NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|156551613|ref|XP_001600684|]
View 

N-acetylneuraminate lyase isoform X1 [Nasonia vitripennis]

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

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 9-297 2.90e-59

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: 191.37  E-value: 2.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   9 RGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:cd00954    2 KGLIAALLTPF--DENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKG-KVTLIAHVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTSVEDLIEYLSIvSKSAPNTPLLYYHIPKASMVNIHMGKFLQTVEerI 167
Cdd:cd00954   79 SLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREI-IAAAASLPMIIYHIPALTGVNLTLEQFLELFE--I 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 168 PTFSGIKFTSNDLEEgFEAMRA--NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIARTN 245
Cdd:cd00954  156 PNVIGVKFTATDLYD-LERIRAasPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFN-AGDIDTAREL 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156551613 246 QEFINKTVKAITHFGTwVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMK 297
Cdd:cd00954  234 QHVINDVITVLIKNGL-YPTLKAILRL-MGLDAGPCRLPLRKVTEKALAKAK 283
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 9-297 2.90e-59

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: 191.37  E-value: 2.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   9 RGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:cd00954    2 KGLIAALLTPF--DENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKG-KVTLIAHVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTSVEDLIEYLSIvSKSAPNTPLLYYHIPKASMVNIHMGKFLQTVEerI 167
Cdd:cd00954   79 SLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREI-IAAAASLPMIIYHIPALTGVNLTLEQFLELFE--I 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 168 PTFSGIKFTSNDLEEgFEAMRA--NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIARTN 245
Cdd:cd00954  156 PNVIGVKFTATDLYD-LERIRAasPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFN-AGDIDTAREL 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156551613 246 QEFINKTVKAITHFGTwVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMK 297
Cdd:cd00954  234 QHVINDVITVLIKNGL-YPTLKAILRL-MGLDAGPCRLPLRKVTEKALAKAK 283
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 8-305 8.79e-53

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: 174.96  E-value: 8.79e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   8 FRGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:COG0329    2 FRGVIPALVTPF--DADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAG-RVPVIAGVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTsVEDLIEYLSIVSKSAPnTPLLYYHIPKASMVNIHMgkflQTVEE-- 165
Cdd:COG0329   79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKPT-QEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSP----ETLARla 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 166 RIPTFSGIKFTSNDLEEGFEAMRA-NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLE-FGKGNRDLkiAR 243
Cdd:COG0329  153 EIPNIVGIKEASGDLDRIAELIRAtGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEaALAGDLAE--AR 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156551613 244 TNQEFINKTVKAITHFGTWVeTMKIAMSMtTNLFMGPPRAPLKLISRESVEKMKTNLAEIGL 305
Cdd:COG0329  231 ALQDRLLPLIRALFAEGNPA-PVKAALAL-LGLPSGPVRLPLLPLSEEERAELRAALKELGL 290
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 8-256 2.44e-31

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 118.62  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613    8 FRGLIVPVFSPFNNDANrsLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKeTKQHLMVQIG 87
Cdd:pfam00701   2 FSGIITALVTPFDTDGT--LDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAK-GRIPVIAGVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPtSVEDLIEYLSIVSkSAPNTPLLYYHIPKASMVNIHmgkfLQTVEE-- 165
Cdd:pfam00701  79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKP-SQEGLYQHFKAIA-EATDLPMILYNVPSRTGVDLT----PETVGRla 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  166 RIPTFSGIKFTSNDLEEGFEAMR-ANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIART 244
Cdd:pfam00701 153 TNPNIVGIKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALK-NGDLATAAL 231

                         250
                  ....*....|..
gi 156551613  245 NQEFINKTVKAI 256
Cdd:pfam00701 232 INHKLLPLIKIL 243
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 8-309 8.80e-30

