34e-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: 124.53  E-value: 6.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   8 LQGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAE---EWVtRGRNKldqIVIH 84
Cdd:cd00950     1 FGGSITALVTPFKDDGSVDFDALERLIEFQIE-NGTDGLVVCGTTGESPTLSDEEHEAVIEavvEAV-NGRVP---VIAG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  85 VGALSLKESQELAQHAAKIGADGIAVIAPFFLKPwNKDILVNFLKEVAAAAPaLPFYYYHIPALTGVKIRAEELLdgIQE 164
Cdd:cd00950    76 TGSNNTAEAIELTKRAEKAGADAALVVTPYYNKP-SQEGLYAHFKAIAEATD-LPVILYNVPGRTGVNIEPETVL--RLA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 165 KIPTFQGLKFSDTDlLDFGQCVDQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALN 244
Cdd:cd00950   152 EHPNIVGIKEATGD-LDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARE 230


                  ....
gi 1811022935 245 YQEK 248
Cdd:cd00950   231 LHRK 234
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 10-248 1.50e-28

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: 110.50  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  10 GLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGRNKLdQIVIHVGALS 89
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIE-NGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRV-PVIAGTGSNA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  90 LKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlKEVAAAApALPFYYYHIPALTGVKIRAEELLDgiQEKIPTF 169
Cdd:TIGR00674  79 TEEAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHF-KAIAEEV-DLPIILYNVPSRTGVSLYPETVKR--LAEEPNI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811022935 170 QGLKFSDTDLLDFGQCVdQNRQRQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDFSSALNYQEK 248
Cdd:TIGR00674 155 VAIKEATGNLERISEIK-AIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQK 232
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 12-246 1.89e-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: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  12 VAATITPMTEhGEINFSVIGQYVDYLVEEqGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGrnklDQIVIHVGALSLK 91
Cdd:cd00953     5 ITPVITPFTG-NKIDKEKFKKHCENLISK-GIDYVFVAGTTGLGPSLSFQEKLELLKAYSDIT----DKVIFQVGSLNLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  92 ESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFLKEVAAaapALPFYYYHIPALTGVKIRAeELLDGIQEKIPTFQG 171
Cdd:cd00953    79 ESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISS---PYPTFIYNYPKATGYDINA-RMAKEIKKAGGDIIG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 172 LKfsDT-----DLLDFGQCVDqnrqrQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFERKDfssALNYQ 246
Cdd:cd00953   155 VK--DTnedisHMLEYKRLVP-----DFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAIED---AFKLQ 224
PLN02417 PLN02417
dihydrodipicolinate synthase
 9-243 7.22e-14

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 70.06  E-value: 7.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935   9 QGLVAATITPMTEHGEINFSVIGQYVDYLVEeQGVKNIFVNGTTGEGLSLSISERCRVAEEWVTRGRNKLdQIVIHVGAL 88
Cdd:PLN02417    3 LRLITAIKTPYLPDGRFDLEAYDSLVNMQIE-NGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKI-KVIGNTGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  89 SLKESQELAQHAAKIGADGIAVIAPFFLKPWNKDILVNFlkevAAAAPALPFYYYHIPALTGVKIraeelLDGIQEKI-- 166
Cdd:PLN02417   81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHF----ETVLDMGPTIIYNVPGRTGQDI-----PPEVIFKIaq 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935 167 -PTFQGLKfsdtdlldfgQCVDQNRQRQFA---FLF--GVDEQLLSA-LVMGATGAVGSTYNYLGKKTNQMLEAFERKDF 239
Cdd:PLN02417  152 hPNFAGVK----------ECTGNDRVKQYTekgILLwsGNDDECHDArWDYGADGVISVTSNLVPGLMHKLMFAGKNKEL 221


                  ....
gi 1811022935 240 SSAL 243
Cdd:PLN02417  222 NDKL 225
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 10-180 9.78e-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: 52.32  E-value: 9.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  10 GLVAATITPMTEHGEINFSVIGQYVDYLVEEqGVKNIFVNGTTGEGLSLSISE--RC-RVAEEwVTRGRnkldqIVIHVG 86
Cdd:cd00951     3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSY-GAAALFAAGGTGEFFSLTPDEyaQVvRAAVE-ETAGR-----VPVLAG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  87 A-LSLKESQELAQHAAKIGADGIaVIAPFFLKPWNKDILVNFLKEVAAAAPaLPFYYYHipalTGVKIRAEELLDGIQEK 165
Cdd:cd00951    76 AgYGTATAIAYAQAAEKAGADGI-LLLPPYLTEAPQEGLYAHVEAVCKSTD-LGVIVYN----RANAVLTADSLARLAER 149

                         170
                  ....*....|....*..
gi 1811022935 166 IPTFQGLK--FSDTDLL 180
Cdd:cd00951   150 CPNLVGFKdgVGDIELM 166
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 34-146 1.46e-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: 48.60  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  34 VDYLVEEqGVKNIFVNGTTGEGLSLSISER----CRVAEewVTRGRnkldqIVIHVGALSL--KESQELAQHAAKIGADG 107
Cdd:cd00952    35 VERLIAA-GVDGILTMGTFGECATLTWEEKqafvATVVE--TVAGR-----VPVFVGATTLntRDTIARTRALLDLGADG 106

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1811022935 108 IAVIAPFFLKPwNKDILVNFLKEVAAAAPALPFYYYHIP 146
Cdd:cd00952   107 TMLGRPMWLPL-DVDTAVQFYRDVAEAVPEMAIAIYANP 144
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 16-173 7.35e-06

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 46.73  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  16 ITPMTEHGEINFSVIGQYVDYLVEEqGVKNIFVNGTTGEGLSLSISE--RC-RVAEEwVTRGRnkldqIVIHVGA-LSLK 91
Cdd:PRK03620   16 VTPFDADGSFDEAAYREHLEWLAPY-GAAALFAAGGTGEFFSLTPDEysQVvRAAVE-TTAGR-----VPVIAGAgGGTA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811022935  92 ESQELAQHAAKIGADGIAVIAPfFLKPWNKDILVNFLKEVAAAAPaLPFYYYHipalTGVKIRAEELLDGIQEKIPTFQG 171
Cdd:PRK03620   89 QAIEYAQAAERAGADGILLLPP-YLTEAPQEGLAAHVEAVCKSTD-LGVIVYN----RDNAVLTADTLARLAERCPNLVG 162


                  ..
gi 1811022935 172 LK 173
Cdd:PRK03620  163 FK 164
 
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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