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 114.71  E-value: 8.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   8 FRGLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQI 86
Cdd:PRK04147   4 LKGVYAALLTPFDEDG--QIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKG-KVKLIAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  87 GGTSLNDVKELAAHAEKLGVNSLLCLPELYFkPTSVEDLIEYLSIVSKSAPNtPLLYYHIPKASMVNIHMGKFLQTVEer 166
Cdd:PRK04147  81 GSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSADN-PMIVYNIPALTGVNLSLDQFNELFT-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 167 IPTFSGIKFTSNDLeegFEAMRANKRFA---VFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKGNrDLKIAR 243
Cdd:PRK04147 157 LPKVIGVKQTAGDL---YQLERIRKAFPdklIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAG-DIQEAQ 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156551613 244 TNQEFINKTVKAITHFGTWVETMKIAMSMTTNlfMGPPRAPLklisRESVEKMKTNLAEIGLKVNQ 309
Cdd:PRK04147 233 ELQHECNDVIDLLIKNGVYPGLKEILHYMGVD--AGLCRKPF----KPVDEKYLPALKALAAKYLK 292
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 10-302 1.37e-19

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: 86.61  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   10 GLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETwaaAVKETKQHLMVqIGGT 89
Cdd:TIGR00674   1 GVITALITPFKEDG--SVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEF---VVDLVNGRVPV-IAGT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   90 SLNDVKE---LAAHAEKLGVNSLLCLPELYFKPTSvEDLIEYLSIVSKSApNTPLLYYHIPKASMVNIhmgkFLQTVEE- 165
Cdd:TIGR00674  75 GSNATEEaisLTKFAEDVGADGFLVVTPYYNKPTQ-EGLYQHFKAIAEEV-DLPIILYNVPSRTGVSL----YPETVKRl 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  166 -RIPTFSGIKFTSNDLEEGFEAMR-ANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEfgkgnrdlkiAR 243
Cdd:TIGR00674 149 aEEPNIVAIKEATGNLERISEIKAiAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVN----------NA 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156551613  244 TNQEFInktvKAITHFGTWVETMKiAMSMTTN------------LFMGPPRAPLKLISRESVEKMKTNLAE 302
Cdd:TIGR00674 219 LEGDFA----EAREIHQKLMPLHK-ALFIETNpipvktalallgLIEGELRLPLTELSEEHRNKLRDVLKD 284
 
Name Accession Description Interval E-value
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 9-297 2.90e-59

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: 191.37  E-value: 2.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   9 RGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:cd00954    2 KGLIAALLTPF--DENGEINEDVLRAIVDYLIEKqGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKG-KVTLIAHVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTSVEDLIEYLSIvSKSAPNTPLLYYHIPKASMVNIHMGKFLQTVEerI 167
Cdd:cd00954   79 SLNLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREI-IAAAASLPMIIYHIPALTGVNLTLEQFLELFE--I 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 168 PTFSGIKFTSNDLEEgFEAMRA--NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIARTN 245
Cdd:cd00954  156 PNVIGVKFTATDLYD-LERIRAasPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFN-AGDIDTAREL 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156551613 246 QEFINKTVKAITHFGTwVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMK 297
Cdd:cd00954  234 QHVINDVITVLIKNGL-YPTLKAILRL-MGLDAGPCRLPLRKVTEKALAKAK 283
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 8-305 8.79e-53

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: 174.96  E-value: 8.79e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   8 FRGLIVPVFSPFnnDANRSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQIG 87
Cdd:COG0329    2 FRGVIPALVTPF--DADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAG-RVPVIAGVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPTsVEDLIEYLSIVSKSAPnTPLLYYHIPKASMVNIHMgkflQTVEE-- 165
Cdd:COG0329   79 SNSTAEAIELARHAEEAGADAVLVVPPYYNKPT-QEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSP----ETLARla 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 166 RIPTFSGIKFTSNDLEEGFEAMRA-NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLE-FGKGNRDLkiAR 243
Cdd:COG0329  153 EIPNIVGIKEASGDLDRIAELIRAtGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEaALAGDLAE--AR 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156551613 244 TNQEFINKTVKAITHFGTWVeTMKIAMSMtTNLFMGPPRAPLKLISRESVEKMKTNLAEIGL 305
Cdd:COG0329  231 ALQDRLLPLIRALFAEGNPA-PVKAALAL-LGLPSGPVRLPLLPLSEEERAELRAALKELGL 290
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 11-297 4.26e-48

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: 162.33  E-value: 4.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  11 LIVPVFSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKETKQhLMVQIGGTS 90
Cdd:cd00408    1 VIPALVTPFTADG--EVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVP-VIAGVGANS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  91 LNDVKELAAHAEKLGVNSLLCLPELYFKPTSvEDLIEYLSIVSkSAPNTPLLYYHIPKASMVNIHmgkfLQTVEE--RIP 168
Cdd:cd00408   78 TREAIELARHAEEAGADGVLVVPPYYNKPSQ-EGIVAHFKAVA-DASDLPVILYNIPGRTGVDLS----PETIARlaEHP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 169 TFSGIKFTSNDLEEgFEAMRA--NKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIARTNQ 246
Cdd:cd00408  152 NIVGIKDSSGDLDR-LTRLIAllGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAAR-AGDLEEARALQ 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 156551613 247 EFINKTVKAITHFGtWVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMK 297
Cdd:cd00408  230 DRLLPLIEALFKEG-NPAPVKAALAL-LGLDAGPVRLPLVPLSEEERAKLE 278
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 12-302 1.56e-31

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: 119.02  E-value: 1.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  12 IVPVFSPFNNdaNRsLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTEtwaaAVKETKQHLMVQIGGTSL 91
Cdd:cd00953    5 ITPVITPFTG--NK-IDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLK----AYSDITDKVIFQVGSLNL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  92 NDVKELAAHAEKLGVNSLLCLPELYFKPTSVEDLIEYLSIVSKSapnTPLLYYHIPKASMVNIHmGKFLQTVEERIPTFS 171
Cdd:cd00953   78 EESIELARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISSP---YPTFIYNYPKATGYDIN-ARMAKEIKKAGGDII 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 172 GIKFTSNDLEEGFEAMRANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEfgkgNRDLKIARTNQEFINK 251
Cdd:cd00953  154 GVKDTNEDISHMLEYKRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKD----HVAIEDAFKLQFLINE 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 156551613 252 TVKAITHFGTW------VETMKiamsmttNLFMGPPRAPLKLISRESVEKMKTNLAE 302
Cdd:cd00953  230 VLDASRKYGSWsanyslVKIFQ-------GYDAGEPRPPFYPLDEEEEEKLRKEVNE 279
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 8-256 2.44e-31

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 118.62  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613    8 FRGLIVPVFSPFNNDANrsLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKeTKQHLMVQIG 87
Cdd:pfam00701   2 FSGIITALVTPFDTDGT--LDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAK-GRIPVIAGVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   88 GTSLNDVKELAAHAEKLGVNSLLCLPELYFKPtSVEDLIEYLSIVSkSAPNTPLLYYHIPKASMVNIHmgkfLQTVEE-- 165
Cdd:pfam00701  79 SNSTSEAIHLAQLAEEYGADGALAVTPYYNKP-SQEGLYQHFKAIA-EATDLPMILYNVPSRTGVDLT----PETVGRla 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  166 RIPTFSGIKFTSNDLEEGFEAMR-ANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKIART 244
Cdd:pfam00701 153 TNPNIVGIKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALK-NGDLATAAL 231

                         250
                  ....*....|..
gi 156551613  245 NQEFINKTVKAI 256
Cdd:pfam00701 232 INHKLLPLIKIL 243
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 8-309 8.80e-30

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 114.71  E-value: 8.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   8 FRGLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASK-NINGVLVNGTTGEGTSLSTNERKKVTETWAAAVKEtKQHLMVQI 86
Cdd:PRK04147   4 LKGVYAALLTPFDEDG--QIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKG-KVKLIAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  87 GGTSLNDVKELAAHAEKLGVNSLLCLPELYFkPTSVEDLIEYLSIVSKSAPNtPLLYYHIPKASMVNIHMGKFLQTVEer 166
Cdd:PRK04147  81 GSVNTAEAQELAKYATELGYDAISAVTPFYY-PFSFEEICDYYREIIDSADN-PMIVYNIPALTGVNLSLDQFNELFT-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 167 IPTFSGIKFTSNDLeegFEAMRANKRFA---VFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKGNrDLKIAR 243
Cdd:PRK04147 157 LPKVIGVKQTAGDL---YQLERIRKAFPdklIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAG-DIQEAQ 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156551613 244 TNQEFINKTVKAITHFGTWVETMKIAMSMTTNlfMGPPRAPLklisRESVEKMKTNLAEIGLKVNQ 309
Cdd:PRK04147 233 ELQHECNDVIDLLIKNGVYPGLKEILHYMGVD--AGLCRKPF----KPVDEKYLPALKALAAKYLK 292
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 8-300 1.27e-25

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: 103.34  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   8 FRGLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTEtwaAAVKETKQHLMVqIG 87
Cdd:cd00950    1 FGGSITALVTPFKDDG--SVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIE---AVVEAVNGRVPV-IA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  88 GTSLND---VKELAAHAEKLGVNSLLCLPELYFKPTSvEDLIEYLSIVSkSAPNTPLLYYHIPKASMVNIHmgkfLQTVE 164
Cdd:cd00950   75 GTGSNNtaeAIELTKRAEKAGADAALVVTPYYNKPSQ-EGLYAHFKAIA-EATDLPVILYNVPGRTGVNIE----PETVL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 165 E--RIPTFSGIKFTSNDLEEGFE-AMRANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKgNRDLKI 241
Cdd:cd00950  149 RlaEHPNIVGIKEATGDLDRVSElIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAAL-AGDLEK 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156551613 242 ARTNQEFINKTVKAIthFgtwVET----MKIAMSMtTNLFMGPPRAPLKLISRESVEKMKTNL 300
Cdd:cd00950  228 ARELHRKLLPLIKAL--F---AEPnpipVKAALAL-LGLISGELRLPLVPLSEELRAKLRAAL 284
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 10-302 1.37e-19

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: 86.61  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   10 GLIVPVFSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETwaaAVKETKQHLMVqIGGT 89
Cdd:TIGR00674   1 GVITALITPFKEDG--SVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEF---VVDLVNGRVPV-IAGT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613   90 SLNDVKE---LAAHAEKLGVNSLLCLPELYFKPTSvEDLIEYLSIVSKSApNTPLLYYHIPKASMVNIhmgkFLQTVEE- 165
Cdd:TIGR00674  75 GSNATEEaisLTKFAEDVGADGFLVVTPYYNKPTQ-EGLYQHFKAIAEEV-DLPIILYNVPSRTGVSL----YPETVKRl 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  166 -RIPTFSGIKFTSNDLEEGFEAMR-ANKRFAVFLGSDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEfgkgnrdlkiAR 243
Cdd:TIGR00674 149 aEEPNIVAIKEATGNLERISEIKAiAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVN----------NA 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156551613  244 TNQEFInktvKAITHFGTWVETMKiAMSMTTN------------LFMGPPRAPLKLISRESVEKMKTNLAE 302
Cdd:TIGR00674 219 LEGDFA----EAREIHQKLMPLHK-ALFIETNpipvktalallgLIEGELRLPLTELSEEHRNKLRDVLKD 284
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 14-228 3.24e-09

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 57.13  E-value: 3.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  14 PVfSPFnnDANRSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTETwaaAVKETKQHLMVQIG-GTSLN 92
Cdd:PRK03620  15 PV-TPF--DADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRA---AVETTAGRVPVIAGaGGGTA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  93 DVKELAAHAEKLGVNSLLCLPElYFKPTSVEDLIEYLSIVSKSApNTPLLYYHipKASMVnihmgkF----LQTVEERIP 168
Cdd:PRK03620  89 QAIEYAQAAERAGADGILLLPP-YLTEAPQEGLAAHVEAVCKST-DLGVIVYN--RDNAV------LtadtLARLAERCP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156551613 169 TFSGIKFTSNDLEEGFEAMRA-NKRFAVFLG---SDVLMAAGSTIGIDSFIMTSLNFIPEPALE 228
Cdd:PRK03620 159 NLVGFKDGVGDIELMQRIVRAlGDRLLYLGGlptAEVFAAAYLALGVPTYSSAVFNFVPEIALA 222
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 11-298 1.27e-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: 55.02  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  11 LIVPVfSPFNNDAnrSLNLSIIPEYAKFLASKNINGVLVNGTTGEGTSLSTNERKKVTEtwaAAVKETKQHLMVQIG-GT 89
Cdd:cd00951    5 LSFPV-THFDADG--SFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVR---AAVEETAGRVPVLAGaGY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  90 SLNDVKELAAHAEKLGVNSLLCLPElYFKPTSVEDLIEYLSIVSKSAPnTPLLYYHipKASMVniHMGKFLQTVEERIPT 169
Cdd:cd00951   79 GTATAIAYAQAAEKAGADGILLLPP-YLTEAPQEGLYAHVEAVCKSTD-LGVIVYN--RANAV--LTADSLARLAERCPN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 170 FSGIKFTSNDLeegfEAMR-----ANKRFAVFLG---SDVLMAAGSTIGIDSFIMTSLNFIPEPALELLEFGKGNRDLKI 241
Cdd:cd00951  153 LVGFKDGVGDI----ELMRrivakLGDRLLYLGGlptAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATV 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156551613 242 ARTNQEF------INKTVKaithfGTWVETMKIAMSMtTNLFMGPPRAPLKLISRESVEKMKT 298
Cdd:cd00951  229 KRLLRDFflpyvdIRNRRK-----GYAVSIVKAGARL-VGRDAGPVRPPLTDLTEEELAQLTA 285
PLN02417 PLN02417
dihydrodipicolinate synthase
 10-241 2.18e-08

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 54.26  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  10 GLIVPVFSPFNNDANRSLnlsiiPEYAKFLASKNING---VLVNGTTGEGTSLSTNERKKVTetwAAAVKETKQHLMVqI 86
Cdd:PLN02417   4 RLITAIKTPYLPDGRFDL-----EAYDSLVNMQIENGaegLIVGGTTGEGQLMSWDEHIMLI---GHTVNCFGGKIKV-I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  87 GGTSLNDVKElAAHAEKLGVN-----SLLCLPelYFKPTSVEDLIEYLSIVsksAPNTPLLYYHIPKASMVNIhmgkfLQ 161
Cdd:PLN02417  75 GNTGSNSTRE-AIHATEQGFAvgmhaALHINP--YYGKTSQEGLIKHFETV---LDMGPTIIYNVPGRTGQDI-----PP 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613 162 TVEERI---PTFSGIK-FTSNDLEEGFeamrANKRFAVFLG-----SDVLMAAGStigiDSFIMTSLNFIPEPALELLEF 232
Cdd:PLN02417 144 EVIFKIaqhPNFAGVKeCTGNDRVKQY----TEKGILLWSGnddecHDARWDYGA----DGVISVTSNLVPGLMHKLMFA 215

                        250
                 ....*....|..
gi 156551613 233 GKG---NRDLKI 241
Cdd:PLN02417 216 GKNkelNDKLLP 227
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 44-149 2.44e-05

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: 45.13  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156551613  44 INGVLVNGTTGEGTSLSTNERKKVTETwaaAVKETKQHLMVQIGGTSLN--DVKELAAHAEKLGVNSLLCLPELYFKPTs 121
Cdd:cd00952   43 VDGILTMGTFGECATLTWEEKQAFVAT---VVETVAGRVPVFVGATTLNtrDTIARTRALLDLGADGTMLGRPMWLPLD- 118

                         90       100
                 ....*....|....*....|....*...
gi 156551613 122 VEDLIEYLSIVSKSAPNTPLLYYHIPKA 149
Cdd:cd00952  119 VDTAVQFYRDVAEAVPEMAIAIYANPEA 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH